Pathological Blood Coagulation and the Mycotoxic Oxidative Stress Test

 

Robert Young M.Sc., D.Sc.. Ph.D

Naturopathic Practitioner – The pH Miracle Ti Sana Detox Medical Spa and Universal Medical Imaging Group

Abstract

Historical analysis suggests that conventional understandings of Disseminated Intravascular Coagulation (DIC) may be misguided; further examination may be necessary.  Here, a theoretical analysis provides an alternative explanation for DIC pathology; it is suggested that the cause and mechanics of DIC are largely due to the proliferation of several intravascular microforms and their associated metabolic toxic acidic waste products — Mycrozymian Acidic Toxins (MAT) and Exotoxic-Mycotoxic-Producing Microorganisms (EMPO).  The Mycotoxic Oxidative Stress Test (MOST) is presented here as an easy, inexpensive and non-invasive alternative to conventional measurements for the detection of intravascular  acidic toxins, DIC  and oxidative stress.

Introduction and Historical Perspective

More than 150 years ago, British physician T. W. Jones asked the question, “Why does the blood circulating in the vessels not coagulate?”[1]  though a general answer to this question is now obvious, the biochemical mechanisms involved in how the blood coagulates (clots) are complex and varied, and all the intricacies have not yet been explained. A. Trousseau, recognized that the blood of cancer patients is in a hyper-coagulable state in the process of coagulation, even while confined in the blood vessels.[2]  The name given to this discovery is still in use today, as “Trousseau’s Syndrome.”[2]  Early in his career, Rudolph Virchow, the Father of Pathology, was interested in thrombosis and embolism.  He speculated that intravascular blood could be altered so it would clot as a result of a stimulus too weak to clot normal blood.[3]  In 1856 Virchow delivered a lecture setting forth this concept.

Although the concept of partial clotting within vessels reaches back to the beginnings of modern medicine, much of the discovery of its biochemical mechanisms – the activation of clotting factors – has been left to chance.  The admission of a patient to the hospital with an unceplained bleeding disorder challenged researchers to discover the cause of hemorrhaging.  Analysis of blood from normal persons helped in the study of the patient with the blood disorder. A new clotting factor was hereby discovered which was missing from the  patient’s blood.  For this reason, several clotting factors have been named after the individuals in which they were missing: e.g., Christmas factor (factor IX)[4], Hageman factor (factor XII)[4].

In this article, the causes of pathological (intravascular) clotting will be described, as will various methods of detecting this condition, especially a blood test I call the Mycotoxin Oxidative Stress Test (MOST).

The Mechanics of Blood Coagulation

Blood clotting is a highly detailed chemical-mechanism involving many distinct components.  The problem for the hematologist hs been to understand it at the biochemical level.  Undoubtedly, efforts to fully understand blood clotting will continue for many more years.

Recalling Antione Bechamp’s[8] and Gunther Enderlein’s[9] research into the sub cellular living elements and combining this with what is known of colloidal flocculation[6], it is suggested that the clotting of blood begins with the end-linking (polymerizing) of the fundamental protein unit called by Bechamp the microzyma[8].  A chain of these living units constitutes fibrinogen, which is still dispersed 9micro-hetergenous0 in the blood, and it may or may not be further processed.  If processing continues, it will be either by continued end-linking or by cross-linking.  End-linked fibrinogen is referred to here as fibrin monomer, which I have suggested is a repair protein also dispersed in the blood. Due to a number of blood clotting factors, the process may continue until the excess fibrin monomer and/or until fibrin becomes excessively end-linked.

Cross-linking the polymerized strands to form a three-dimensional network results in what is called the hard clot (fibrin – the major protein of clotting blood).  Factor XIII, which instigates the forming of these blood networks. is always present but latent in the blood, and must be activated before the formation can occur.  Persons who are producing fibrin monomer or excessively linked fibrinogen are said to be in a hyper-coagulable state, while those having diminished  ability to form clots are in a hypo-coagulated state.  It is the activation of the colloidal clotting factors which is so complex.  Blood clotting may occur through many pathways and be initiated by many different stimuli.  Regardless of initiation factors, the process is a sequence of events in which the activation of one factor triggers another, until, after a series of discrete steps, fibrin is formed.

When blood is clotted prematurely, and the factors involved are consumed (incorporated into) the body recognizes a deficiency of clotting agents and generates more.  Thus, people with a tendency to clot excessively will alternate between a hyper coagulable state and a hypo-coagulatable state.  When in the hypo coagulated state, such people hemorrhage until the deficient clotting factors are replaced.[4]  When only fibrin monomer or excessively linked fibrinogen is formed (no cross-linking), it is quite subtle and may go undetected.  It may be detected by a change in blood viscosity (sedimentation rate), by the Mycotoxic Oxidative Stress Test (described later), or by other more subtle means.  If strands of fibrinogen are cross-linked, however, a suggicient amount of insoluble precipitate of fires may result, and these can be detected microscopically using a phase contrast and dark-field microscopy in prepared slides of fresh tissue or blood.  An excessive formation of fibrin leads to  an impairment in circulation, and eventual organ failure usually results.[5]

With this background, we are in a position to consider a standard medical term: disseminated intravascular coagultion (DIC).[6]  This term encompasses the hyper coagulable state, i refer to as pathological blood coagulation which consists of both insoluble and excess dispersed polymers of colloidal proteins.

Key Ingredients of Pathological Blood Coagulation

Before discussing DIC in more detail, it si necessary to introduce its fur important ingredients according to this view – mycotoxins, endotoxins, exotoxins, and tissue factor.  Any of these elements, or any combination of them, can play a major role in initiating unwanted DIC.[6]  However, mycotoxins or the acids from yeast have been found to be the underlying element which instigates and intensifies the participation of the other three.[6]  Each will now be described in turn and brought into the clotting picture.

(Micrograph 1: left, shows normal hyper-coagulated blood in a healthy blood clot sample and right, hypo coagulated blood in an unhealthy blood clot sample)

Mycotoxins and Metabolism by Fermentation

As discussed in the main text of my published book, Sick and Tired book[7 ]. acidification of blood and body tissues and organs and the accompanying lack of oxygen lead to pathological metabolic fermentation, which is carried out primarily by yeast and mold.  Such pathological microorganisms, or their precursors, ar inherent to the human body and to all higher organisms.  Their precursors according to Bechamp, the microzymas, carry on a nominal and homeostatic fermentation themselves. under healthy conditions.[8]  The primary function of yeast and mold is to decompose the body upon the death of the animal or human organism.  Their premature overgrowth indicates a biochemical environment akin to death.  During pathological metabolic fermentation, high concentrations of several acidic substances called mycotoxins are created.  They are highly damaging, always acidic, metabolic products.  If not immediately buffered by specific antioxidants, such as hydrogen peroxide and the hydroxyl free-radical, mycotoxins can seriously disrupt the physiology by disrupting normal metabolism and by penetrating blood and body cells and poisoning them.  As will be seen, they interact with many of the mechanisms for DIC in various pathological symptomologies.

In my published article called The Finger on the Magic of Life: Antoine Bechamp, 19th Century Genius (1816-1908),  I discuss pleomorphism in some detail.[7] Understanding this phenomenon – the rapid evolution of microorganisms across traditional taxonomic  lines is helpful in getting a complete picture of DIC.  Briefly stated, collodial living microzymas evolve intracellularly into more complex forms (microorganisms), beginning with a healthy primitive stage comprising of repair proteins.  As the disease condition worsens, morbid intermediate forms (filterable bacteria or viruses, cell-wall deficient forms and full bacteria) develop from repair proteins, or directly from microzymas.  A third macrostage comprises the commonly recognized culminate microorganisms which are yeast, fungus to mold.  In terms of pleomorphism, all of these microorganisms represent a single family of variously functioning forms.[8]  The culminate forms produce the lions share of acids, which are mycotoxins and the primary focus of my research.[7][8][9]  For convenience, bacteria, yeast, fungus and mold that produce acidic metabolic wastes and protein cellular fragments called exotoins, endotoxins and mycotoxins will here be referred to collectively ash EMPO, or exotoxic, mycotoxic-producing microorganisms.

What follows is a shortened description or the description and origin of several exotoxins and mycotoxins, referred to collectively microzymian acidic toxins of MAT, which are involved in the processes leading to DIC.  The bio-effects, or the pathology of cellular fermentation, of these toxic metabolites are know as mycotic illness, mycotoxicosis, or mycotoxic stress as seen in the MOST and described and published by Dr. Bolin in the 1940’s.[10]

One such metabolic product is acetyl aldehyde, which is formed by  cellular breakdown of food, especially carbohydrate and the birth of  EMPO.  Acetyl aldehyde can also break down into a secondary substance know as ethyl alcohol.  Although acetyl aldehyde presents an immediate hazard to health and well-being, nature has provided a means of buffering of neutralizing this acidic by-product of cellular digestion and fermentation almost as soon as it is created.[11] The controls of acetyl aldehyde (and ethyl alcohol) are the sulfur amino acids, cysteine, taurine, methionine and the peptide glutathione which is found in red blood cells and almost all cells utilizing oxygen.[12]  In an attempt to buffer or neutralize MAT, the body will also bind or chelate both fats and minerals to them.[12]

Another member of the MAT family is uric acid, which is formed by the digestion of protein and the creation of EMPO.[13]  Uric acid can also break down into secondary substance, on of which is alloxan.[14] This has been shown to damage the insulin-producing pancreatic beta cells leading to diabetes [Refer to Tables 1 and 2]

A shortage of alkalizing nutrients or an excess of MAT initi­ates an immune response in which a special class of free radicals which I call microzymian oxidative buffering species (MOBS) are released.[15] These oxygen metabolites carry unpaired electrons and are intended to disrupt bacteria, yeast, fungus and mold, and buffer exotoxins, endotoxins, and mycotoxins. Current medical savants believe that they can disrupt just about any­thing they contact, including healthy cells and tissue: this is not accurate. The fact is that MOBS carriers a nega­tive surface-charge and repel healthy cells, which also have a negative surface-charge. [16] It is the positively surface-charged bacteria, yeast/fungus, mold, exotoxins, endotoxins, and myco­toxins that MOBS bind too.[17]  This aspect gives some insight into autoimmune phenomena, which are not, as is often maintained, the result of an overburdened immune system. They result either as a side-effect of the immune system’s attempt to remove foreign or toxic ele­ments, or as a direct attempt by the immune system to remove cells or tissue rendered useless or disturb­ing to the body by MAT.

In every degenerative symptomatology I have studied, I have found excessive MAT and MOBS (see Tables 1-3). Some of these degenerative symptoms and their underlying disease conditions, including cancer are described in my recently published paper on a deficiency on alkaline nutrition and cancer. [15] But the fact that myco­toxins cause harm to humans and other animals is purely a secondary effect, since, as noted, the prima­ry function of the microorganism is not to cause illness. We know from the fossil record that pleomorphic microforms existed long before animals.[19] In fact, humans and animals developed in terms of micro­organisms.[20] The reverse, however, is not true. Since micro­organisms appeared first in the developmental sequence, they are not physiologically aware of humans and animals. There is much evidence that human and animal physiologies are highly aware of, and respond to MAT – these acidic compounds signaling the presence of bacteria, yeast, fungi and/or mold or  EMPO.[21].

Endotoxins

Also involved in the process leading to DIC are endotoxins, substances endogenous to symptogenic (i.e., “pathogenic” in orthodox terms) bacteria. Endotoxins are a family of related substances having certain common characteristics, but differing from one bacterial form (or strain) to another. Endotoxins are lipopolysaccharides (LPS). LPS form a widely diversified group because of (1) the number of long- chain fatty acids composing lipids; (2) the number of individual sugars as well as their modes of linkage to one another; (3) the branching of sugar chains; and (4) the number of possible arrangements of these units. Endotoxins also contain proteins, further com­pounding the structural diversity.[22]

One theory on endotoxin states that its purpose is to act as a semi-permeable membrane for the bac­terium, limiting and regulating substances entering the organism.[22] Endotoxin resides solely on or near the interior surface of the cell membrane and is shed into the surrounding medium only upon the death of the bacterium. Thus, as these microforms die off, or are lysed by bodily activity, endotoxin is released. (This fact may well be an explanation for the Herxheimer reaction, in which a patient becomes worse following the administration of toxic drugs or other forms of treatment that drastically alter the associated organ­ism.[23]) Another endotoxin theory states that LPS are a constituent of the membrane, and as the organism grows, endotoxin fragments are repeatedly sloughed off into the medium. This phenomenon has been observed in the digestive tract.[24] Since bacterial translocation into the blood is not only possible but common where epithelial hyperpermeability exists, one can assume that the process will continue there. Both theories may be correct if we think of the first one as true of “adult” forms, and the second as true of newly developed and expanding ones.

Basic to the structure of an endotoxin is the lipid common to all forms, designated lipid A, to which is attached a “core” polysaccharide, identical for large groups of bacteria. To the core polysaccharide is attached the O-antigen, consisting of various lengths of polysaccharide chains which are chemically unique for each type of organism and LPS. These chains pro­vide endotoxin specificity.[25] Experiments conducted over many years indicate that most, if not all, of the toxic effects of an endotoxin may be attributed to the lipid portion, and it is sometimes used per se in experiments rather than the entire molecule.[26] An important additional feature of lipid A is its phos­phate content. Each phosphate group carries a nega­tive charge, and since lipid A is a rather large mole­cule, it provides, essentially, a negatively charged sur­face. The importance of this will be seen shortly.

Exotoxins

These are the metabolic excretions of bacteria. While endotoxin’s ongoing effect is, in a manner of speaking, in the background, exotoxins, like myco­toxins, present a double-edged sword. Not only do they initiate DIC, but they produce, or influence the body to produce, the various and numerous infec­tious symptomatologies, such as typhoid fever, diph­theria, etc. (See “Vaccination Reconsidered” in Section 4 of the Appendix of Sick and Tired for details on the action of diphtheria toxin.)[7] By comparison, mycotoxins not only initiate DIC, but there is much evidence to sug­gest that they produce, or influence the body to pro­duce, degenerative symptomatologies, such as arthri­tis, diabetes, etc., and cancer and AIDS as well.

