Category Archives: Alkaline Lifestyle and Diet

Pathological Blood Coagulation and the Mycotoxic Oxidative Stress Test

 Robert Young PhD

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.

allergiesbefore

 

 

 

 

 

 

 

[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.

BowelCancerLive Blood Dried Blood_0166

 

 

 

 

 

 

 

 

[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.

calciumpattern

 

 

 

 

 

 

 

[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.)

sialicacid

[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.

Aspergillusnigercrystal

 

 

 

 

 

[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}

HIV

 

 

 

 

 

 

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.

poorfibrin

[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 MedicineVolume 28, Issue 12, 15 June 2000, Pages 1685–1696

 [12] Chang JCvan der Hoeven LHHaddox 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 FernandesCarlos 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]

Table1a

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.

Table2a

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.

Table3a

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.

Table4a

 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.

Table5aTable 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.

Talble6

 Table 7

ENDOTHELIAL CELL CONVERSION
FROM AN ANTITHROMBOTIC STATE
(NORMAL PATHWAY)

Table7

Table 8

MECHANISM OF DISSEMINATED INTRAVASCULAR COAGULATION GENERATED BY MAT

Table8Table 9

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

Table9

Table 10

DISSEMINATED INTRAVASCULAR COAGULATION RESULTING FROM PHAGOCYTIC OXIDATIVE BURST

Table10

Table 11

MOST BLOOD TEST and DISSEMINATED INTRAVASCULAR COAGULATION WITH SOLUBILIZED EXTRACELLULAR MATRIX

Table11

Table 12

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

Table12

Table 13

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

Table13

What Happens to ALL the Disappearing Can

12311128_1639530499647197_8412997691509003664_nWhat Happens to ALL the Disappearing Cancer Patients?

It’s been almost 20 years since I met my first disappearing patient — a nurse in her early 40s, let’s call her Kate. Kate was diagnosed with breast cancer. As a nurse, she had seen the results of breast cancer treatments. She was terrified, and determined. She was not heading for surgery, nor chemotherapy, nor radiation.

But Kate worked in a hospital. She worked with the doctors who diagnosed her cancer, and she worked with the surgeon, who wanted to schedule her into surgery “as soon as possible.”

The first thing Kate did was slow down. She did some research. It didn’t take her long to remind herself that in Canada, and in the USA, the treatments for cancer are akin to law. No hospital would dare deviate from the deadly three (cut, poison, burn).

Kate’s cancer was not large. She had been tested for cancer last year and no cancer was found. She knew it took many years for cancers to develop. At first, she was furious, “If it is here today, it must have been here last year. Why didn’t you find it last year?” It had not metastasized. It was not growing rapidly and was not affecting her health in any way. In theory, she had lots of time. So, she took some time.

But Kate didn’t look for magic cures. She didn’t search for the latest “cancer medicine.” She wasn’t interested in curing herself. She knew she was a nurse, not a doctor. She searched instead for the “cured” – patients who were diagnosed with cancer, and no longer had cancer. She knew from her work in the hospital, from conversations with patients, and with some staff, that these people existed — but from the perspective of the medical establishment, they seemed to disappear.

It didn’t take her long to find some patients who claimed they were cured. They hadn’t disappeared from life. They were eating, drinking, loving, and living full healthy and prosperous lives. But according to the medical records, they didn’t exist. They were “never cured.”

The medical system treated their cures as “anecdotal.” It ignored them. There was no attempt by any doctors to understand what happened to these cancer patients. They were no longer sick. The medical system looks after sick patients, treats sick patients. These patients were not sick.

Kate looked and listened. Her interest was not clinical science vs. anecdotal evidence. Her interest was personal. She talked, listened, compared stories. From several, she learned about a clinic that did not claim to cure cancer. It did not use medicines to treat cancers. But patients were cured, somehow. This clinic was not in Canada. It was not in the USA. She would have to go to Mexico to learn more.

There are lots of alternative treatment clinics in Mexico. Are some of them valid, using important techniques to cure cancers? Are some of them scams, wanting to take money from desperate clients? Do some of them have a cure that works sometimes, but might not work for her? Kate didn’t know. She did more research. She called the clinic.

The staff did not claim to cure cancer. Claiming to cure cancer is dangerous, even for a clinic outside of North America. They suggested Kate visit the clinic and see what happens there, no charge for a visit, but she would need to pay for her travel to Mexico. Kate had done her research. She had met and talked to patients whose cancers had disappeared.

Kate made her decision. She was familiar with cancer diagnosis techniques in Canada. She had undergone a physical examination, a mammogram, that detected a lump in her breast. Then she had a biopsy, where tissue was taken from the lump and was sent to a lab for analysis. The lab technician tested and examined the sample and issued a diagnosis “cancer” or “not cancer.” Once the diagnosis is issued, everybody swings into action. Kate knew that the mammogram had a high false positive rate and a false negative rate. Many people who are diagnosed with a “possible cancer” by a mammogram do not actually have cancer. She was also aware that cancer biopsies have a false positive rate and a false negative rate, as well. Her work in the hospital, with real patients, had made this very clear.

She didn’t really know for certain if she had cancer. Her surgeon, on the other hand, was still pressing her to schedule treatment.

Kate knew one thing. She had time. She cashed out some savings and booked a “holiday” in Mexico.

At the clinic, Kate was surprised that there was no “cancer diagnosis.” They did check the presence and size of the lump on her breast. But they didn’t repeat the biopsy. The clinic read her diagnostic reports, but did not investigate them further. There was instead a very thorough analysis completed by a suite of doctors. It took two full days of tests and interviews, if I remember correctly.

Kate was asked about her family’s medical histories. She gave blood samples. She was questioned extensively about her diet, about what she eats on a regular basis. What foods does she like and eat often. What foods does she not like and never eat. Doctors examined her lungs, her heart, liver, and other bodily organs with various tests. Her immune system was tested. Extensive interviews about her life, her work, her relationships, and more.

At the time I talked to Kate, I didn’t realize that she was not getting a “medical analysis,” she was actually getting a “healthicine analysis.” Her tests and questions fit perfectly to the hierarchy of healthicine: genetics, nutrition, cells, tissues, organs, bodily systems, body, mind, spirit, and community.

Kate’s genetics were analyzed through family history. There may have been further genetic analysis, I don’t remember all of the details. Her nutritional status was analyzed, not just by analyzing what she ate, and what she preferred to eat, but also by studying what she didn’t like to eat, what she deliberately never ate, what foods she believed she was allergic to. Her cells and tissues were analyzed directly, through blood samples and physical examination, and indirectly through medical history and other tests. Many of her organs were tested for healthiness. Her bodily systems, immune system, circulatory system, respiratory system, hormonal systems and more were analyzed and assessed. Her physical body was measured, weighed, and examined. Her mental health was assessed, as well as her spiritual healthiness. She was in good spirits, even in light of a potentially life threatening illness. Her community health was analyzed as well. Her family, her relationships with her children, her spouse, her parents, her work community, and more.

After a few days, Kate met with a group of doctors to discuss her health, not her illness, her healthiness. Diagnosing illness is difficult. Analyzing healthiness is more complex. It took several doctors and several hours for Kate to learn and understand what they had learned about her healthinesses and her unhealthinesses.

They then “prescribed” two weeks, if I remember correctly, of healthiness training, tailored to Kate’s specific situation. She spent the next two weeks at the clinic, learning to be healthier, not learning how to be “healthier in principle,” rather – learning what Kate needed to do to make her diet, her body, her mind, her spirits, and even her relationships with her communities healthier. She could not change her work community. But she could change how she reacted to and interacted with it – to improve her own health. After two weeks of learning at the clinic, her breast lump had started to shrink.

Kate went back to Canada, to put her learning into action. The lump disappeared. Her diagnosis was still there on paper. But her “cancer” had disappeared. She was retested at her hospital and no cancer was found.

Then Kate began to disappear.

When the surgeon asked again, she explained that she was not going to surgery. The surgeon looked away. He refused to look her in the eye after that.

But Kate didn’t disappear from her family. She went back to her family. She didn’t disappear from her job. She went back to her job. She disappeared from the cancer system. Her cancer disappeared, so, as a cancer patient, she disappeared.

Was she cured? We don’t know. There is no useful definition of a cancer cure. No medical or scientific test that can prove a patient has been cured of cancer. Our cancer treatment statistics have no count for people who are cured of cancer. Patients that are cured, whether they are cured with medicines or not, are not counted. No breast cancer patients are officially cured by medicine. If their cancer goes away without treatment, they disappear from statistics. If their cancer is killed by radiation, chemotherapy or surgery, they are not cured, they are a “survivor.” Everyone knows that cancer survivors are always waiting for the cancer to reappear. Their symptoms are in remission, but their cancer is not cured. They are not cured. With no proof of a cure, it might just be hidden.