Tissue Factor

Crucial to the understanding of DIC is recogni­tion of the role of tissue factor (TF), formerly known as thromboplastin. This transmembrane lipoprotein exists on the surface of platelets, vas­cular endothelial cells, leukocytes, monocytes, and most cells producing EMPO.[27] It plays a major role in several biochemical mechanisms leading to DIC.

TF is the primary cell-bound initiator of the blood coagulation cascade. Its gene is activated in wound healing and other conditions. By itself it is capable of initiating clotting, but also becomes active when complexed with factor VII or activated factor VII (Vila).[28] TF has been described as the receptor for factor VII because of the close association between the two proteins and because it causes a shape change (conformational) in factor VII, allowing it to attain activity. Both factor Vila and the TF/VII com­plex activate factors IX and X, which initiate the clotting cascade and the formation of thrombin.[29]

Development of Disseminated
Intravascular Coagulation (DIC)

DIC Induced by MAT and Tissue Factor

An infusion of toxins into the blood has a direct effect on TF gene expression in leukocytes. Contact of MAT, endotoxins (lipid A), or exotoxins with leukocytes, activates proteins that bind to DNA nucleotide sequences, thereby activating the TF gene.[30] (See Tables 4-6.)

Endothelial cells damaged in culture by exotoxins, endotoxins, or mycotoxins attract polymorphonuclear leukocytes (PMNs), which adhere to the damaged cells. Once the leukocytes are bound, they can still have their TF gene activated if it hasn’t yet occurred, and they may release MOBS in response to toxins and to organisms of disease, possibly creating further dis­turbances. (Cellular disorganization then releases acti­vating proteins into the blood, which is discussed in more detail later.) Research shows that exotoxic and mycotoxic stress resulting in bound PMNs can be blocked by “antioxidants.”[31] These might better be called anti-exotoxins or antimycotoxins. Both observa­tion and study have led the author to conclude that cellular disorganization is initiated and primarily caused by fermentation pathology, not, as is the cur­rent belief, by the MOBS, or free radicals, generated to destroy toxins and microorganisms. MOBS or free radicals, because of their negative charge, are released to chelate or bind EMPO and MAT. It is suggested by current savants that free radical tissue damage is the secondary, “shotgun” effect of intense immune response to EMPO toxification and MAT-damaged cells. This could not be the case since healthy cells or their membranes carry a negative charge and would resist any electromagnetic attraction because of simi­lar charge. The concentration and instability of MAT generated in a compromised terrain, as opposed to the fleeting existence of free radicals, especially exoge­nous ones, also lead to this conclusion.

Endothelial cells grown in culture can be induced to express tissue factor. In one experiment, no procoagulant activity could be detected in the absence of toxins. However, the addition of mycotoxins from Aspergillus niger or Micrococcus neoformas (Mucor racemosus Fresen) resulted in procoagulant activity which reached a maximum in four to six hours and was dose-dependent. The same experiment was applied using E. coli and Salmonella enteritidis endo­toxin with a similar result.[32] A single intravenous injection of a mycotoxin from Aspergillus niger into experimental animals resulted in circulating endothelial cells within five minutes. In other exper­iments with the mycotoxin, detachment of endothe­lial cells from the basement membrane was noted.[33] (See Table 8.)

Removal of endothelial cells has dire conse­quences from two standpoints: First, the surface of these cells is covered with a specific prostaglandin (PGI2) known as prostacyclin. If blood contacts a surface not covered with PGI2, it will clot. For example, surfaces devoid of this prostaglandin are formed whenever a vessel is cut or punctured. An abrasion or other injury may also expose a surface on which PGI2 is lacking. The removal of endothelial cells by exotoxins or mycotoxins creates a surface devoid of PGI2, leading to blood clotting (see Table 7). Secondly, disorganization of endothelial cells cre­ates increased levels of EMPO and MAT which are attracted to an exposed surface (basement mem­brane) which expresses a negative charge. This also leads to clotting.

DIC Induced by Electrostatic Attraction

It was discovered in 1964 that blood will clot sim­ply from contacting a negatively charged surface.[34] Previously it was believed that the clotting process comprised a cascade of enzyme activity in which one activated the next, etc. The discovery that blood could be clotted simply by contacting a negatively charged surface ruled out the purely enzyme hypoth­esis. Only some of the known clotting factors have been shown to be enzymes.[35] As a result of this sur­prising discovery, detailed research was conducted in an attempt to describe the process. In some experi­ments, the negatively charged surfaces of selected, finely divided, inorganic crystals, including alu­minum oxide, barium sulfate, jeweler’s rouge, quartz, and titanium oxide, were considered.[36]

The clotting factor eventually shown to be activat­ed when whole blood contacted negatively charged surfaces was factor XII, also known as the Hageman factor. This is a positively charged protein migrating in an electric field (electrophoresis) toward the anode.[37] It is believed that factor XII is normally in the shape of a hairpin which binds to the negatively charged sur­face at the bend. Electrostatic attraction forces the two arms to lie flat on the surface, thereby exposing the inner faces and activating the molecule.

It was discovered that if the negatively charged particles were smaller than the clotting factor itself, activation was minimal. Or, if the concentration of clotting factor was too great, there was little or no activation.[38] Both of these observations indicated that the process was one of electrostatic attraction between the negatively charged surface and the clot­ting factor, which is a “basic” protein, that is, posi­tively charged.[39]

Activation of factor XII allows the activation of factor XI, which then activates factor IX. Thus, the blood clotting cascade continues to the formation of fibrin in the normal manner.[40] However, due to a series of activations begun by contact of factor XII with a negatively charged surface, trace amounts of factor Xa also show up in the blood. Factor VII is activated to Vila by factor Xa. Factor Vila then acti­vates factors IX and X, leading to the formation of thrombin. Factor Xa, with co-factor Va, continues the clotting cascade until fibrinogen is activated, leading to fibrin formation.[41] (See Table 5.)

As discussed earlier in terms of prostacyclin, beneath endothelial cells is another surface—the basement membrane. Called the extracellular matrix, it is a thin, continuous net of specialized tis­sue between endothelial cells and the underlying connective tissue. It has four or more main con­stituents, including proteoglycans (protein/polysac- charide).[42] The removal of endothelial cells by’MAT exposes this membrane, which is negatively charged by virtue of its sulfonated polysaccharides in the pro­teoglycans. This brings a reduced negatively charged surface into direct contact with the blood, which activates factor XII and the clotting cascade.[43]The positively charged toxic components of MAT also activate factor XII, as do disturbed disorganized cells, yeast/fungus cells, moldy cells, and the phos­phate groups in the lipid A component of endotoxin. (See Tables 2-5.)

To summarize this section, exotoxic, mycotoxic, and oxidative stress resulting from the overgrowth of bacteria, yeast/fungus, and then mold, has multiple actions, all leading to disseminated intravascular coagulation:

MAT activation of tissue factor gene in leukocytes; subsequent activation of factors VII, IX, and X, resulting in the blood clotting cascade.

MAT activation of tissue factor gene in endothelial cells, again leading to the clotting cascade.

MAT damage to endothelial cells, resulting in neu­trophil attraction, with TF gene activation and generation of MOBS, which, in turn, neutralize MAT, protecting healthy endothelial cells or the basement membrane and supporting the janitorial services of the leukocytes.

Removal of negatively charged endothelial cells by positively charged exotoxins, endotoxins, and mycotoxins, creating a surface devoid of PGI2, also exposes the negatively charged basement membrane, leading to the activation of factor XII and initiation of the clotting cascade. Positively charged components of EMPO, exotoxins and mycotoxins, and several other elements, including the lipid A component of bacterial endotoxin, also activate factor XII and the clotting cascade.

Endothelial Cells as Antithrombotics or Procoagulants

Normal, resting (unstimulated) endothelial cells show antithrombotic activity in several ways: (1) by the inhibition of prostacyclin (platelet adhesion and aggregation); (2) the inhibition of thrombin genera­tion; and (3) the activation of the fibrinolytic system, leading to clot lysis.[45] We will take a brief look at the thrombin aspect.

On the surface of endothelial cells is a protein called thrombomodulin, which acts as a receptor for thrombin. When bound to thrombomodulin, throm­bin can activate protein C. Activated protein C then catalyzes the proteolytic cleavage of factors Va and Vila, thereby destroying their participation in blood clotting. Thus thrombin, which normally activates fib­rinogen, plays an opposite role in this case and inhibits the clotting process.[46,47] (See Table 7.)

On the other side of the coin, the endothelial cell becomes a procoagulant agent when acted on by cer­tain lymphokines, such as interleukin-1. Not only can interleukin-1 induce TF gene expression, but it also suppresses transcription of the thrombomodulin gene in endothelial cells. As in other situations, the lymphokine-activated endothelial cell expresses TF on its surface as a result of TF gene activation. This leads to the production of thrombin and the trigger­ing of the blood clotting cascade.[48] (See Table 5.) Many lymphokines also stimulate adhesion of leuko­cytes to endothelial cells damaged by MAT, resulting in recycling of the cells by MOBS, as described later.

DIC Induced by Intracellular Exotoxic, Mycotoxic, Oxidative Stress by Bacteria, Yeast/Fungus and/or Mold

Any cell which has gone from an oxidative to a fer­mentative state can biochemically cause macrophage production of the lymphokine tumor necrosis factor (TNF). This protein has been shown to activate the gene for TF in fermenting cells, which are so behaved due to morbid evolution of bacteria, yeast/fungus, and then mold.[49,50] In the author’s view, a cell having been switched entirely to fermentation metabolism as a result of a physical or emotional disturbance of that cell, is what constitutes cancer (see Tables 5 and 13). (One might argue that this definition does not fit all “forms” of cancer, such as leukemia, for example. This is because leukemia is not cancer, but an immune response to the rise in EMPO and MAT in the body, and a relatively easy compensation to correct.)

The surface of many disorganizing or fermented cells (cancer cells) is characterized by small projec­tions in the plasma membrane which pinch off, becoming free vesicles containing toxins as well as TF complexed with factor VII. These vesicles can aggre­gate and/or lodge anywhere, ultimately releasing their contents. Also, the presence of excessive amounts of TF/factor VII complexes on the surface of fermented cells allows the formation of a fibrin net around the cell and around the entire mass of cells (tumor). This seems to be an attempt by the body to encapsulate and contain the mass. However, fermented cells do escape from the primary fibrin net, perhaps due to some electromagnetic effect, and become free-float­ing in the circulation. They may thus lodge elsewhere and instigate the fermentation of other cells by fungal penetration or by poisoning them and provoking a morbid evolution of their inherent microzymas.

Because of the surrounding fibrin net, these mobi­lized fermenting cells are protected from collection by the immune system while in transit.[51,52] (See Table 4.) The blockage or dissolution of fibrin net forma­tion by an anticoagulant such as heparin allows freed, fermenting (metastasizing) cells to be dismantled by natural killer cells and other immune cells (see Tables 5, 12 and 13).

DIC Induced by MAT/EMPO and Immune System Response (Release of MOBS)

Unsaturated fatty acids are highly susceptible to EMPO as well as MAT. Linoleic acid, a long-chain fatty acid present in white cells, has 18 carbons and 2 unsaturations. Subjected to MAT, linoleic acid binds the exotoxin, endotoxin, or mycotoxin, there­by forming an epoxide at the first unsaturation.[53] Research has revealed that this compound, named leukotoxin, is highly disturbing to other cells. It caus­es platelet lysis, thereby releasing TF and initiating DIC.[54] (See Table 10.) The fact that MAT result in fermented fats lends further credence to the sugges­tion that the initial and primary degenerative damage to structures and substances in the body is caused by exotoxins and/or mycotoxins, and that damage by MOBS, or by other free radicals, is not possible.

Another mechanism leading to DIC is the release of a special glycoprotein, sialic acid, from the terminal ends of cell-membrane polysaccharides, where it is always found. Polysaccharides play a highly significant role in biochemical processes, with both enzymes and membrane receptors recognizing various groupings of specific sugars linked in highly specific ways.

Immediately preceding the release of sialic acid in the polysaccharide chain is the sugar galactose. The sialic acid/galactose arrangement is utilized as a biolog­ical indicator of cellular and molecular aging. As cells age, sialic acid is naturally expressed from the terminal ends of polysaccharides, thereby exposing galactose. A membrane-bound enzyme from the liver, galactose oxi­dase, recognizes galactose and eventually disorganizes it, disrupting cell function integrity and hastening demise. Aged red blood cells, which have expressed a significant amount of sialic acid, are removed from the blood by this process. (I theorize that the biological ter­rain may be at work in normal cell aging. That is, the rate at which sialic acid is expressed is determined by the levels of corrosive acids in the system and the body’s ability to remove them, although there are no doubt intracellular factors at work as well.)

I suggest from my years of  clinical research  that cellular breakdown is compounded by the fermentation of the galactose by the microzyma. This is a process that begins from within and not necessarily from without. Not only does this action create more sialic acid, it creates other toxic waste products such as acetic aldehyde, alcohol, uric acid, oxalic acid, etc. The increase in cellular disturbances and fermenta­tion of the galactose creates biochemical signals for more galactose oxidase. This leads to greater cellular disorganization and developmental morbidity, espe­cially in the red blood cells, and a rise in the level of detrital serum proteins, which encourages clotting. From this perspective, diabetes, arthritis, atheroscle­rosis and other symptomatologies become more clearly “degenerative” (see Tables 2-5, 12 and 13).

Fibrinogen is a rather elaborate protein having the structure of three beads on a string. Expressed on the end beads is sialic acid, which indicates the beginning of disorganization of the fibrinogen and a declining negative charge to the positive. Prior to the declining charge and the expression of sialic acid on the end beads, fibrinogen, which is negatively charged, will not polymerize the healthy blood due to mutual repulsion. However, fibrinogen will poly­merize to damaged cells, EMPO, MAT and other positively charged areas of the body for repair pur­poses. Thus, as more and more sialic acid is expressed, there will be a significant reduction in the charge of the fibrinogen, acting as the primary requirement for the polymerization of fibrinogen (hypercoagulable state). The resulting polymer, fib­rin monomer, is the protein chain used in the repair of cells and clotting of blood.[55] End-linking will take place after the release of sialic acid (positive charge) by whatever means.