Kate no longer has cancer. She paid, from her own pocket, for her trip to a clinic in Mexico. After the trip, her cancer disappeared. She had medical insurance. But her insurance wouldn’t pay for her trip. Insurance pays for treatments, not for cures. It pays for treatments, even if they fail. But it does not pay for success. Success disappears.

There are two ways for a cancer patient to disappear. You might be cured by health. Or you might be cured by a medicine that is not approved. In both cases, the medical system will ignore the cure, and ignore the patient.

In healthicine, there are no incurable diseases. If it is not curable – it is not a disease, it is a handicap, a disability, a deficiency, or simply an attribute of the person. All diseases can be cured by definition.

I have since met several cancer patients who have disappeared, and not just cancer patients. Maybe you have too? I’ve met more by internet, email, etc. There is no way for me to determine if a disappeared patient actually had cancer, if their treatment cured their cancer, if their body cured their cancer or if they still have cancer. We can only tell if there is another cancer diagnosis. Nothing can be told from the absence of a diagnosis.

There is no way for any doctor to tell either. There are no tests for a cancer cure. There is no way to recognize, much less document a cancer cure. There are no statistics for cancers cured.

Many cured patients don’t disappear quietly. They speak out. They write books and newspaper articles. They blog. But it doesn’t matter. They still don’t count. Once cured, they disappear. The medical system does not study their cases, does not study their diagnosis, does not study their cures. For chronic diseases, like cancer, arthritis, diabetes, heart disease, even obesity, and many more, there are no techniques to document “cured patients.” As a result, there are no statistics for “cured patients” of any chronic illness.

Once they are cured, they disappear. Health doesn’t cure illness, it disappears illness. And medicine doesn’t count people who have disappeared.

To your health

Red meat triggers toxic immune reaction which leads an increased risk for cancer!

Scientists at the University of California discovered that the human body views red meat as a foreign invader and launches an immune response

The body views red meat as a foreign invader which must be stamped out

The body views red meat as a foreign invader which must be eliminated immediately!

Red meat has been linked to cancer for decades, with research suggesting that eating large amounts of pork, beef or lamb raises the risk of deadly tumours.

But for the first time scientists think they know what is causing the effect. The body, it seems, views red meat as a foreign invader and sparks a toxic immune response.

Researchers have always been puzzled about how other mammals could eat a diet high in red meat without any adverse health consequences.

Now they have discovered that pork, beef and lamb contains a sugar which is naturally produced by other carnivores but not humans.

It means that when humans eat red meat, the body triggers an immune response to the foreign sugar, producing antibodies which spark inflammation, and eventually cancer.

In other carnivores the immune system does not kick in, because the sugar – called Neu5Gc – is already in the body.

Scientists at the University of California proved that mice which were genetically engineered so they did not produce Neu5Gc naturally developed tumours when they were fed the sugar.

“This is the first time we have directly shown that mimicking the exact situation in humans increases spontaneous cancers in mice,” said Dr Ajit Varki, Professor of Medicine and Cellular and Molecular Medicine at the University of California.

“The final proof in humans will be much harder to come by.

“This work may also help explain potential connections of red meat consumption to other diseases exacerbated by chronic inflammation, such as atherosclerosis and type 2 diabetes.

“Of course, moderate amounts of red meat can be a source of good nutrition for young people. We hope that our work will eventually lead the way to practical solutions for this catch-22.”

Red meat is a good source of protein, vitamin and minerals, but an increasing body of research suggests too much is bad for long-term health.

Health experts recommend eating no more than 2.5oz (70g) a day, the equivalent of three slices of ham, one lamb chop or two slices of roast beef a day

A study published by Harvard University in June suggested that a diet high in red meat raised the risk of breast cancer for women by 22 per cent.

In 2005 a study found those who regularly ate 5.6oz (160g) of red meat a day had one third higher risk of bowel cancer.

The average person in the UK has 2.5oz (70g) meat a day 3oz (88g) among men, 2oz (52g) among women) but 33 per cent have more than 3.5oz (100g) a day.

Previous research has suggested that a pigment in red meat may also damage the DNA of cells lining the digestive system.

The new research was published online in the journal, Proceedings of the National Academy of Sciences.

Ten Acidic Signs That Your Liver is Toxic and Sick!

liver-disease-s1a-did-you-knowLiver disease is any disturbance of liver function that causes illness. The liver is responsible for many critical functions within the body and should it become dis-eased or injured, the loss of those functions can cause significant damage to the body.  Liver dis-ease is also referred to as hepatic dis-ease.

Liver dis-ease is a broad term that covers all the potential problems that cause the liver to fail to perform its designated functions. Usually, more than 75% or three-quarters of liver tissue needs to be affected before a decrease in function occurs.

The liver is the largest solid organ in the body; and is also considered a gland because among its many functions, it makes and secretes an alkaline substance called bile. The liver is located in the upper right portion of the abdomen protected by the rib cage. It has two main lobes that are made up of tiny lobules. The liver cells have two different sources of blood supply. The hepatic artery supplies oxygen rich blood that is pumped from the heart, while the portal vein supplies alkalizing minerals from the large intestine and the spleen.

Normally, veins return blood from the body to the heart, but the portal vein allows alkaline minerals from the large intestines to enter the liver for “detoxification” and filtering prior to entering the general circulation. The portal vein also efficiently delivers minerals and fats that liver cells need to produce the proteins, cholesterol, and electrons required for normal body activities.

There are several early signs of  an acidic liver to understand in order to protect the liver and its many functions from sickness and dis-ease.
Without a fully functioning liver,  your health and wellbeing will be compromised.  Fortunately your liver is capable of repairing and renewing itself every six weeks.  Understanding the following acidic liver conditions and spotting them early,  will help to prevent and/or reverse a serious life-threatening degenerative live dis-ease.

livertoxicity

Warning Sign # 1 – Skin discoloration – Jaundice

One of the early signs of excess liver acidity and the beginning of liver dis-ease is the liver’s inability to filter out all of the dietary and/or metabolic toxins from the blood.  With a build-up of toxins this may also lead to a build-up of Bilirubin which is a breakdown product of the blood.  The breakdown of the blood which increases bilirubin is caused by an acidic lifestyle, diet, congested liver and gallbladder and constipation of the elimination organs,  The body and specifically the gallbladder uses bile  to help alkalize the food ingested coming out of the stomach.  When the body cannot evacuate Bilirubin from the liver/gallbladder and blood via the bowels, it will accumulate in the bloodstream and results in the skin taking on a yellowish hue.  This yellowing can also affect the fingernails, the tips of the fingers, and especially the eyes. This acidic condition caused by an acidic lifestyle and diet is known as Jaundice.  Read, share and like more:

Continue reading Ten Acidic Signs That Your Liver is Toxic and Sick!

The Dangers of Drinking Cow’s Milk

10527262_10152224047863317_4714492967142919885_n-1
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 prostate 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 millilitre 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 an 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!
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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!To learn more about other healthy alkaline food and drink choices read: The pH Miracle revised and updated by Dr. Robert O. Young.

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One of my favorite milks that I drink every day is our Green Milk which contains fresh organic almond milk with fresh organic greens of spinach, cucumber and celery.

How To Make Green Milk!

Click here: http://www.phmiracleliving.com/t-reci… to get ALL the new Fun Food Show episodes the day they come out (Only a few select cooking videos will be posted here on Youtube.)

To check our pH cookbooks click here: http://www.phmiracleliving.com/c-67-c…

For additional information on alkaline foods and drinks and the Green Milk recipe go to:

https://www.youtube.com/user/pHMiracleCenter

www.phmiracle.com

http://www.phoreveryoung.com

www.phmiraclebooks.com

http://www.phoreveryoung.wordpress.com

– 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.

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Reversing Autism With The pH Miracle Lifestyle and Diet

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The following is another unsolicited pH Miracle Testimony on reversing Autism from Tony Paterniti:

Our 21-year-old, severely autistic daughter (low-functioning) met Dr. Young last night. He spent some time connecting with her and sorted out the extreme crisis she had been going through for the past week – thrashing wildly about in apparent pain, with loud vocalizations and no sleep for a full week.

We applied his immediate suggestions, and by the time we got home at around 10 p.m. (the meeting was some distance from our home), she was quiet and still. Heading up to bed an hour later, we could see the exhaustion of the past week finally descending upon her, looking for rejuvenation – and knowing she would find it.