With this background, it is interesting to note that blood taken from persons suffering from anxiety is expressing sialic acid from fibrinogen, and is halfway toward clotting. Hormones released during anxiety states are easily fermented, giving more momentum to MAT and thereby resulting in this important change in fibrinogen. It leads to a clotting pattern characteristic of anxiety stress, and is readily identi­fied in the MOST. As can be seen in this picture, the pattern is a “snowstorm” of protein polymeriza­tions measuring from 2 to 10 microns.

 

 

 

 

 

 

 

[Micrograph 2: An Anxiety Profile showing a ‘snowstorm’ of 2 to 10 micron protein polymerizations starting from the center of the clot and moving out towards the edge]

As mentioned earlier, despite the attempt by the body to neutralize EMPO and MAT, an excess will initiate the release of MOBS by immune cells. A major MOBS is superoxide, designated chemically as O ₂. It may exist alone or be attached to another ele­ment, such as potassium (KO’₂) or sulfur (SO). Again, however, nature has provided a means of pro­tecting healthy cells—their negative charge[1]. Another protection against superoxide is the enzyme superox­ide dismutase (SOD), also found in all healthy cells.

A second member of the MOBS family is hydro­gen peroxide (H₂0₂). This molecule is very unstable and tends to react rapidly with other biological mol­ecules, damaging them. The release of hydrogen per­oxide in the body is a response to the overgrowth of decompositional organisms in a declining pH (com­promised biological terrain). The control for healthy cells against hydrogen peroxide is their negative charge and the protective enzyme catalase, one of the most efficient enzymes known.

When leukocytes and other white blood cells are stimulated by the presence of bacteria, yeast/fungus and mold, they treat these organisms as foreign par­ticles to be eliminated. During and prior to phagocy­tosis, the foregoing oxidative cytotoxins, along with the hydroxyl radical (OH’), are generated and released specifically for neutralizing microforms or harmful substances. This release is referred to as an “oxidative burst.” As a result of fermentation and the production of exotoxins and mycotoxins that fer­ment galactose from cells, the immune system is activated. An oxidative burst is released to neutralize the morbid microforms and mycotoxicity.[56] Like other biological processes faced with constantly alarming situations, the continued release of MOBS can get out of control. This may damage endothelial cells, the basement membrane, or other body ele­ments, and this activates fibrinogen to fibrin monomer (repair protein), leading to DIC [see Table 9]. Interestingly, the white blood cells capable of neutralizing MAT through MOBS production are the same ones capable of phagocytosis, the process by which foreign matter, waste products and microor­ganisms are collected and dumped in the liver.[57]

To summarize this section, pathological microforms and their acids create DIC by a number of pathways:

Leukotoxin (linoleic acid bound to mycotoxin) is highly toxic to cells. It causes platelet lysis, there­by releasing TF and initiating DIC.

The expression or release of sialic acid residues from healthy cells that have been disturbed allows for the fermentation of galactose, creating exotox­ins and mycotoxins, biochemically activating galactose oxidase, which further disturbs and dis­organizes healthy cells. This cycle loads the blood with debris.

EMPO and MAT disturb fibrinogen, which releas­es sialic acid and reduces the charge, allowing it to polymerize into fibrin monomer and fibrin nets.

The presence of exotoxins, endotoxins, and myco­toxins and their poisoning of cells activates the immune system. White blood cells generate MOBS (e.g., superoxide [0′₂] or hydrogen perox­ide [H₂0₂]). These substances bind to and neu­tralize EMPO and MAT. MOBS are repelled by healthy endothelial cells and the basement mem­brane because of their negative charge. Cellular disturbances and disorganization stimulate the generation of fibrin monomer for repair purposes, leading to DIC.

Detection of Disseminated Intravascular Coagulation

The Sonodot Analyzer

The Sonoclot Coagulation Analyzer provides a reaction-rate record of fibrin and clot formation with platelet interaction. An axially vibrating probe is immersed to a controlled depth in a 0.4 ml sample of blood. The viscous drag imposed upon the probe by the fluid is sensed by the transducer. The electronic circuitry quantifies the drag as a change in electrical output. The signal is transmitted to a chart recorder which provides a representation of the entire clot for­mation, clot contraction and clot lysis processes. The analyzer is extremely sensitive to minute changes in visco-elasticity and records fibrin formation at a very early stage. The Sonoclot has been evaluated scientif­ically and shown to provide an accurate measurement of the clotting process.[58,59]

One application of the Analyzer has been the development of a test to distinguish non-advanced breast cancer from tumors that are benign. The ratio­nale for the test is the hypercoagulable state seen in cancer patients (Trousseau’s Syndrome), resulting from the generation of TF by leukocytes (mono­cytes).[60] (See Table 4.)

Fibrin Degradation
Products and Fibrin Monomer

DIC can be seen as a two-step process. First, fib­rinogen, which is always present in the blood, is acti­vated by any of several mechanisms. This activation leads to an automatic polymerization (chain forma­tion) resulting in fibrin monomer. This is not apparent in a microscope unless the blood is allowed to clot, as in the MOST.[61,62] The second step is the precipitation or deposition of fibrin (hard clot) by several other mechanisms. One of these is the formation of cross­links through the action of factor XIII. Another such mechanism may be poor circulation in an organ already blocked by deposited fibrin. The deposition of precipitated fibrin may be detected microscopically in tissue sections and diagnosed as DIC.[62]

Because fibrin monomer is not readily detected, a chemical test for it is of immense value in diagnosing DIC. Research has indicated that its detection may be very useful in the early diagnosis of DIC and MAT.[63] There are three fundamental physiologic areas related to blood clotting: (1) the prevention of blood clotting, (2) the clotting of blood, and (3) the removal of clotted blood once it has formed.

Enzymes are present that are capable of removing (lysing) clotted blood, one of which is plasmin. Another enzyme, plasminogen, is always present in the blood, but is inactive as a proteolytic agent. Plasminogen acti­vator converts plasminogen to plasmin, which can degrade deposited fibrin. This process is not specific for fibrin, however, and other proteins may be affected. When fibrin is degraded (fibrinolysis), fibrin monomer, as well as several other products, are formed. Commercial kits are available for the analysis of fibrin degradation. This test is an indirect measure of the pres­ence of DIC and MAT.[64]

Other tests include:

Protamine Sulfate: Protamine sulfate is a heparin binder sometimes used in surgery for excessive bleed­ing. The test, which indicates fibrin strands and fibrin degradation products, is conducted in a test tube, with fibrin monomer and fibrin forming early and polymer­ization of fibrin degradation products occurring later.[65] Ethanol Gelation: A white precipitate is formed by the addition of ethanol to a solution in a test tube containing fibrin monomer as a degradation product of fibrin, indicating DIC and MAT.[66]

The Mycotoxic Oxidative Stress Test (MOST)

Up to now, blood chemistries have been the prima­ry mode of diagnosis or analysis for the presence of pathology. In the view presented here, the bright-field microscope, is used to easily and inexpensively reveal a disease state as reflected by changes in certain aspects of blood composition and clotting ability. DIC is char­acterized by the abnormal presence in the blood of fib­rin monomer. When allowed to clot, blood containing such an abnormal artifact will exhibit distortions of normal patterns. The presence in the blood of soluble fragments of the extracellular matrix and soluble fibronectin, as well as other factors, will also create abnormal blood clotting patterns as described below.

A small amount of blood from a fingertip is con­tacted with a microscope slide. A series of drops is allowed to dry and clot in a normal manner. Under the compound microscope, the pattern seen in healthy subjects is essentially the same—a dense mat of red areas interconnected by dark, irregular lines, completely filling the area of the drop. The blood of people under mycotoxic/oxidative stress exhibits a variety of characteristic patterns which deviate from nor­mal, but with one striking, common abnormality: “clear” or white areas, in which the fibrin net/red blood cell conglomerate is missing.

 

 

 

 

 

 

 

 

[Micrograph 3; An abnormal clot with striking ‘clear’ or white areas or protein polymerization as seen in the hyper coagulated blood of a patient with lower bowel imbalances]

Why the fibrin net is missing may be understood from the following: Two peptides—A and B—in the central protein bead of the fibrinogen structure become bound in the cross-linking process. There are two ways this can be configured: (1) Thrombin is capable of activating peptides A and B, resulting in the formation of a polymer loosely held together only by hydrogen bonds; (2) With peptides A and B acti­vated normally, the resulting hard clot is insoluble, indicating that the peptides are linked by covalent bonds. The difference in bonds results from factor XIII, an enzyme which links the two fibrin strands with a glutamine-lysine peptide bond.

Additional research has shown that the release of sialic acid from fibrinogen inhibits the action of factor XIII, resulting in a soft, white clot. In addition, acetic aldehyde has been shown to inactivate factor XIII directly. The soft clotting, compounded by other polymeric aggregations (described below), results in clear areas in the dry specimens. In the opposite extreme, high serum levels of calcium, for the pur­pose of neutralizing MAT, activates factor XIII, lead­ing to excessive cross-linking of fibrin to form a clot harder than normal. This is reflected in the MOST pattern characteristic of definite hypercalcemia— that of a series of cracks in the clot radiating outward from the center, resembling the spokes of a wheel. High serum calcium is the body’s attempt to com­pensate for the acidity of mycotoxic stress by pulling this alkalizing mineral from bone into the blood. This demand creates endocrine stress in turn, because reabsorption of bone is mediated by parathormone (PTH). Therefore, this clotting pattern indicates cal­cium deficiency and thyroid/parathyroid imbalance.

 

 

 

 

 

 

 

[Micrograph 4: A mineral deficiency or more specifically a calcium deficiency pattern associated with an imbalance of they thyroid and/or parathyroid}

Advanced research has shown that there are seven carbohydrate chains in fibrinogen (each terminated by sialic acid). A second action of factor XIII is to ferment a large amount of carbohydrate during clot­ting. Because carbohydrate is most often water solu­ble, the loss of this material undoubtedly adds to the insolubility of a clot, while pathological retention contributes to the softness of the abnormal clot.

Clinical experience demonstrates that the MOST is a reliable indicator of exotoxic and mycotoxic stress and, concurrently, of various disorganizing symptoma­tologies associated with fermentative and oxidative processes. As various cellular degradation occurs, the blood-borne phenomena which accompany such symptoms as diabetes, arthritis, heart attack, stroke, atherosclerosis and cancer show up in the MOST, often with sialic acid beads in the clear areas of poly­merized proteins. (Determination of the liberation of sialic acid from carbohydrate has been approved by the U.S. Food and Drug Administration as an accept­ed indicator for cancer, and is clinically available.)

[Micrograph 5: Sialic acid beads are seen inside the protein
polymerization of the hypocoagulated blood as black dots]

The extent and shape of the clear areas are reflec­tive of particular symptomatologies which have arisen from the way in which the disease condition manifests in a given individual. This observation is borne out by having the patient undergo appropriate alkalizing therapy. With success of treatment based on the patient’s freedom from symptoms, sense of well-being, and live blood exams discussed in the main text of Sick and Tired, Reclaim Your Inner Terrain, Appendix C,[7] repeated analysis with the MOST reveals a progressively improving clotting pattern.

[Micrographs 6 and 7: Medically diagnosed cancer patient with large polymerized protein pools (PPP) in the hypo-coagulated blood above. In the picture below PPP’s have significantly reduced in size and the blood is moving to a more hyper-coagulated state as a result of reducing acid loads with an alkaline lifestyle and diet (7, 70)]

Because of its very nature, the MOST is emi­nently suited to reveal and measure the presence in the blood of abnormal substances, clotting factors, and disorganization of cells due to an inverted way of living, eating, and thinking, which gives rise to MAT. The MOST indicates both the direct and indirect activity of MAT on blood clotting, endothelium, and the extracellular matrix (described next), as well as on biochemical pathways, including hormonal ones. The generation of excessive MOBS in response to EMPO and MAT, the inability that accompanies all degenerative symptoms to neutralize or eradicate EMPO and MAT, and the recognized hyper- and hypocoagulable states seen in various symptomatolo­gies, will beyond doubt be revealed in the MOST.

 

 

 

 

 

[Micrograph 8 and 9: Medically Diagnosed HIV/AIDS micrograph showing above an Aspergullus niger mold crystal using dark field microscopy and below a hypocoagulated blood clot with systemic protein polymerizations measuring in excess of 40 microns using bright field microscopy}

 

 

 

 

 

 

As mentioned, hormones are easily fermented, and this will show up as a hypocoagulated blood pattern in the MOST. It is my opinion, this hypocoagulated blood appears in the MOST as misty clouds of protein polymerizations throughout the clot, as seen in the accompanying picture.

[Micrograph 10: Poor fibrin interconnection in the clot associated with endocrine or hormonal imbalance]

The MOST from Solubilized Extracellular Matrix

There is now a clearer picture of the biochemical rationale for correlating abnormal blood clotting patterns with the presence of degenerative symptoms.  A link between symptoms and the distorted clotted blood patterns has been delineated in the MOST.
Another reason for the abnormal clotting patterns accompanying pathological states, in addition to insufficient bonding of fibrinogen peptides as seen in the MOST, is presence in the blood of water-soluble fragments of the extracellular matrix.

Extracellular Matrix Degradation by MAT

The extracellular matrix (EM) is a three-dimen­sional gel, binding cells together and composed of five or more major constituents: collagen (protein), hyaluronic acid (polysaccharide), proteoglycans (pro- tein/polysaccharide), fibronectin and laminin. Also included are glycosaminoglycans and elastin.[67] In every degenerative disease studied by this author, evidence has been found for MAT activity destruc­tive of EM.

One of the proteolytic enzymes activated in response to EMPO and MAT is alpha-1 antitrypsin (capable of neutralizing MAT), normally not active in the presence of the enzyme trypsin. The active por­tion of this anti-exotoxin and antimycotoxin contains the amino acid methionine, which includes a C-S-C linkage. When chelated by the hydroxyl radical (one of the MOBS oxidants), methionine’s central sulfur atom acquires one or two oxygen atoms (forming the sulfone or sulfoxide respectively). The fermentation of methionine is a secondary effect of immune response to an alarming situation, intended to neutral­ize MAT and prevent degradation of the EM. Once alpha-1 antitrypsin is exhausted, MAT will have more access to the EM. If the EM is damaged beyond repair, then the enzyme trypsin is released to disorganize and recycle the cells involved.[68]

A similar scenario holds for the enzymes collage- nase and elastase. Thus, the absence of alpha-1 antitrypsin in the presence of EMPO and MAT activates three enzymes which degrade the extracellular matrix. Degradation of the EM by enzymes and MAT puts into the blood the water-soluble fragments (proteins and glycoproteins) of normally insoluble EM components (see Table 11). The presence of these fragments modifies the normal clotting pattern (described below), as seen in the M/OST, and is therefore an indication of EM degradation, which is always found with degenerative symptoms. (Also present is fibrin monomer, which has been found in the blood of patients suffering from collagen dis­ease.[69] See Table 11.)

Fibronectin is a molecule in EM having several binding sites for various long-chain molecules— heparin (a sulfonated polysaccharide) and collagen, for example. As such, it functions as a cellular glue, bind­ing cells together as well as various components of the EM. A soluble form of fibronectin is normally found free in the blood, and enters into the formation of a blood clot through the action of factor XIII. This form of fibronectin binds to fibrin. Elevated, bound-serum fibronectin results from EM fragmentation by MAT, and accompanies degenerative symptoms such as arthritis and emphysema (collagen diseases).

Water-soluble fragments of the EM bound by fibronectin form a three-dimensional network or gel in the pathologically clotted blood (fibrin and com­ponents of the blood clotting cascade). Since fibronectin binds to both fibrin and collagen, the two polymeric networks are superimposed and intermin­gled, resulting in a modification of the normal clot­ting pattern. Exactly how the pattern is modified depends upon the nature of the collagen abnormally present, the nature and extent of hyaluronate pre­sent, and the degree to which EM fibronectin has been released by MAT.

Conclusion

Thus, it is easily seen that there are many forms which the pattern of clotted blood may take, depending on the individual and the internal terrain that produced the modifying substances. The MOST reveals not only the presence of exotoxic and mycotoxic stress, but indicates as well the nature of the symptom(s) resulting from the stress (see Table 12). Since MAT underlie the entire complex of events which degrade the extracellular matrix, I must conclude that the absence of these exotoxins, endotoxins and mycotoxins would provide substantial improvements in tissue integrity and the overall physiology and functionality of the organism or animal and human.

­

­

References

[1]  Jones, T.W., “Observations on some points in the anatomy, physiology and pathology of the blood.”  British Foreign Medical Review, 1842. 14 : 585.

[2] Trousseau, A., Phlegmasis alba delens. “Clinque Medicale de L’Hotel Dieu de Paris.”, 1865, 3:94

[3]  Virchow, R., “Hypercoagulability: A review of its development, clinical application, and recent progress.”  Gesammelte Abhandlungen our Wussenschaftlichen Medizin, 1856, 26:477.

[4]  Rapaport, S.I., “Blood Coagulation and its Alterations in Hemorrhagic, and Thrombotic Disorders.”  The Western Journal of Medicine, 1993; 158: 153.

[5]  Hamilton, P.J. et al., “Disseminatied Intravascular Coagulation: A Review.”  Journal of Clinical Pathology, 1978, 31: 609

[6] The Harper Collins Illustrated Medical Dictionary, 1994, p.13.

[7] Young, RO, “Sick and Tired, Reclaim Your Inner Terraine,” Woodland Publishing, 1999.

[8] BeChamp, A., “The Blood and Its Third Anatomical Element,”  Hikari Omni Publishing, 1999.

[9]  Schwerdtle, C, Arnoul, F, Enerlein, G, “Introduction to Darkfield Diagnostics”, Semmelweis-Verlag (2006).

[10]  Hawk, BO, Thoma, GE, Inkley, JJ, The Evaluation of the Bolen Test as a Screening Test for Malignancy*, cancerres.aacrjournals.org on December 5, 2015. © 1951 American Association for Cancer Research.

[11]  Uchida, K., “Role of Reactive Aldehyde in Cardiovascular Diseases”,  Labortory of Food and Biodynamics, Nagoya University Graduate School of Bioagricultural Sciences, Nagoya, Japan , Free Radical Biology and Medicine, Volume 28, Issue 12, 15 June 2000, Pages 1685–1696

 [12] Chang JC, van der Hoeven LH, Haddox CH, “Glutathione reductase in the red blood cells”,  Ann Clin Lab Sci. 1978 Jan-Feb;8(1):23-9.

[13] Kutzing, MK, Firestein, BL, “Altered Uric Acid Levels and Disease States”, Department of Cell Biology and Neuroscience (M.K.K., B.L.F.), Graduate Program in Biomedical Engineering (M.K.K.), Rutgers University, Piscataway, New Jersey. Address correspondence to: Dr. Bonnie L. Firestein, Department of Cell Biology and Neuroscience, Rutgers University, Piscataway, NJ 08854-8082. E-mail: firestein@biology.rutgers.edu

[14] Claudino, M,. Ceolin,,DS, Alberti, S.,  Cestari, TM,  Spadella, CT, Fischer Rubira-Bullen, IR, Gustavo Pompermaier Garlet, Gerson Francisco de Assis, ” Alloxan-Induced Diabetes Triggers the Development of Periodontal Disease in Rats”,  Published: December 19, 2007. DOI: 10.1371/journal.pone.0001320

[15] Young RO (2015), “Alkalizing Nutritional Therapy in the Prevention and Reversal of any Cancerous Condition. Int J Complement Alt Med 2(1): 00046. DOI: 10.15406/ijcam.2015.02.00046

[16] Heloise Pöckel Fernandes, Carlos Lenz Cesar, and  Maria de Lourdes Barjas-Castro, “Electrical properties of the red blood cell membrane and immunohematological investigation”, Rev Bras Hematol Hemoter. 2011; 33(4): 297–301. doi:  10.5581/1516-8484.20110080 PMCID: PMC3415751

[17] Harris, JO, “The Relationship Between the Surface Charge and the Absorption of Acid Dyes by Bacterial Cells”, Department of Bacteriology, Kansas Agricultural Experiment Station, Manhattan,Kansas, Received for publication March 3, 195.

[18] Young, RO, “Metabolic and Dietary Acids are the Fuel That Lights the Fuse that Ignites Inflammation that Leads to Cancer”. https://www.linkedin.com/pulse/metabolic-dietary-acids-fuse-ignites-inflammation-causes-young. 2015.

[19] Snaders, R, “Did Bacteria Spark Evolution of Multicellular Life?” Berkeley News, Research, Science and Environment,  October 24, 2012.

[20] Wenner, M, “Humans Carry More Bacterial Cells than Human Ones”. Scientific American, November 30th, 2007.

[21} Animals and humans respond to MAT as a poison.

[22]  Morrison, D.C. et al. The effects of bacterial endotox­ins on host mediation systems. American Journal of Pathology, 1978; 93: 526.

[23]  Ibid.

[24]  Ibid.

[25]  Van Deventer, S.J.H. et al. Intestinal Endotoxemia. Gastroenterology, 1988; 94(3): 825-831.

[26]  Morrison, D.C. et al., op. cit.

[27]  Ibid.

[28]  Hu, T. et al. Synthesis of tissue factor messenger RNA and procoagulant activity in breast cancer cells in response to serum stimulation. Thrombosis Research, 1993; 72: 155.

[29]  Rapaport, op. cit. (Ref. 4).

[30]  Ibid.

[31]  Mackman et al. Lipopolysaccharides—mediated tran­scriptional activation of the human tissue factor gene in THP-1 monocytic cells requires both activator protein 1 and nuclear factor kappa B binding sites. Journal of Experimental Medicine, 1991; 174: 1517.

[32]  Yamada, O. et al. Deleterious effects of endotoxins on cultured endothelial cells: An in vitro model of vascular injury. Inflammation, 1981; 5: 115.

[33]  Colucci, M. et al. Cultured human endothelial cells: An in vitro model of vascular injury. Journal of Clinical Investigation, 1983; 71: 1893.

[34]  Cho, T.H. et al. Effects of Escherichia coli toxin on structure and permeability of myocardial capillaries.

[35]  Acta Pathologica Japonica, 1991; 41: 12.

[36]  Rapaport, op. cit. (Ref. 4).

[37]  Ibid.

[38]  Margolis, J. The interrelationship of coagulation of plasma and release of peptides. Annals of the New York Academy of Sciences, 1963; 104: 133.

[39]  23-25. Ibid.

[40]  Morrison, D.C. et al., op. cit.

[41]  Rapaport, op. cit. (Ref. 4).

[42]  Alberts, B. et al, eds. Molecular Biology of the Cell. New York: Garland Publishing, Inc., 1989 (2nd ed.), p. 818.

[43]  Rapaport, op. cit. (Ref. 4).

[44] Bertz, A., et al. Modulation by cytokines of leukocyte endothelial cell interactions. Implications for thrombo­sis. Biorheology, 1990; 27: 455.

[45]  Rapaport, op. cit. (Ref. 4).

[46]  Nachman, R.L. et al. Hypercoagulable states. Annab of Internal Medicine, 1993; 119: 819.

[47]  Ibid.

[48]  Tallman, M.S., et al. New insights into the pathogene­sis of coagulation dysfunction in acute promyelocytic leukemia. Leukemia and Lymphoma, 1993; IT. 27.

[49]  Silberberg, J.M., et al. Identification of tissue factor in two human pancreatic cancer cell lines. Cancer Research, 1989; 49: 5443.

[50]  Grimstad, I.A. et al. Thromboplastin release, but not content, correlates with spontaneous metastasis of can­cer cells. International Journal of Cancer, 1988; 41: 427.

[51]  Gunji, Y. et al. Role of fibrin coagulation in protection of murine tumor cells from destruction by cytotoxic cells. Cancer Research, 1988; 48: 5216.

[52]  Sugiyama, S. et al. The role of leukotoxin (9, 10- epoxy-12-octadecenoate) in the genesis of coagulation abnormalities. Life Sciences, 1988; 43: 221.

[53]  Ibid.

[54]  White, A. et al, eds. Principles of Biochemistry. McGraw-Hill Book Co., New York, 1964, p. 648.

[55]  Mueller, H.E. et al. Increase of microbial neu­raminidase activity by the hydrogen peroxide concen­tration. Experientia, 1972; 23: 397.

[56]  Young, Robert O. Fermentology and oxidology. The study of fungus-produced mycotoxic species and the activation of the immune system and release of microzymian oxidative buffering species (MOBS). Self- published: InnerLight Biological Research Foundation, Alpine, Utah, 1994.

[57]Chandler, WL. et al. Evaluation of a new dynamic vis­cometer for measuring the viscosity of whole blood and plasma. Clinical Chemistry, 1986; 32: 505.

[58]  Saleem, A. et al. Viscoelastic measurement of clot for­mation: A new test of platelet function. Annals of Clinical and Laboratory Science, 1983; 13: 115.

[59]  Spillert, C.R. et al. Altered coagulability: An aid toselective breast biopsy. Journal of the National Medical Association, 1993; 85: 273.

[60]  Bowie, E.J. et al. The clinical pathology of intravascular coagulation. Bibliotheca Haematologica, 1983; 49: 217.

[61]  Muller-Berghaus, G. et al. The role of granulocytes in the activation of intravascular coagulation and the pre­cipitation of soluble fibrin by endotoxin. Blood, 1975; 45: 631.

[62]  Bick, R.L. Disseminated intravascular coagulation. Hematology/Oncology Clinics of North America, 1993; 6: 1259.

[63]  Bredbacka, S. et al. Laboratory methods for detecting disseminated intravascular coagulation (DIC): New aspects. Acta Anaesthesiologica Scandinavica, 1993; 37: 125.

[64]  Sigma Diagnostics, St. Louis, MO 63178; tel: 314- 771-5765.

[65]  Nachman, R.L. et al. Detection of intravascular coag­ulation by a serial-dilution protamine sulfate test. Annals of Internal Medicine, 1971; 75: 895.

[66]  Breen, F.A. et al. Ethanol gelation: A rapid screening test for intravascular coagulation. Annals of Internal Medicine, 1970; 69: 1197.

[67] Hay, E.D., ed. Cell Biology of Extracellular Matrix. New York: Plenum Press, 1981, p. 653.

[68]  Carp, H. et al. In vitro suppression of serum elastase- inhibitory capacity by ROTS generated by phagocytos- ing polymorphonuclear leukocytes. Journal of Clinical Investigation, 1979; 63: 793.

[69]  Wilson, C.L. The alternatively spliced V region con­tributes to the differential incorporation of plasma and cellular fibronectins into fibrin clots. Journal of Cell Biology, 1992; 119: 923.

[70] Young, RO, Young, SR, “The pH Miracle Revised and Updated”, Hachette Publishing, 2010.

Tables

Table 1

Expression of Sialic Acid/Galactose [MAT] from Cell and Protein Degeneration (From All Serum Proteins, RBC/WBC and Other Cell Surfaces)

1.  Carbohydrate, Proteins, and Fats From Diet, Body Cells or Reserves
2. As cells breakdown or ferment they give birth to bacteria, yeast, fungus and mold [EMPO] and their associated metabolic acidic waste [MAT]
3. Exotoxins, Endotoxins, and Mycotoxins [MAT]
4. Acetyl Aldehyde, Ethyl Alcohol, Uric Acid, Alloxan, Lactic Acid are examples of MAT
5. MAT  Ferments Other Body Cells and their Extracellular Membranes and Proteins
6. MAT Modifies Glycoprotein
7. Binds to liver Galactosidase
8. Creating an Increase in Cell and Protein Fermentation and Degeneration and Increased Amounts of Exotoxins, Endotoxins and Mycotoxins [MAT]

Table 2

Expression of Sialic Acid [MAT] From the Fermentation of Degeneration of Insulin Producing Pancreatic Beta-Cells in Type I, Type II and Type III Diabetes

1. Pancreatic Insulin producing Beta-Cells with no or minimal Surface Sialic Acid [MAT]A Physical and/or Emotional Disturbance Occurs from Lifestyle and/or Diet
2. Normal regulation of Insulin Production
3. A Physical and/or Emotional Disturbance Occurs from Lifestyle and/or Dietary choicesdd
4. Leads to cellular fermentation and degeneration and the birth of EMPO
5. This lead to increased abnormal amounts of MAT that the immune system, the alkaline buffering system and the elimination organs has to deal with
6. Fermenting and degenerating Insulin Producing Beta Cells
7. Giving Rise to Surface Cell Sialic Acid [MAT}
8. Increased Amounts of Sialic Acid Activates the Immune Response [MOBS] and Sialidase [AB]
9. Leads to Lowered or No Insulin Production
10. Symptoms of Type I, Type II or Type III Expressed
11. The insulin producing beta cells of the Islets of Langerhans express silica acid on their surface as a break down metabolite.  I have suggested that when insulin producing beta cells are physically disturbed by MAT they begin to disorganize and express sialic acid on the surface of the cell.  This indicates the death of the cell and insulin production will stop.