Elena slept peacefully through the night. By morning, it was clear that the serious gut issues Dr. Young had tuned in on had been cleared – at least for the moment. Clearly, we are now on a path with Elena that can only lead to more good, more health and greater well-being.

And for this, we feel extremely grateful and happy.

Blessings on you and on your assistants, Dr. Young – Especially during Elena’s time of extreme crisis, you were – and are – a godsend.

Tony & Ziek Paterniti

El suceso mas soprendente que ocurre en tu organismo es…

10858499_10204309099584119_528553348156452247_n

Que los jugos verdes o sangre de las plantas es casi identica en su estructura molecular a la sangre humana, por lo que es ideal para renovarla, es decir crear celulas madre sanas, siendo la materia prima para que la sangre pueda fabricar células madre corporales que solo nuestra madre naturaleza nos puede proporcionar.

El proceso de asimilación de los nutrientes y la fabricación de células madre sanas o cancerígenas ocurre en las criptas de las microvellosidades intestinales (villi) del yeyuno en el intestino delgado.

La diferencia entre fabricar celulas madre cancerígenas o células madre saludables depende de como es la calidad de lo que estas bebiendo y comiendo diariamente, es decir de la calidad de los nutrientes o desnutrientes.

Para aprender más sobre este interesante tema y conocer algunos de los estudios publicados en revistas científicas que avalan estas afirmaciones, te invito a que asistas a mis conferencias mensuales y adquieras la serie de libros de Robert y Shelley Young, “La milagrosa dieta del pH”, perder peso con la milagrosa dieta del pH y la milagrosa dieta del ph para diabetes (2015) de Ediciones Obelisco SL Ediciones Urano MéxicoEdiciones Obelisco Mex

The pH Miracle 14 Day Whole Body Cleanse – January 14th – 27th

pHMiracleRevisedandUpdated

We are excited to announce the next pH Miracle® 14 Day Whole Body Group Cleanse. Based on the science of Dr. Robert O. Young, pioneer of the “New Biology™” for over 3 Decades. Join us as we empower you to take your health to the next level.  

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The pH MIRACLE® 14 Day
Whole Body Cleanse


January 14th – 27th, 2015

 Our Group Cleanse consists of Daily Cleanse Classrooms and Nightly Calls with Expert Guest Speakers.

Hosted by: Glenn & Lori Stone & Brian Claypool

Enroll Now


Your Body is a MIRACLE!
It’s time to treat it like one.

The human body is a miracle designed to operate with effortless ease when its properly supported. Trillions of cells functioning and working in harmony together to support the miles of arteries, organs and tissues. Most take for granted all of these functions as they happen automatically without much conscious awareness on our part. They take better care of their cars and possessions than they do their own bodies. Health is our birthright but like all rights it requires responsibility. When we take the right actions we can correct imbalances and heal ourselves. The secret key to health is alkalizing energizing. There is nothing more important to health than the environment we create in our body. By supporting this alkaline design you allow your mind and body to function optimally. You are working with the bodies biochemistry, not against it. This is what happens when people adopt an alkaline lifestyle on the pH Miracle cleanse. Their bodies regenerate, heal and become stronger than ever. They achieve new levels of well-being they never thought imaginable, many eliminated pain and health challenges they have had for years. The testimonials continue to flood in from people throughout the world who are participating on the cleanse. If you are seeking to achieve more health, more energy, more balance and more wellness in any aspect of your life, the pH Miracle provides you with a powerful and proven program for attaining your God given potential. Join us now and transform your life by enrolling in the pH Miracle 14 Day Whole Body Cleanse. Give yourself the gift that keeps on giving.

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Lori, Glenn & Brian have over 17 years experience facilitating these cleanses for our alkaline community in the US and throughout the world. We are offering you an amazing opportunity to gain profound knowledge of the pH Miracle science, lifestyle and live-it program. We have also put together a list of many amazing expert guest speakers who will join us throughout the cleanse. These guests will all speak on a range of important holistic health subjects that will help you to accelerate your whole body detoxification, healing and more. The program itself is over 28 calls including daily cleanse classrooms and nightly calls. These calls are also recorded and archived for your convenience to listen to on your computer, smart phone or MP3 player at any time. Enroll Now and join us on this life changing experience.

This is just some of what you will receive when you sign up for this cleanse.