Table 3

HIGH BLOOD PRESSURE, ATHEROSCLEROSIS, HEART ATTACKS, STROKES, and CONGESTIVE HEART FAILURE

1. A Physical and/or Emotional Disturbance Occurs from Lifestyle and/or Dietary choices
2. Leads to cellular fermentation and degeneration and the birth of EMPO
3. This lead to increased abnormal amounts of MAT that activates the immune system to chelate the MAT.
4. Increased amounts of MAT will cause endothelial breakdown and the expression of Sialic acid.
5. Increased Amounts of Sialic Acid and damage to the endothelial will cause a reduction in the negative surface-charge leading to the release of Glycoproteins.
6. The release of Glycoproteins will cause the activation of Factor XII and the blood clotting cascade.
7. This cause the creation and formation of fibrin monomers and the increase of Platelet Deposition out of the red blood cells for clotting purposes
8. The immune system will activate and MOBS will be released as well as sodium bicarbonate, calcium, lipids and other alkaline buffers to reduce metabolic acidity.
9. The build-up of fibrin monomers in the clotting cascade will lead to fibrin nets and clots causing an increase in blood pressure and the risk of blockages potentially causing a Stroke or Heart Attack.

Table 4

DISSEMINATED INTRAVASCULAR COAGULATION RESULTING
FROM INTRACELLULAR DISORGANIZATION OR FERMENTATION WHICH GIVES RISE TO MAT AND EMPO

1. A Physical and/or Emotional Disturbance Occurs from Lifestyle and/or Dietary choices
2. Leads to cellular fermentation and degeneration and the birth of EMPO
3. This lead to increased abnormal amounts of MAT that activates the Tumor Necrosis Factor (TNF).
4. Increased amounts of TNF activates the Tissue Factor Gene (TF)
5. Increased Amounts of TF causes the release of Thromboplastin.
6. The release of Thromboplastin activates the release of clotting Factors VII (VIIa) and trace amounts of Factor Xa into the blood.
7. This activates the release of Factors IX and X to IXa and the increase of Factor Xa.
8. The activation of the blood clotting cascade leads to Disseminated Intravascular coagulation and the clotting or thickening of the blood inside the blood vessels.
9. The DIC or hyper-coagulation will mask the fermentation of healthy cells to unhealthy cells or cancerous cells.
10. As the unhealthy cells or cancerous cells increase the body will go into preservation mode and begin forming fibrin nets to encapsulated these unhealthy cells to protect healthy body cells.
11. As body and blood cells breakdown from MAT this causes an increase of MAT and EMPO leading to systemic latent tissue acidosis and a potential metastatic cancerous condition.

 Table 5

DISSEMINATED INTRAVASCULAR COAGULATION RESULTING
IN CELLULAR DISORGANIZATION OR FERMENTATION/OXIDATON AND THE INCREASE OF MAT AND EMPO

1. A Physical and/or Emotional Disturbance Occurs from Lifestyle and/or Dietary choices.
2. Leads to cellular fermentation and degeneration and the birth of EMPO
3. This lead to increased abnormal amounts of MAT that activates the Tumor Necrosis Factor (TNF).
4. Increased amounts of TNF activates the Tissue Factor Gene (TF)
5. Increased Amounts of TF causes the release of Thromboplastin.
6. The release of Thromboplastin activates the release of clotting Factors VII and Factor Xa in the blood.
7. This activates the release of Factors IX and X to IXa and the increase of Factor Xa.
8. The activated blood clotting cascade leads to Disseminated Intravascular coagulation and the clotting or thickening of the blood inside the blood vessels.
9. The DIC or hyper-coagulation will mask the fermentation of healthy cells to unhealthy cells or cancerous cells.
10. As the unhealthy cells or cancerous cells increase the body will go into preservation mode and begin forming fibrin nets to encapsulated the unhealthy cells.
11. This leads to tumor formation of the unhealthy or cancerous cells.
12. As the body and blood cells breakdown this causes an increase of MAT and EMPO leading to an increased risk of  systemic metastatic cancer.

Table 6

ENDOTHEIAl CELL CONVERSION FROM AN
ANTITHROMBOTIC STATE TO A PROCOAGULANT STATE
CELLULAR DISORGANIZING PATHWAY

1. A Physical and/or Emotional Disturbance Occurs from Lifestyle and/or Dietary choices
2. Leads to cellular fermentation and degeneration and the birth of EMPO
3. This leads to increased abnormal amounts of MAT that damages the protective endothelial cover cells leading to a reduction of PGI2
4. The absence of PGI2 causes the release of Interleukin-1 and/or Tumor Necrosis Factor (TNF).
5. In addition the loss of protective endothelial cover cells leads to Tissue Factor Gene Activation and the release of Thrombin causing a pro-coagulate state leading to DIC
6. Another pathway to DIC would be the loss of protective endothelial cover cells and the absence of PGI2 causes the suppression of Thromomodulin, Protein C leading to procogradulation and DIC.

 Table 7

ENDOTHELIAL CELL CONVERSION
FROM AN ANTITHROMBOTIC STATE
(NORMAL PATHWAY)

Table 8

MECHANISM OF DISSEMINATED INTRAVASCULAR COAGULATION GENERATED BY MAT

Table 9

ACTIVATION OF SIALIDASE AND MICROZYMIAN OXIDATIVE BUFFERING SPECIES (MOBS) BY EMPO AND MAT

Table 10

DISSEMINATED INTRAVASCULAR COAGULATION RESULTING FROM PHAGOCYTIC OXIDATIVE BURST

Table 11

MOST BLOOD TEST and DISSEMINATED INTRAVASCULAR COAGULATION WITH SOLUBILIZED EXTRACELLULAR MATRIX

Table 12

TYPICAL SOURCES OF FERMENTATION INSULT (MAT) IN BIOLOGICAL SYSTEMS INITIATING DIC

Table 13

POSITIVE CHARGE OF CANCEROUS CELLS AND TUMORS AND THE FORMATION OF FIBRIN NETS AND TREES IN RESPONSE TO MAT

Will Soy Prevent or Reverse Disease?

Will Eating and/or Drinking Soy Prevent or Reverse Dis-ease or So-called Disease?

Cancer is a group of dis-eases characterized by the uncontrolled fermentation and degeneration of body cells. Over 10 million Americans today are cancer survivors, and about 1.4 million Americans are expected to be diagnosed each year.¹

“Diet plays an important role in the prevention and treatment of ALL cancerous conditions, and soy protein is one of the leading anti-acid or alkalizing and therefore anti-carcinogenic foods being studied,” stated Dr. Robert O. Young, Director of Research at the pH Miracle Living Center.

SOY FOODS & CANCER

There has been much focus during the past 15 years on the anticancer effects of soy foods.²There are several presumed chemopreventive agents in the soy bean,⁶ but the isoflavones have received the most attention.³ A particular interest lies in the role of soy foods and isoflavones in reducing the risk of breast and prostate cancer.²

SOY & BREAST CANCER

Data modestly supports the hypothesis that soy food intake may reduce the incidence of breast cancer. A recently published analysis found the relative risk for breast cancer was 95 percent when comparing high- vs. low-soy consumers.⁵ However, many of the case-control and prospective studies included in this analysis were of poor quality.⁶

Rodent studies have generally shown that isoflavones, or soy protein, inhibit chemically induced mammary tumors when given prior to tumor initiation^7-9, although there are a number of exceptions.^10-12 Interestingly, the chemopreventive effects of isoflavones appear to be affected by the background dietary choices.

When the isoflavone genistein was added to the semi-purified diet, chemically induced rodent mammary tumors were not inhibited, but when added to the regular chow diet, tumor development was suppressed by approximately 50 percent.¹³ This suggests that animal research, which most commonly uses semi-purified diets, may actually underestimate the potential anticarcinogenic effects of soy and other foods.

Soy & Markers of Breast Cancer

In contrast to the animal and epidemiologic data, there is little clinical evidence that soy or isoflavones favorably affect markers of breast cancer risk including breast tissue density,^{14, 15}serum estrogen levels,^{16, 17} and breast cell proliferation.¹⁸ There is limited evidence that estrogen metabolism is favorably affected¹⁹ and that menstrual cycle length is increased (which decreases cancer risk).¹⁶

Nevertheless, there remains considerable enthusiasm for the possibility that soy food intake contributes to the low breast cancer rate in Japan.

Early Intake of Soy May Reduce Breast Risk

There is both epidemiologic ^20-22 and animal ^{23, 24} data in support of the hypothesis that early soy intake reduces later risk of developing breast cancer. This hypothesis is consistent with mounting evidence that early life influences — parity, lactation, age at menses, birth weight, etc. — impact risk of developing breast cancer.^25-36 Studies of migrants suggest that the first 20 years of life have an especially profound impact on risk.^36-38 The epidemiologic data suggest just one to two servings of soy foods is protective.

Breaking News – Soy Breast Cancer Study

Soy Breast Cancer Study Holds Promise, But Calls for Further Research

For more than 15 years, soy foods have been actively investigated for their possible role in reducing breast cancer risk. Initial enthusiasm about this hypothesis was based on several observations. These include the low breast cancer rates in Japan, early animal research indicating that soy beans in rodent diets reduced mammary tumor development and evidence suggesting that the isoflavones (phytoestrogens) in soy foods may exert anti-estrogenic effects.

However, establishing a relationship between cancer risk and diet – especially specific foods – is much more difficult than establishing such links in the case of other chronic diseases such as coronary heart disease. This is because there are few well-established non-invasive indicators of cancer risk, and studies are very rarely conducted for long enough to measure actual differences in tumor incidence. Consequently, it is difficult to claim with confidence whether a particular intervention increases or decreases the chances of developing cancer.

Epidemiologic research is a useful mode of investigation for exploring a relationship between diet and cancer. Epidemiology is the study of the patterns, causes, and control of disease in groups of people. There are two primary types of epidemiologic studies, case-control and prospective studies. In case-control studies, scientists compare people with cancer to those without in hopes of identifying characteristics such as lifestyle or diet that are more common to one group than the other. In prospective studies, scientists first evaluate the characteristics of a large group of healthy people, then follow those subjects for many years in hopes of identifying whether certain factors are more common to those who develop cancer than to those who don’t. Generally, prospective studies are considered more credible than case-control studies. It is important to recognize, however, that epidemiologic studies cannot establish cause and effect relationships. Only clinical trials can do that. But epidemiologic studies are often used as a basis for clinical research.

To evaluate the relationship between soy intake and breast cancer risk, Bruce Trock and colleagues from the Johns Hopkins School of Medicine and Georgetown University conducted a meta-analysis of epidemiologic studies. A meta-analysis is the statistical analysis of a large collection of results from individual studies for the purpose of integrating the findings. This particular analysis included 12 case-control studies and 6 prospective studies. The major finding of this analysis was that when all women (Asian and non-Asian, pre- and postmenopausal) were considered, soy intake was associated with a 14% reduction in breast cancer risk. That is, women consuming higher quantities of soy were 14% less likely to develop breast cancer than women who consumed relatively little soy. However, subgroup analysis revealed that soy was more protective against pre- compared to postmenopausal breast cancer, and was protective in studies involving non-Asian women but not Asian women.

The analysis by Trock and colleagues provides modest support for the notion that soy may protect against breast cancer. A 14% reduction is certainly noteworthy, but for several reasons the study results should be interpreted with caution.

First, in many studies, soy intake was not actually quantified. Rather, it was estimated based on the urinary excretion of isoflavones. Because urinary isoflavone excretion varies so much from person to person, it provides only a rough approximation of soy intake. Furthermore, although soy was found to be protective in studies involving non-Asian women, the intake of soy by the women in these studies was quite low. There is some doubt as to whether such low intakes are sufficient to exert biological effects. Since soy foods are still consumed by only a minority of people in non-Asian countries – and are often favored by especially health-conscious individuals – we must consider the possibility that the perceived cancer-protective effects of soy may result from an overall healthy lifestyle, rather than soy consumption per se. Although the researchers employed statistical techniques to try to separate the effects of soy from other factors common to people who eat soy, this is very difficult to do.

While some evidence, including the new analysis by Trock and colleagues, suggests soy foods may reduce breast cancer risk, no conclusions can be made at this time. Nevertheless, because soy foods provide excellent nutrition, they can play an important role in an overall healthy diet, regardless of their possible relationship to breast cancer protection.

SOY & PROSTATE CANCER

The soy bean isoflavone genistein inhibits the growth of both androgen-dependent^39-42 and androgen-independent^{39, 42-45} prostate cancerous cells, depending on the level of soy doses administered. In addition, genistein inhibits the invasive capacity of prostate cancerous cells ⁴²and enhances the ability of radiation to kill these cells.⁴⁶ However, the concentration of genistein required to exert these effects is higher than the serum isoflavone levels of people who eat soy foods.^47-49 Nevertheless, several observations suggest these effects are biologically relevant.^39,44-49

Regional Diets Can Impact Prostate Cancer

In Japan, although many men have prostate cancer, few die of this dis-ease. This is because the small tumors often referred to as latent prostate cancer, not uncommon to Japanese men, rarely progress to the more advanced form of this disease.^{51, 52} Isoflavones in combination with tea extracts were shown to reduce tumor growth in mice more effectively than either agent alone.⁹

In Asia, and especially in Japan, where prostate cancer mortality rates are low, both soy foods and tea are important components of their diet. There are likely several factors that contribute to this clinical situation in Japanese men and according to the International Prostate Health Council, and isoflavone intake from soy foods may be one.⁵³

There has been limited epidemiologic investigation of the relationship between soy intake and prostate cancer. These studies have produced mixed results but can be said to be consistent with the hypothesis that soy intake reduces prostate cancer risk.

A recent analysis of 10 epidemiologic studies found that soy intake was associated with a one-third reduction in prostate cancer risk.⁵ However, many of the epidemiologic studies involved a small number of cases^{54, 55} and/or did not comprehensively evaluate soy food intake. However, a recent comprehensive Japanese case-control study found that when comparing the highest with the lowest soy food intake cases, risk was reduced by nearly 50 percent.⁵⁶

Soy May Help Treat Existing Prostate Cancer

Data suggests that soy foods may be useful in the treatment of existing prostate cancer, but this remains speculative. A study of 11 trials, three involving healthy subjects^57-59 and eight involving prostate cancer patients,^60-67 examined the effects of isoflavones on PSA levels. No benefits were noted in healthy subjects, but among the cancer patients one-half noted favorable effects.⁶⁸Recent intervention data demonstrate that reducing prostate cancer risk is not dependent upon reductions in PSA levels.⁶⁹

References

1. American Cancer Society. Cancer Facts and Figures; 2005.
2. Messina MJ, Persky V, Setchell KD, Barnes S. Soy intake and cancer risk: a review of thein vitro and in vivo data. Nutr Cancer 1994;21:113-131.
3. Messina M, Barnes S. The role of soy products in reducing risk of cancer. J Natl Cancer Inst 1991;83:541-546.
4. Sarkar FH, Li Y. Soy isoflavones and cancer prevention. Cancer Invest 2003;21:744-757.
5. The health claim petition: soy protein and the reduced risk of certain cancers. 2004.(Accessed at http://www.fda.gov/ohrms/dockets/dockets/04q0151/04q0151.htm.)
6. Yan L, Spitznagel E. A meta-analysis of soy foods and risk of breast cancer in women. Int J Cancer Prevention 2005;1:281-293.
7. Messina MJ, Loprinzi CL. Soy for breast cancer survivors: a critical review of the literature.J Nutr 2001;131:3095S-3108S.
8. Magee PJ, Rowland IR. Phyto-oestrogens, their mechanism of action: current evidence for a role in breast and prostate cancer. Br J Nutr 2004;91:513-531.
9. Zhou JR, Yu L, Mai Z, Blackburn GL. Combined inhibition of estrogen-dependent human breast carcinoma by soy and tea bioactive components in mice. Int J Cancer 2004;108:8-14.
10. Cohen LA, Zhao Z, Pittman B, Scimeca JA. Effect of intact and isoflavone-depleted soy protein on NMU-induced rat mammary tumorigenesis. Carcinogenesis 2000;21:929-935.
11. Day JK, Besch-Williford C, McMann TR, Hufford MG, Lubahn DB, MacDonald RS. Dietary genistein increased DMBA-induced mammary adenocarcinoma in wild-type, but not ER alpha KO, mice. Nutr Cancer 2001;39:226-232.
12. Thomsen AR, Mortensen A, Breinholt VM, Lindecrona RH, Penalvo JL, Sorensen IK. Influence of Prevastein(R), an Isoflavone-Rich Soy Product, on Mammary Gland Development and Tumorigenesis in Tg.NK (MMTV/c-neu) Mice. Nutr Cancer 2005;52:176-188.
13. Kim H, Hall P, Smith M, Kirk M, Prasain JK, Barnes S, Grubbs C. Chemoprevention by grape seed extract and genistein in carcinogen-induced mammary cancer in rats is diet dependent. J Nutr 2004;134:3445S-3452S.
14. Atkinson C, Warren RM, Sala E, Dowsett M, Dunning AM, Healey CS, Runswick S, Day NE, Bingham SA. Red-clover-derived isoflavones and mammographic breast density: a double-blind, randomized, placebo-controlled trial. Breast Cancer Res 2004;6:R170-179.
15. Maskarinec G, Takata Y, Franke AA, Williams AE, Murphy SP. A 2-year soy intervention in premenopausal women does not change mammographic densities. J Nutr2004;134:3089-3094.
16. Kurzer MS. Hormonal effects of soy in premenopausal women and men. J Nutr2002;132:570S-573S.
17. Maskarinec G, Franke AA, Williams AE, Hebshi S, Oshiro C, Murphy S, Stanczyk FZ. Effects of a 2-year randomized soy intervention on sex hormone levels in premenopausal women. Cancer Epidemiol Biomarkers Prev 2004;13:1736-1744.
18. Palomares MR, Hopper L, Goldstein L, Lehman CD, Storer BE, Gralow JR. Effect of soy isoflavones on breast proliferation in postmenopausal breast cancer survivors. Breast Cancer Res Treatment 2004;88 (Suppl 1):4002.
19. Brown BD, Thomas W, Hutchins A, Martini MC, Slavin JL. Types of dietary fat and soy minimally affect hormones and biomarkers associated with breast cancer risk in premenopausal women. Nutr Cancer 2002;43:22-30.
20. Shu XO, Jin F, Dai Q, Wen W, Potter JD, Kushi LH, Ruan Z, Gao YT, Zheng W. Soy food Intake during Adolescence and Subsequent Risk of Breast Cancer among Chinese Women.Cancer Epidemiol Biomarkers Prev 2001;10:483-488.
21. Wu AH, Wan P, Hankin J, Tseng CC, Yu MC, Pike MC. Adolescent and adult soy intake and risk of breast cancer in Asian-Americans. Carcinogenesis 2002;23:1491-1496.
22. Korde L, Fears T, Wu A, West D, Pike M, Hoover R, Ziegler R. Adolescent and childhood soy intake and breast cancer risk in Asian-American women. Breast Cancer Res Treat2005;88 (suppl 1):S149.
23. Lamartiniere CA, Zhao YX, Fritz WA. Genistein: mammary cancer chemoprevention, in vivo mechanisms of action, potential for toxicity and bioavailability in rats. J Women’s Cancer 2000;2:11-19.
24. Hilakivi-Clarke L, Onojafe I, Raygada M, Cho E, Skaar T, Russo I, Clarke R. Prepubertal exposure to zearalenone or genistein reduces mammary tumorigenesis. Br J Cancer1999;80:1682-1688.
25. Russo J, Lareef H, Tahin Q, Russo IH. Pathways of carcinogenesis and prevention in the human breast. Eur J Cancer 2002;38 Suppl 6:S31-32.
26. Hamilton AS, Mack TM. Puberty and genetic susceptibility to breast cancer in a case-control study in twins. N Engl J Med 2003;348:2313-2322.
27. Elias SG, Peeters PH, Grobbee DE, van Noord PA. Breast cancer risk after caloric restriction during the 1944-1945 Dutch famine. J Natl Cancer Inst 2004;96:539-546.
28. Michels KB, Ekbom A. Caloric restriction and incidence of breast cancer. JAMA2004;291:1226-1230.
29. Lee SY, Kim MT, Kim SW, Song MS, Yoon SJ. Effect of lifetime lactation on breast cancer risk: a Korean women’s cohort study. Int J Cancer 2003;105:390-393.
30. Leon DA, Carpenter LM, Broeders MJ, Gunnarskog J, Murphy MF. Breast cancer in Swedish women before age 50: evidence of a dual effect of completed pregnancy. Cancer Causes Control 1995;6:283-291.
31. Zheng T, Duan L, Liu Y, Zhang B, Wang Y, Chen Y, Zhang Y, Owens PH. Lactation reduces breast cancer risk in Shandong Province, China. Am J Epidemiol 2000;152:1129-1135.
32. Zheng T, Holford TR, Mayne ST, Owens PH, Zhang Y, Zhang B, Boyle P, Zahm SH. Lactation and breast cancer risk: a case-control study in Connecticut. Br J Cancer2001;84:1472-1476.
33. Vatten L. Can prenatal factors influence future breast cancer risk? Lancet 1996;348:1531.
34. Michels KB, Trichopoulos D, Robins JM, Rosner BA, Manson JE, Hunter DJ, Colditz GA, Hankinson SE, Speizer FE, Willett WC. Birthweight as a risk factor for breast cancer.Lancet 1996;348:1542-1546.
35. Freudenheim JL, Marshall JR, Vena JE, Moysich KB, Muti P, Laughlin R, Nemoto T, Graham S. Lactation history and breast cancer risk. Am J Epidemiol 1997;146:932-938.
36. Hemminki K, Li X. Cancer risks in second-generation immigrants to Sweden. Int J Cancer 2002;99:229-237.
37. Shimizu H, Ross RK, Bernstein L, Yatani R, Henderson BE, Mack TM. Cancers of the prostate and breast among Japanese and white immigrants in Los Angeles County. Br J Cancer 1991;63:963-966.
38. Hemminki K, Li X, Czene K. Cancer risks in first-generation immigrants to Sweden. Int J Cancer 2002;99:218-228.
39. Peterson G, Barnes S. Genistein and biochanin A inhibit the growth of human prostate cancer cells but not epidermal growth factor receptor tyrosine autophosphorylation.Prostate 1993;22:335-345.
40. Onozawa M, Fukuda K, Ohtani M, Akaza H, Sugimura T, Wakabayashi K. Effects of soy bean isoflavones on cell growth and apoptosis of the human prostatic cancer cell line LNCaP. Jpn J Clin Oncol 1998;28:360-363.
41. Shen JC, Klein RD, Wei Q, Guan Y, Contois JH, Wang TT, Chang S, Hursting SD. Low-dose genistein induces cyclin-dependent kinase inhibitors and G(1) cell-cycle arrest in human prostate cancer cells. Mol Carcinog 2000;29:92-102.
42. Santibanez JF, Navarro A, Martinez J. Genistein inhibits proliferation and in vitro invasive potential of human prostatic cancer cell lines. Anticancer Res 1997;17:1199-1204.
43. Naik HR, Lehr JE, Pienta KJ. An in vitro and in vivo study of antitumor effects of genistein on hormone refractory prostate cancer. Anticancer Res 1994;14:2617-2619.
44. Kyle E, Neckers L, Takimoto C, Curt G, Bergan R. Genistein-induced apoptosis of prostate cancer cells is preceded by a specific decrease in focal adhesion kinase activity. Mol Pharmacol 1997;51:193-200.
45. Bhatia N, Agarwal R. Detrimental effect of cancer preventive phytochemicals silymarin, genistein and epigallocatechin 3-gallate on epigenetic events in human prostate carcinoma DU145 cells. Prostate 2001;46:98-107.
46. Hillman GG, Forman JD, Kucuk O, Yudelev M, Maughan RL, Rubio J, Layer A, Tekyi-Mensah S, Abrams J, Sarkar FH. Genistein potentiates the radiation effect on prostate carcinoma cells. Clin Cancer Res 2001;7:382-390.
47. Doerge DR, Chang HC, Churchwell MI, Holder CL. Analysis of soy isoflavone conjugation in vitro and in human blood using liquid chromatography-mass spectrometry. Drug Metab Dispos 2000;28:298-307.
48. Chang HC, Churchwell MI, Delclos KB, Newbold RR, Doerge DR. Mass spectrometric determination of Genistein tissue distribution in diet-exposed Sprague-Dawley rats. J Nutr2000;130:1963-1970.
49. Dalu A, Haskell JF, Coward L, Lamartiniere CA. Genistein, a component of soy, inhibits the expression of the EGF and ErbB2/Neu receptors in the rat dorsolateral prostate. Prostate1998;37:36-43.
50. Messina M. Emerging evidence on the role of soy in reducing prostate cancer risk. Nutr Rev 2003;61:117-131.
51. Yatani R, Kusano I, Shiraishi T, Hayashi T, Stemmermann GN. Latent prostatic carcinoma: pathological and epidemiological aspects. Jpn J Clin Oncol 1989;19:319-326.
52. Shibata A, Whittemore AS, Imai K, Kolonel LN, Wu AH, John EM, Stamey TA, Paffenbarger RS. Serum levels of prostate-specific antigen among Japanese-American and native Japanese men. J Natl Cancer Inst 1997;89:1716-1720.
53. Griffiths K. Estrogens and prostatic disease. International Prostate Health Council Study Group. Prostate 2000;45:87-100.
54. Jacobsen BK, Knutsen SF, Fraser GE. Does high soy milk intake reduce prostate cancer incidence? The Adventist Health Study (United States) [see comments]. Cancer Causes Control 1998;9:553-557.
55. Severson RK, Nomura AM, Grove JS, Stemmermann GN. A prospective study of demographics, diet, and prostate cancer among men of Japanese ancestry in Hawaii.Cancer Res 1989;49:1857-1860.
56. Lee MM, Gomez SL, Chang JS, Wey M, Wang RT, Hsing AW. Soy and isoflavone consumption in relation to prostate cancer risk in China. Cancer Epidemiol Biomarkers Prev2003;12:665-668.
57. Urban D, Irwin W, Kirk M, Markiewicz MA, Myers R, Smith M, Weiss H, Grizzle WE, Barnes S. The Effect of Isolated Soy Protein on Plasma Biomarkers in Elderly Men with Elevated Serum Prostate Specific Antigen. J Urol 2001;165:294-300.
58. Adams KF, Chen C, Newton KM, Potter JD, Lampe JW. Soy isoflavones do not modulate prostate-specific antigen concentrations in older men in a randomized controlled trial.Cancer Epidemiol Biomarkers Prev 2004;13:644-648.
59. Jenkins DJ, Kendall CW, D’Costa MA, Jackson CJ, Vidgen E, Singer W, Silverman JA, Koumbridis G, Honey J, Rao AV, Fleshner N, Klotz L. Soy consumption and phytoestrogens: effect on serum prostate specific antigen when blood lipids and oxidized low-density lipoprotein are reduced in hyperlipidemic men. J Urol 2003;169:507-511.
60. Hussain M, Banerjee M, Sarkar FH, Djuric Z, Pollak MN, Doerge D, Fontana J, Chinni S, Davis J, Forman J, Wood DP, Kucuk O. Soy isoflavones in the treatment of prostate cancer. Nutr Cancer 2003;47:111-117.
61. Fischer L, Mahoney C, Jeffcoat AR, Koch MA, Thomas BE, Valentine JL, Stinchcombe T, Boan J, Crowell JA, Zeisel SH. Clinical characteristics and pharmacokinetics of purified soy isoflavones: multiple-dose administration to men with prostate neoplasia. Nutr Cancer2004;48:160-170.
62. deVere White RW, Hackman RM, Soares SE, Beckett LA, Li Y, Sun B. Effects of a genistein-rich extract on PSA levels in men with a history of prostate cancer. Urology2004;63:259-263.
63. Spentzos D, Mantzoros C, Regan MM, Morrissey ME, Duggan S, Flickner-Garvey S, McCormick H, DeWolf W, Balk S, Bubley GJ. Minimal effect of a low-fat/high soy diet for asymptomatic, hormonally naive prostate cancer patients. Clin Cancer Res 2003;9:3282-3287.
64. Jarred RA, Keikha M, Dowling C, McPherson SJ, Clare AM, Husband AJ, Pedersen JS, Frydenberg M, Risbridger GP. Induction of Apoptosis in Low to Moderate-Grade Human Prostate Carcinoma by Red Clover-derived Dietary Isoflavones. Cancer Epidemiol Biomarkers Prev 2002;11:1689-1696.
65. Kumar NB, Cantor A, Allen K, Riccardi D, Besterman-Dahan K, Seigne J, Helal M, Salup R, Pow-Sang J. The specific role of isoflavones in reducing prostate cancer risk. Prostate2004;59:141-147.
66. Dalais FS, Meliala A, Wattanapenpaiboon N, Frydenberg M, Suter DA, Thomson WK, Wahlqvist ML. Effects of a diet rich in phytoestrogens on prostate-specific antigen and sex hormones in men diagnosed with prostate cancer. Urology 2004;64:510-515.
67. Kranse R, Dagnelie PC, van Kemenade MC, de Jong FH, Blom JH, Tijburg LB, Weststrate JA, Schroder FH. Dietary intervention in prostate cancer patients: PSA response in a randomized double-blind placebo-controlled study. Int J Cancer 2005;113:835-840.
68. Messina M, Kucuk O, Lampe J. An overview of the health effects of isoflavones with an emphasis on prostate cancer risk and prostate specific antigen levels. JAOAC; (accepted).
69. Meyer F, Galan P, Douville P, Bairati I, Kegle P, Bertrais S, Estaquio C, Hercberg S. Antioxidant vitamin and mineral supplementation and prostate cancer prevention in the SU.VI.MAX trial. Int J Cancer 2005;116:182-186.