  • A 30 Minute Complimentary Coaching Call to discuss your products and individual requirements.
  • The Daily Cleanse Classroom where you can interact with other cleanse members,  instructors and get all of your questions answered.
  • Nightly Cleanse Call Including Expert Guest Speakers. Audio Recordings of each call will be provided.
  • Cleanse Companion 65 Page Ebook – Your Comprehensive Guide to the cleanse.
  • Personal Email Support – Email us anytime and we will respond ASAP during the cleanse.
  • *Enroll in the cleanse and receive 20% off the products on the pHMiracleCleanse.com website up until 1 month after the cleanse.
  • **Refer 2 People and Receive Your Cleanse 50% Off! Refer 3 People and Receive Your Cleanse Free!
  • Get a tremendous amount of support for the next 6 weeks, by listening to the complimentary calls and signing up for the cleanse.

Enroll Now

Complimentary Pre-Cleanse Kick-off Calls

Please join us for any or all of our complimentary kick-off calls prior to the next cleanse. During these calls we will  discuss the various ways to do the cleanse including the best ways to prepare, which products to use and how to get the most out of this life changing experience. We will also answer your questions at the end of the call.

OUR NEXT CALL:
This Sunday
12/21/14 @ 6pm PST 9pm EST

Remaining Calls

Sunday 1/4/15 @ 6pm PST 9pm EST
Wednesday 1/7/15 @ 6pm PST 9pm EST
Sunday 1/11/14 @ 6pm PST 9pm EST

Dial-in Number: 605-562-3140 (Subject To Change)
Access Code: 200013#

If you have any challenge with the above number, we have provided a backup number.
Back-up Phone Number: (559) 546-1400
Enter the Dial-In Phone Number & Access Code

For International Callers:

International Phone Numbers

To Call Online For Free On Your Mobile Devices:

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On the Complimentary Calls you will learn the following…

  • Learn how to prepare for the cleanse, what to look out for and what to do to get the most ouf of this life changing experience.
  • Learn the four choices to cleanse from a lifestyle shift to the complete liquid feast.
  • Learn which foods, drinks and supplements to move towards and which to move  away from.
  • Learn strategies on how to stay alkaline and maintain balance during the hustle and  bustle of modern living
  • Learn how to create healthy alkaline meals 70/30.
  • Learn how to naturally support your immune and lymphatic system while avoiding any of the flu like symptomologies.
  • Learn how to transform your mind body and soul into the alkaline way of living,  eating and thinking.

The cost of the cleanse is $454, which is a huge value considering all of the support and knowledge that you are going to gain during this period. You will receive more coaching, support and education than you ever have in adopting the pH Miracle alkaline lifestyle. We are currently offering an Early Bird Special Discount for $75 Off @ $379. This special ends on 12/31/14. Enroll Now and Transform Your Lifeyou’ll be so glad you did.

*Get 20% off all pHMiracleCleanse.com packs and products except for pH Strips, Oils & Books

**Referrals for Refer 3 Get Yours Free Program must enroll in the cleanse for you to receive free cleanse

Just a few of our many amazing Cleanse Testimonials…

Jane H.
You guys are amazing coaches and I am so glad that Tim and I chose to do this cleanse. We learned so much and feel and look so much better! I will join you again on the next cleanse. Thank you!!!
Mitzi M.
Most of my health challenges, including migraines and extreme vertigo, disappeared. I am thrilled to say that I lost 90 lbs. in the first 90 days! Almost two years later, I remain at a size 4/6 and love the simplicity of the program that keeps me at this size and in this state of health.
Leighanne D.
I just want to say how much of a gift to the universe you all are and I extend that to Dr Young. I cannot thank you enough for your energy, your passion, your knowledge, your love and for this opportunity to be your student. Words just do not express my gratitude to each of you.
Rosalie E.
I just want to let you know guys that I had a problem with my eyesight at night time. After a week of the cleanse, my eyesight has been much clearer and not needing my glasses at night time. I am able to drive without my glasses at night  Isn’t that amazing?!

Corinne F.
“You guys rock!”  That’s the way I feel about you three and this cleanse. I am learning so much from you all and your passion for this lifestyle is contagious!!?

This cleanse and information,  materials, documents, and products are not intended to diagnose, treat, cure or prevent any disease. Before starting this program please be sure to check with your physician or health care practitioner.