The Dangers of Drinking Cow’s Milk!

Due to the extreme processes that milk goes through and the high amounts of antibiotics, hormones, and genetically-modified substances that cows are continually exposed to, I believe there are real and eminent concerns associated with drinking milk from cows. All cows release toxins through their milk, as milk is a natural exit-portal for substances that the body cannot use.

“Ingredients” Added to Cow’s Milk

A Veritable Hormone Cocktail: including pituitary, steroid, hypothalamic, and thyroid hormones (remember most cows are extremely stressed)

Gastrointestinal Peptides: Nerve and epidermal growth factors, and the growth inhibitors MDGI and MAF rBGH (Recombinant Bovine Growth Hormone): a genetically engineered hormone directly linked to breast, colon and prostrate cancer. This is injected into cows to increase milk production[1]

Pus: National averages show at least 322 million cell-counts of pus per glass! [2] This is well-above the human limit for pus-intake, and has been directly linked to paratuberculosis bacteria, as well as Crohn’s disease. The pus comes from infected udders on the cows known as mastitis.

Blood Cells: The USDA allows up to 1.5 million white blood cells per milliliter of commonly-sold milk. [3] Yes, you are drinking cows blood in the milk and the USDA allows this!

Antibiotics: Currently, cows are in such a state of disease and mistreatment that they are continually being injected with antibiotic medicines, and rubbed down with chemical-laden ointments to deal with their chronic infections. Currently, regulating committees only test for 4 of the 85 drugs in dairy cows. This means that the other 81 drugs in cow’s milk are coming directly into your glasses and bodies.

Estimates show that 38% of milk in the U.S. is “contaminated with sulfa drugs or other antibiotics,” according to a study by the Centre for Science in the Public Interest and published in the Wall Street Journal on December 29, 1989. A study from the FDA data showed that over half of all milk was laden with traces of pharmaceuticals yet nothing has been done to control this.

How Does This Affect the Cows?

Not only are people drinking these toxins, they are also taking in the energetic effects of the life of the cow.

Studies show that many cows are infected with incredibly painful infections such as mastitis. [4] Due to over-milking, artificial hormones, bacteria and medications, cow’s udders can become chronically inflamed, thus altering the color and taste of the milk.

Over time, this bacterial invasion causes harm to the cow’s mammary gland, reeking havoc on the milk being produced. From parasitic worms to cancerous tumors, these diseases are often passed along to the next generation of cows, and more often, into the milk we drink.

Often times the conditions in which cows live, as well as the rigorous milking regimes, cause dairy cattle to live in a permanent state of sympathetic (stress) response, as well as adrenal over-load. When our adrenal glands are overworked for long periods of time, there is a overload of cortisol in the blood. When we drink this milk, we are then exposed to the millions of stress-response cells in the milk of cows. It is no wonder that we are a chronically stressed society!

Avoid Dangers Related to Cow’s Milk

Here are some ways to avoid the dangers associated with cow’s milk:

Replace cow’s milk with healthy natural substitutes: raw almond milk, raw hazel nut milk, raw coconut milk or my favorite – hemp milk.

If you do insist on drinking cow’s milk, make sure to buy only the non-genetically modified, range fed, organic raw versions. Even better, talk to your local organic farmer to make sure the cow’s are treated kindly.

Eliminate cheese because it is concentrated milk and always buy organic versions. Goat’s milk or cheese would be a better choice if you choose to continue to drink animal milk!

– Dr. Edward F. Group III, DC, ND, DACBN, DCBCN, DABFM

References:
The Cancer Prevention Coalition and Food & Water. New study Warns of Breast and Colon Cancer Risks from rBGH Milk. 1996 January 23.
PETA. Cows Used for Their Milk. The Dairy Industry.
Adkinson RW, Gough RH, Graham R, Yilmaz A. Implications of proposed changes in bulk tank somatic cell count regulations. J Dairy Sci. 2001 Feb;84(2):370-4
The Merck Veterinary Manual. Mastitis in Cattle. Merck Sharp & Dohme Corp.

Sex Protects Against Prostate and Breast Cancer!

Sex Protects Against Prostate and Breast Cancer!

Some studies have suggested that men who ejaculate more frequently may have a reduced risk of prostate cancer—although the difference appears to be very small, and others haven’t found a conclusive link. The benefits may be clearer for breast cancer prevention, however: A French study found that women who had sex at least once a month were less likely to develop breast cancer than those who didn’t.

https://phoreveryoung.wordpress.com/2014/11/17/sex-protects-against-prostate-and-breast-cancer/

Resource:

Marie-Elise Parent, associate professor, University of Montreal School of Public Health; David Samadi, M.D., chairman of urology, Lenox Hill Hospital, New York City; Oct. 28, 2014, Cancer Epidemiology

Meat Declared TOO Dangerous/ACIDIC for Human Consumption – Causes Cancer!

Processed Meats Declared too Dangerous/Acidic for Human Consumption

The World Cancer Research Fund recently completed a detailed review of 7,000 clinical studies covering links between diet and cancer. Upon conclusion it is evident that processed meats are dangerous for human consumption and consumers should stop buying and eating processed meats.

What are processed meats?Processed meats include bacon, sausage, hot dogs, sandwich meat, packaged ham, pepperoni, salami and nearly all meat found in prepared frozen meals. Processed meats are usually manufactured with a carcinogenic (linked to promote and cause cancer) ingredient known as sodium nitrate. Sodium nitrate is primarily used as a colour fixer by meat companies to make the packaged meats look bright red and fresh. Monosodium glutamate is also added on a regular basis to enhance the savoury flavour.

Sodium Nitrate has been strongly linked to the formation of cancer-causing nitrasamines in the human body, leading to a sharp increase in the risk of cancer for those consuming them. A 2005 Hawaii University study found that eating processed meats increased the risk of pancreatic cancer by 67%, whilst another study found that it increased the risk of colorectal cancer by 50%. These are scary numbers for those consuming processed meats on a regular basis.

Monosodium glutamate (MSG) is a second dangerous chemical found in virtually all processed meat products. MSG is a dangerous excitotoxin linked to neurological disorders such as migraine headaches, Alzheimer’s disease, loss of appetite control, obesity and many other serious health conditions. Manufacturers use MSG to add an addictive savory flavor to dead-tasting processed meat products.

Foods to NEVER eat:

• Beef jerky
• Bacon
• Sausage
• Pepperoni
• Hot dogs
• Sandwich meat
• Deli slices
• Ham/Pork
• Frozen pizzas with meat
• Canned soups containing meat
• Frozen meals with meat
• Ravioli and meat pasta foods
• Turkey
• Chicken
• Beef

…and many more meat products

If it’s so dangerous to consume why are they allowed to sell it?

Unfortunately now days the food industry interests now dominate the actions of the government regulators. The USDA for example tried to ban sodium nitrate in the late 1970′s but were overridden by the meat industry insisting the chemical was ‘safe’. Today the food and agriculture corporations hold tremendous influence over the food industry and as a result  consumers have little protection from dangerous chemicals intentionally added to foods, medicines and personal care products.

To avoid the dangers of processed meats:

• Always read ingredient labels
• Don’t buy anything made with sodium nitrate or MSG
• Avoid eating red meats served by restaurants, schools, hospitals, hotels or other institutions without asking for details
• Eat more fresh green organic fruit and vegetables
• Avoid processed meats always
• Spread the word and tell others about the dangers of sodium nitrate and MSG and the acids in meat including nitric acid, sulphuric acid, phosphuric acid and uric acid, all poisons to the body.

Antioxidants naturally found in fresh organ fruits and vegetables have been shown to help prevent the formation of cancerous-causing nitrosamines, protecting you from the devastating health effects of animal proteins. The best defence of course is to avoid animal protein/flesh all together!

Sources:

http://www.wcrf.org/PDFs/Colorectal-cancer-CUP-report-2010.pdf

http://voices.yahoo.com/sodium-nitrite-processed-meats-causes-cancer-2522974.html?cat=5

http://preventcancer.aicr.org/site/News2?page=NewsArticle&id=15642&news_iv_ctrl=0&abbr=pr_

http://organicconsumers.org/foodsafety/processedmeat050305.cfm

http://today.com/id/16361276/ns/today-food/t/things-you-need-know-about-deli-meats

Why Eating Meat and Cheese Is Making Your Body Dangerously Over-Acid Leading To Sickness and Disease Including Diabetes and/or Cancer!

 

Twenty-Five Scientific Points In Understanding Dr. Young’s “New Biology” and Why Eating Meat and Cheese Is Making Your Body Dangerously Over-Acid Leading To Sickness and Disease Including Diabetes and Cancer!

The following scientific discourse are twenty-five important points to understand concerning the creation of sodium bicarbonate (NaHCO3) and hydrochloric acid (HCL) in the stomach lining, the ingestion of protein, cheese and sugar in any form and how acid/alkaline biochemistry, physiology, and anatomy relate to health, sickness, and disease.

Unfortunately, contemporary medical doctors and scientists as well as alternative health practitioners do not understand how acid/base are created in the body and the onset of latent tissue acidosis in the colloidal connective tissue or the “Schade”. Welcome to the 21st century and Dr. Young’s “New Biology.”

How is acid/base created in the body?

1) The parietal or cover cells of the stomach split the sodium chloride of the blood. The sodium is used to bind with water and carbon dioxide to form the alkaline salt, sodium bicarbonate or NaHCO3. The biochemistry is: H20 + CO2 + NaCl = NaHCO3 + HCL. This is why a call the stomach an alkalizing organ NOT an organ of digestion. The stomach DOES NOT digest the food or liquids you ingest it alkalizes the food and liquid you ingest.

2) For each molecule of sodium bicarbonate (NaHCO3) made, a molecule of hydrochloric acid (HCL) is made and secreted into the so-called digestive system – specifically, the stomach (the gastric pits in the stomach) – to be eliminated. Therefore HCL is an acidic waste product of sodium bicarbonate created by the stomach to alkalize the food and liquids ingested.

3) The chloride ion from the sodium chloride (salt) binds to an acid or proton forming HCL as a waste product of sodium bicarbonate production. HCL has a pH of 1 and is highly toxic to the body and the cause of indigestion, acid reflux, ulcers and cancer.

4) When large amounts of acids, including HCL, enter the stomach from a rich animal protein or dairy product meal, such as meat and cheese, acid is withdrawn from the acid-base household. The organism would die if the resulting alkalosis – or NaHCO3 (base flood) or base surplus – created by the stomach was not taken up by the alkalophile glands that need these quick bases in order to build up their strong sodium bicarbonate secretions. These glands and organs are the stomach, pancreas, Brunner’s glands (between the pylorus and the junctions of the bile and pancreatic ducts), Lieberkuhn’s glands in the liver and its bile with its strong acid binding capabilities which it has to release on the highly acidic meat and cheese to buffer its strong acids of nitric, sulphuric, phosphoric, uric and lactic acids.

5) When a rich animal protein and dairy product meal is ingested, the stomach begins to manufacture and secrete sodium bicarbonate (NHCO3) to alkalize the acids from the food ingested. This causes a loss in the alkaline reserves and an increase in acid and/or HCL found in the gastric pits of the stomach. These acids and/or HCL are taken up by the blood which lowers blood plasma pH. The blood eliminates this increase in gastrointestinal acid by throwing it off into the Pishinger’s spaces.

6) The space enclosed by these finer and finer fibers is called the Pishinger’s space, or the extracellular space that contains the fluids that bath and feed each and every cell while carrying away the acidic waste from those same cells. There is no mention of this organ in American physiology text books. There is mention of the extracellular space but not of any organ that stores acids from metabolism and diet, like the kidney. I call this organ the “pre-kidney” because it stores metabolic and gastrointestinal acids until they can be buffered and eliminated via the skin, urinary tract, or bowels.

7) After a rich animal protein or dairy product meal, the urine pH becomes alkaline. The ingestion of meat and cheese causes a reaction in acidic fashion in the organism by the production of sulfuric, phosporhoric, nitric, uric, lactic, acetylaldehyde and ethanol acids, respectively, but also through the formation and excretion of base in the urine. Therefore eating meat and cheese causes a double loss of bases leading to tissue acidosis and eventual disease, especially inflammation and degenerative diseases.