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To learn more about Dr. Robert and Shelley Young’s Science visit:
www.phoreveryoung.wordpress.com

Happy Thanksgiving – The Health Benefits of Pomegrantes

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Pomegranates are nearly round, 2-1/2 to 5 in. wide fruit crowned at the base by the prominent calyx.

The tough, leathery skin or rind is typically yellow overlaid with light or deep pink or rich red.

The interior is separated by membranous walls and white, spongy, bitter tissue into compartments packed with sacs filled with sweetly acid, juicy, red, pink or whitish pulp or aril.

In each sac there is one angular, soft or hard seed.

The arils (seed casings) of the pomegranate are consumed raw. The entire seed is eaten, though the fleshy outer portion of the seed is the part that is desired. The taste differs depending on the variety of pomegranate and its state of ripeness.

Pomegranate juice is a popular drink in the Middle East, and is also used in Iranian and Indian cuisine; it began to be widely marketed in the U.S. in 2004. Pomegranate concentrate is used in Syrian cuisine. Grenadine syrup is thickened and sweetened pomegranate juice; it is used in cocktail mixing. Before the tomato arrived to the Middle East, grenadine was widely used in many Persian foods; it can still be found in traditional recipes. The juice can also be used as an antiseptic when applied to cuts. In addition, Pomegranate seeds are sometimes used as a spice.

The primary commercial growing regions of the world are the Near East, India and surrounding countries and southern Europe. In California commercial cultivation is centered in the southern San Joaquin Valley.

One pomegranate delivers 40% of an adult’s daily vitamin C requirement. It is also a rich source of folic acid and of antioxidants.

Recent research into the health benefits of Pomegranates has created unprecedented demand both in the United States and Europe. Recent studies have been published showing a positive relationships between pomegranate consumption and prostate cancer, carotid arteries and hypertension.

A Natural Healthy and Legal Way To Increase Blood Volume – Pass It Along To Lance

There were several questions that came to mind after watching the Oprah Winfrey and Lance Armstrong interview where Lance finally admitted to using EPO, human-growth hormone, testosterone and blood doping.

So What is Blood Doping?

Blood doping is an illicit method of improving athletic performance by artificially boosting the blood’s ability to carry and deliver more oxygen to the connective tissues, including the muscules.

In many cases, blood doping increases the red blood count and its main oxygen carrying molecule, hemoglobin.  So, increasing hemoglobin allows higher amounts of oxygen to reach and alkalize an athlete’s muscles.  This can improve stamina and performance, particularly in long-distance events, such as long-distance running and cycling.

Blood doping is banned by the International Olympic Committe and other sports organizations.

What Are Types of Blood Doping?

The three widely used types of blood doping are:

1) Blood transfusions
2) Injections of erythropoetin (EPO), and 
3) Injections of synthetic oxygen oxygen carriers.

Here are some more details about each of these types of blood doping:
Blood transfusions.  In normal medical practice, patients may undergo blood transfusions to replace blood lost due to injury, surgery or chemotherapy. Transfusions also are given to patients who suffer from low red blood cell counts caused by anemiakidney failure, cancer and chemotherapy treatments.
Illicit blood transfusions are used by athletes to boost athletic performance. There are two types.
Autologous transfusion. This involves a transfusion of the athlete’s own blood, which is drawn and then stored for future use.  Most commonly this involves the removal of two units (approximately 2 pints!) of the athletes blood several weeks prior to competition. The blood is then frozen until 1-2 days before the competition, when it is thawed and injected back into the athlete. This is known as autologous blood doping.
Homologous transfusion. In this type of transfusion, athletes use the blood of someone else with the same blood type and then injected straight into the athlete.
EPO Injections

EPO is a hormone produced by the kidney. It regulates the body’s production of red blood cells.  In medical practice, EPO injections are given to stimulate the production of red blood cells. For example, a synthetic EPO can be used to treat patients with anemia related to chronic or end-stage kidney disease or cancer and its treatment with chemotherapy.
Athletes using EPO do so to encourage their bodies to produce higher than normal amounts of red blood cells, hemoglobin and blood volume called hematocrit to enhance athletic performance.
Synthetic Oxygen Carriers 

These are chemicals that have the ability to carry oxygen. Two examples are:
  • HBOCs (hemoglobin-based oxygen carriers)
  • PFCs (perfluorocarbons)
Synthetic oxygen carriers have a legitimate medical use as emergency therapy. It is used when a patient needs a blood transfusion but:
  • human blood is not available
  • there is a high risk of blood out-fection (A blood outfection is when the blood is breaking down due to metabolic and/or dietary acids or from acidic drug use.)
  • there isn’t enough time to find the proper match of blood type
Athletes use synthetic oxygen carriers to achieve the same performance-enhancing effects of other types of blood doping: increased oxygen in the blood carried by the hemoglobin in red blood cells that helps reduce tissue acidosis in the connective tissues and muscles.  This results in reduced tissue or muscle breakdown and tissue acidosis that causes inflammation and pain.