8) During heavy exercise, if the the resulting lactic acid was not adsorbed by the collagen fibers, the specific acid catchers of the body, the organism would die. The total collection of these fibers is the largest organ of the body called SCHADE, the colloidal connective tissue organ. NO liquid exchange occurs between the blood and the parenchyma cells, or in reverse, unless it passes through this connective tissue organ. This organ connects and holds everything in our bodies in place. This organ is composed of ligaments, tendons, sinew, and the finer fibers that become the scaffolding that holds every single cell in our bodies in place. When acids are stored in this organ, which includes the muscles, inflammation and pain develop. The production of lactic acid is increased with the ingestion of milk, cheese, yogurt, butter and especially ice cream.

That is why I have stated, “acid is pain and pain is acid.” You cannot have one without the other. This is the beginning of latent tissue acidosis leading to irritation, inflammation and degeneration of the cells, tissues and organs.

 

9) The more acidity created from eating meat, cheese, milk or ice cream the more gastrointestinal acids are adsorbed into the the collagen fibers to be neutralized and the less sodium bicarbonate or NaHCO3 that is taken up by the alkalophile glands. The larger the potential difference between the adsorbed acids and the amount of NaHCO3 generated with each meal, the more or less alkaline are the alkalophile glands like the pancreas, gallbladder, pylorus glands, blood, etc. The acid binding power of the connective tissue, the blood, and the alkalophile glands depends on its alkali reserve, which can be determined through blood, urine, and saliva pH, including live and dried blood analysis as taught by Dr. Robert O. Young. The saliva pH is an indication of alkali reserves in the alkalophile glands and the urine pH is an indication of the pH of the fluids that surround the cells or the Pishinger’s space.

10) The iso-structure of the blood maintains the pH of the blood by pushing off gastrointestinal or metabolic acids into the connective tissue or the Pishinger’s space. The blood gives to the urine the same amount of acid that it receives from the tissues and liver so it can retain its iso-form. A base deficiency is always related to the deterioration of the deposit ability of the connective tissues or the Pishinger’s space. As long as the iso-structure of the blood is maintained, the urine – which originates from the blood – remains a faithful reflected image of the acid-base regulation, not of the blood, but of the tissues. The urine therefore is an excretion product of the tissues, not the blood. So when you are testing the pH of the urine, you are testing the pH of the tissues.

11) A latent “acidosis” is the condition that exists when there are not enough bases in the alkalophile glands because they have been used up in the process of neutralizing the acids adsorbed to the collagen fibers. This leads to compensated “acidosis.” This means the blood pH has not changed but other body systems have changed. This can then lead to decompensated “acidosis” where the alkaline reserves of the blood are used up and the pH of the blood is altered. Decompensated “acidosis” can be determined by testing the blood pH, urine pH and the saliva pH. The decrease in the alkaline reserves in the body occurs because of hyper-proteinization, (eating Meat and Cheese!)or too much protein, and hyper-carbonization, or too much sugar. This is why 80 to 90 year old folks are all shrunk up and look like prunes. They have very little or no alkaline reserves in their alkalophile glands. When all the alkaline minerals are gone, so are you and your battery runs down. The charge of your cellular battery can be measured by testing the ORP or the oxidative reduction potential of the blood, urine or saliva using an ORP meter. As you become more acidic this energy potential or ORP increases.

12) If there is not enough base left over after meat and cheese or surgary meal, or enough base to neutralize and clear the acids stored in the connective tissues, a relative base deficiency develops which leads to latent tissue acidosis. When this happens the liver and pancreas are deficient of adequate alkaline juices to ensure proper alkalization of the food in your stomach and small intestine.

13) Digestion or alkalization cannot proceed without enough of these alkaline juices for the liver and pancreas, etc., and so the stomach has to produce more acid in order to make enough base, ad nauseam, and one can develop indigestion, nausea, acid reflux, GERD, ulcers, esophageal cancer and stomach cancer. All of these symptoms are not the result of too much acid or HCL in the stomach. On the contrary, it is the result of too little base in the form of sodium bicarbonate!

14) Therefore the stomach is NOT an organ of digestion as currently taught in ALL biology and medical texts, BUT an organ of contribution or deposit. It’s function is to deposit alkaline juices to the stomach to alkalize the food and to the blood to carry to the alklophile glands!!!!

15) There is a daily rhythm to this acid base ebb and flow of the fluids of the body. The stored acids are mobilized from the connective tissues and Pishinger’s spaces while we sleep.
These acids reach their maximum (base tide) concentration in this fluid, and thereby the urine (around 2 a.m. is the most acidic). The acid content of the urine directly reflects the acid content of the fluid in the Pishinger’s spaces, the extracellular fluid compartments of the body. On the other hand, the Pishinger’s spaces become most alkaline around 2 p.m. (the base flood) as then the most sodium bicarbonate (NaHCO3) is being generated by the cover cells of the stomach to alkalize the food and drink we have ingested.

16) If your urine is not alkaline by 2 p.m. you are definitely in an ACIDIC condition and lacking in alkaline reserves. The pH of the urine should run between 6.8 and 8.4 but ideally 7.2 or greater.

17) After a high protein meal or meat or cheese, the free acids formed such as sulfuric, phosphoric, uric, and nitric acids stick to the collagen fibers to remove them from the blood and protect the delicate pH of the blood at 7.365. The H+ or proton ions from these acids are neutralized by the next base flood, the sodium bicarbonate produced after the meal. The H+ or proton ion combines with the carbonate or HCO3, converts to carbonic acid, H2CO3, which converts to CO2 and H2O. The sulfuric and other acids from proteins are neutralized as follows where the HR represents any acid with the R as its acid radical (SO4, PO4, or NO3) HR + NaHCO3 H2O + NaR (Ca, Mg, K)+ CO2.

18) Medical doctors and savants are not taught in medical school and therefore do not understand or recognize latent tissue acidosis. They understand and recognize compensated acidosis and decompensated acidosis. In compensated acidosis, breathing increases in order to blow off more carbonic acid which decreases PCO2 because of the lowered carbonate or HCO3. When the breathing rate can no longer get any faster and when the kidneys can no longer increase its’ function to keep up with the acid load, then the blood pH starts to change from a pH of 7.365 to 7.3 then to 7.2. At a blood pH of 6.95 the heart relaxes and the client goes into a coma or dies.

19) Metabolism of a normal adult diet results in the generation of 50 to 100 meq of H+ or proton per day, which must be excreted if the urine acid-base balance is to be maintained. A meq is a milliequivalent which is an expression of concentration of substance per liter of solution, calculated by dividing the concentration in milligrams per 100 milliliters by the molecular weight. This process involves two basis steps; 1) the reabsorption of the filtered sodium bicarbonate or NaHCO3 and, 2) excretion of the 50 to 100 meq of H+ or proton produced each day by the formation of titratable acidity and NH4+ or ammonium. Both steps involve H+ or proton secretion from the cells of the kidney into the urine.

20) Sodium bicarbonate (NaHCO3) must be reabsorbed into the blood stream, since the loss of NaHCO3 will increase the net acid load and lower the plasma NaHCO3 concentration. The loss of NaHCO3 in the urine is equivalent to the addition of H+ to the body since both are derived from the dissociation of H2CO3 or carbonic acid.

21) The biochemistry is: CO2 + H2O = H2CO3 = HCO3 + H+. The normal subject must reabsorb 4300 meq of NaHCO3 each day! The secreted H+ or proton ions are generated within the kidney cells from the dissociation of H2O or water. This process also results in the equimolar production OH- or hydroxyl ions. The OH- ions bind to the active zinc-containing site of the intracellular carbonic anhydrase; they then combine with CO2 to form HCO3- ions which are released back into the kidney cells and returned to the systemic circulation. Second, the dietary acid load is excreted by the secretion of H+ or proton ions from the kidney cells into the urine. These H+ or proton ions can do one of two things: the H+ or proton ions can be combined with the urinary buffers, particularly HPO4, in a process called titratable acidity (The biochemistry is: H+ + HPO4 = H2PO4), or the phosphate buffering system or the H+ or proton ions can combine with ammonia (NH3) to form ammonium as follows: NH3 + H+ = NH4.

22) This ammonia is trapped and concentrated in the kidney as ammonium which is then excreted in the urine.

23) In response to acid load, 36% of the H+ or proton goes intracellular in exchange for the release of Na+ (sodium) into the blood stream. 15% of the acid goes intracellular in exchange for K+ (potassium) – common in diabetics. 6% of the H+ or proton or acid goes directly into the cell to be buffered by intracellular processes. 43% is buffered extracellularly as NaHCO3- or sodium bicarbonate combining with H+ or proton to form H2CO3 or carbonic acid which breaks down to CO2 or carbon dioxide to be released by the lungs. 10% of CO2 or carbon dioxide is excreted through the lungs and 90% is used by the body to reabsorb alkaline minerals and make sodium bicarbonate for buffering gastrointestinal and metabolic acids.

The biochemistry is: CO2 + H2O = H2CO3 = HCO3 + H+.24) Of all the ways the body can buffer metabolic and dietary acids, the excretion of protein (the eating of meat and cheese) generated acid residues is the only process that does not add sodium bicarbonate back into blood circulation. This creates a loss of bases which is the forerunner of all sickness and disease. In the long run, the only way to replace these lost bases is by eating more alkaline electron-rich green foods and long-chain polyunsaturated fats. Eating meat and cheese is definitely hazardous to your health. That is why I say, “a cucumber a day keeps the doctor away while eating meat, cheese and even an apple creates more excess acid in the colloidal connective tissues, leading to latent tissue acidosis.

25) With over 30 years of research and testing over 500,000 samples of blood and over 1,000,000 samples of urine and saliva I have come to the conclusion that the Human Body is an acid producing organism by function – yet, it is an alkaline organism by design. Eating animal protein, especially meat and cheese and sugar from any source are deadly acidic choices – unless you interested in becoming sick, tired and fat over time.

Bottom line – the pH Miracle Lifestyle and Diet is a program that focuses on the foundational principal that the body is alkaline by design and yet acidic by function. This make this program the ultimate program for preventing and reversing aging and the onset of sickness and dis-ease. I would say that the pH Miracle Lifestyle and Diet is the diet for a longer healthier life.

Please remember this very important truth, hydrochloric acid is not the cause of digestion but the result of digestion. Start alkalizing today and begin improving the quality and quantity of your life today.

To learn more about the pH Miracle Lifestyle and Diet go to:
http://www.phmiracleliving.com and http://www.articlesofhealth.blogspot.com

 

The Beginning of the End to the Human Male Species or Girls Will Be Girls And Boys Will Be Girls

Here’s something rather rotten from the State of Denmark.

Its government yesterday unveiled official research showing that two-year-old children are at risk from a bewildering array of gender-bending hormonal chemicals in such everyday items as waterproof clothes, rubber boots, bed linen, acidic food, acidic drink, nappies/diapers, sunscreen lotion, moisturizing cream, hormones, birth and control pills.

The 326-page report, published by the environment protection agency, is the latest piece in an increasingly alarming jigsaw. A picture is emerging of ubiquitous chemical contamination driving down sperm counts and feminizing male children all over the developed world. And anti-pollution measures and regulations are falling far short of getting to grips with it.

Sperm counts are falling so fast that young men are less fertile than their fathers and produce only a third as much, proportionately, as hamsters. And gender-bending hormonal acidic chemicals are increasingly being blamed for the mystery of the “lost boys”: babies who should normally be male who have been born as girls instead.

According to Dr. Robert O. Young, Director of Research at the pH Miracle Living Center, “boys are created in an alkaline environment. When acidic hormonal chemicals are introduced into the fetus via the blood of the mother the sex of the fetus will be altered from a boy to a girl. This change in sex or sexual preference is also shifted as acidic hormonal chemicals are introduced via the water and/or food.”

The Danish government set out to find out how much contamination from gender-bending acidic chemicals a two-year-old child was exposed to every day. It concluded that a child could be “at critical risk” from just a few exposures to high levels of the substances, such as from rubber clogs, and imperilled by the amount it absorbed from sources ranging from acidic laced hormonal food to sunscreens.

The results build on earlier studies showing that British children have higher levels of gender-bending acidic chemicals in their blood than their parents or grandparents. Indeed WWF (formerly the World Wildlife Fund), which commissioned the older research, warned that the chemicals were so widespread that “there is very little, if anything, individuals can do to prevent contamination of themselves and their families.” Prominent among them are dioxins, PVC, flame retardants, phthalates (extensively used to soften plastics) and the now largely banned PCBs, one and a half million tons of which were used in countless products from paints to electrical equipment and estrogen.

“Young boys, like those in the Danish study, could end up producing less sperm and developing feminised behaviour,” states Dr. Young.

Research at Rotterdam’s Erasmus University found that boys whose mothers were exposed to PCBs and dioxins were more likely to play with dolls and tea sets and dress up in female clothes.

And it is in the womb that babies are most vulnerable; a study of umbilical cords from British mothers found that every one contained hazardous chemicals. Scientists at the University of Rochester in New York discovered that boys born to women exposed to phthalates had smaller penises and other feminization of the genitals.

The contamination may also offer a clue to a mysterious shift in the sex of babies. Normally 106 boys are born for every 100 girls: it is thought to be nature’s way of making up for the fact that men were more likely to be killed hunting or in conflict. But the proportion of females is rising, so much so that some 250,000 babies who statistically should have been boys have ended up as girls in Japan and the United States alone. In Britain, the discrepancy amounts to thousands of babies a year.

A Canadian Indian community living on ancestral lands at the eastern tip of Lake Huron, hemmed in by one of the biggest agglomerations of chemical factories on earth, gives birth to twice as many girls as boys. It’s the same around Seveso in Italy, contaminated with dioxins from a notorious accident in the 1970s, and among Russian pesticide workers. And there’s more evidence from places as far apart as Israel and Taiwan, Brazil and the Arctic.

Yet gender-benders are largely exempt from new EU regulations controlling hazardous chemicals. Britain, then under Tony Blair’s premiership, was largely responsible for this – restricting their inclusion in the first draft of the legislation, and then causing even what was included to be watered down. Confidential documents show that it did so after pressure from George W Bush’s administration, which protested that US exports “could be impacted”.

Now the Danish government is planning to lobby to have the rules toughened up. It is particularly concerned by other studies which show that gender-bending acidic chemicals acting together have far worse effects than the expected sum of their individual impacts. It wants this to be reflected in the regulations, citing its discovery of the many sources to which the two-year-olds are exposed – modern slings and arrows, as it were, of outrageous fortune.