So what could have Lance Armstrong done differently to achieve athletic superiority in his sport without drugs and blood fransfusions? And, how could have Lance Armstrong naturally increased his red blood cell count, hemaglobin and hematocrit and in turn increased his VO2 or oxygen volume to his connective tissues and muscles thus minimizing acid build-up and cellular breakdown, without taking hormones, steroids, EPO and blood transfusions known as blood doping?

Having been a professional athlete myself I have been doing natural blood doping successfully for myself (My blood counts run consistently – RBC count 5.2 million/mcL, Hemoglobin 17.2 g/dl, Hematocrit 53%, White Blood Count 3.8 thousands/mcL, Platelet Count 156 thousands/mcL, Glucose 80 mg/dl, Sodium 146 mEq/L, Chloride 106 mEq/L, Potassium 5 mEq/L, and Calcium 9.8 mg/dl, just to name a few of the most important markers in the blood), other athletes (including Professional and Olympic athletes) and cancer patients around the World for years with NO negative side-effects.

IT IS SIMPLE – IT IS SAFE – IT IS NATURAL – IT IS SMART and IT IS LEGAL!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!!! No side-effects except for increased health, energy and vitality.

Pass this on to Lance Armstrong?

Here is the formula for natural blood building without medical drugs, hormones, steroids, or blood transfusions (based upon 70kg body):

1)  Drink 250ml of pH Miracle liquid Chlorophyll.  Chlorophyll is the concentrated blood of green plants and is identical to human hemoglobin except for the center atom of magnesium in chlorophyll.  Drinking the blood of green plants will increase hemoglobin in less than two weeks.

2)  Drink 6 liters of pH Miracle Greens with 5 drops of the puripHy per liter.  The pH Miracle greens contains concentrated (28 to 1 concentration) grasses, fruit and vegetables that will increase red blood cell count and blood volume as indicated on a Comprehensive Blood Count Test.  The pH Miracle puripHy drops will increase the pH of the green drink and help to buffer metabolic and dietary acids that break down connective tissue and weaken muscles.

3)  Ingest 16 portions of alkalizing green fruit and vegetables.  Ingesting liberal amounts of green fruit and vegetables daily will help to maintain the high levels of red blood cells, hemoglobin and hematocrit.

4)  Drink 100ml of the pH Miracle Omega 3, 6 and 9 oil.  The ingestin of polyunsaturated oils from hemp, borage and flax will provide the necessary lipids for building the membranes of stem cells and blood cells and keeping them strong.

5)  Ingest 1 scoop of pHour salts in the morning, 1 sccop at night and 1 scoop any time the pH of the urine drops below 7.2.  The pHour salts contain four foundational mineral salts for the purpose of maintaining the alkaline design of the body fluids and reduce and/or eliminate the metabolic and respiratory acids that build-up during strenuous exercise such as carbonic acid and lactic acid.

6)  Spray the pHlavor salts orally to replace electrolytes and reduce the acids that create lightheadedness, dizziness, cold hands, cold feet, poor circulation, low energy, just to name a few symptoms of low mineral salts.

7) And, finally take 2 scoops twice a day of the pH Miracle L-Arginine Max to improve blood and lymph circulation by breaking up acidic mucous, plaque, calcifications, and cysts in the blood, lymph and connective tissue.

When an athlete follows the above recommendations based upon my clinical research for over twenty years he or she will consistantly show increases in their red blood cell count approaching or exceeding 5 million/mcL, hemoglobin increases approaching or exceeding 15 g/dl, and hematocrit increases approaching or exceeding a volume of  50 percent or higher.

The following article suggests other incredible benefits for eating and drinking daily green fruit and vegetables:

http://articlesofhealth.blogspot.com/2013/01/another-reason-to-eat-and-drink-your.html

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