[geocentrism] Cancer
- From: "philip madsen" <pma15027@xxxxxxxxxxxxxx>
- To: "geocentrism list" <geocentrism@xxxxxxxxxxxxx>
- Date: Sat, 2 Jun 2007 09:27:47 +1000
Those given the grace to know TRUTH , know that all the sub conspiracies and
lies et al are from one basic all incompassing conspiracy, under Satan, and the
money power. This elitist family group pull every string. I truly believe that
their operating rule book is the protocols.
Yet the one conspiracy most shocking in pure human terms, driven by greed under
the pretext of health, is the suppression of the natural reason for and control
of cancer. We are aware of the suppression of all forms of natural health, to
get it all under the drug cartel umbrella, but no effort and no amount of
repression and suppression is equal to that which has been mounted against
Laetrile. Not only is the manufactured drug made illegal, but even the sale of
the primary natural source, the simple apricot kernel was legislated against
almost world wide. People have been put in jail over it. Yet a world of quack
cures, where many die in a final attempt for life is allowed to exist with
little or no suppression.
Was it just because a private non-cartel independent pharm company discovered
and patented it? They claim its because its a poison and will kill you, yet
they have no problem with terminal patients seeking euthaniasia? My challenge
still stands, and is ignored. I will eat ounce for ounce crushed apricot seed
if one of them eats the same quantity of common salt. And thats every day. not
just a oncer. Just see who gets sick.
For those not frightened to venture into the world of conspiracy, within
another branch of science , ignored, but not minor, where the real nature of
cancer and its control has been known since 1918.... I place here an article
in its technical detail.. from my archives. It covers the complete mechanism,
and is important to those who may NEED to use it. Notice, laetrile is just part
of the picture. Don't jump through it the second time.. learn it till it comes
natural.
Immuno-Enzymatic Therapy: A review of the Literature
(Work in progress: 9/1/04)
By Roger Scott Cathey
An overview on digestive enzymes
All enzymes accelerate reactions, or even permit reactions that otherwise would
not happen, while the enzymes themselves end up unchanged. Enzymes therefore
are catalysts and can act over and over again doing the same thing. Inorganic
catalysts, such as platinum, are not specific, while most enzymes are highly
specific. A common saying in biochemistry is: one enzyme, one reaction. Thus
proteases are specifically directed to proteins, glucosidases attack sugars,
lipases attack fats, etc. While in some cases a single enzyme may attack only a
single bond in a single molecule amongst a variety of substances of the same
type, others may attack several different molecules with the same type bond in
a category. An example is a sulferase, which only attacks sulfur bonds, while a
protease may attack several different amino acids in a protein.
In most cases enzymes have names that end in -ase. There are a number of
exceptions: pepsin, trypsin, chymotrypsin, emulsin (beta-glucosidase), etc.
These are archaic terms now well entrenched in the nomenclature, but the
standard today is that all enzymes end in -ase.
Each digestive enzyme acts upon one substance at a time. The substance acted on
is termed a substrate. Thus an enzyme first encounters a substrate to form an
enzyme-substrate conjugation. After reaction, the enzyme is left intact and
there is now an altered substrate. In the case of the enzymes we are going to
discuss, reactions result in two parts of substrate per enzyme-substrate
reaction. Thus they may be termed "cleaving" enzymes.
These enzymes can be very efficient. Consider this: although acting on only one
substrate at a time, the enzyme carbonic anhydrase releases about 600,000
molecules of CO2 per second, thus 36 million per minute. Catalase can in one
minute decompose 2,600,000 molecules of hydrogen peroxide per minute at 32
degrees Farenheit (0 degrees Celsius). This turnover number equates to about
430,000 reactions per second. These are, of course, far greater reaction rates
than most other enzymes possess, but all the enzymes we will be discussing can
process hundreds to thousands of reactions per second. Trypsin for example has
a turnover number of 138 peptide bonds hydrolyzed per second. Amylase: 18,000
hydrolyzed carbohydrate bonds per second. The slowest enzyme known is lysozyme
with two reactions per second.
Of the six broad classes of enzymes that exist, we are going to discuss here
only HYDROLASES: enzymes that divide a substance by the addition of water. This
of course requires the splitting of water into two parts and represents one of
the reasons abundant water consumption in enzymatic therapy is so important.
The way substrates are digested by enzymes is beautifully simple: some part of
a length of protein (or carbhohydrate or fat) fits into a specific site or
pocket on the enzyme. Within this comformable pocket is a niche called the
active site where the actual reaction or cleavage takes place. This mutual fit
between enzyme and substrate is often compared to a key in a lock. We might say
it is more like a baseball in a mit, wherein the mit can move or shape itself
to hold the ball, for we know now that enzymes are flexible and plastic during
their functioning, and for an enzyme to function properly, it must be flexible.
Thus an enzyme attaches, undergoes flexure thus straining the substrate, and a
bond is broken in the substrate.
While a portion of the substrate is in the enzyme "pocket", the enzyme
typically binds with some atom on the substrate, and at the same time
surrenders an atom to the substrate. The part of the substrate bound to the
enzyme is then surrendered and thus the enzyme is released at the same time the
substrate pieces are. This process means the enzyme must re-acquire the atom it
surrendered to the substrate, which means absorbing some free radical like a
proton (+H)ydrogen or a hydroxyl (-OH) from water.
Many enzymes require helper molecules to aid in changing their shapes to
facilitate either grabbing onto the substrate or releasing it after having
hydrolysed it. Such factors can be vitamins, minerals or simple molecules. Such
molecules may attach only after the enzyme-substrate molecule is formed. Other
co-factors or co-enzymes must be present to facilitate attachment to the
substrate.
This is why some vitamins are also called co-enzymes, specifically the B
vitamins. These adjunctive, facilitating and helper factors must all be
considered or supplied in successful immuno-enzyme therapy.
All enzymes with few exceptions are proteins. A proven exception is RNA, a
nucleic acid responsible for creating proteins from DNA. Some research seems to
indicate that DNA also has enzymatic properties, and perhaps more surprising, a
single amino acid, proline, also seems to behave like an enzyme (Internet, 1).
Otherwise we refer to enzymes as part of the total protein product of active
cells. DNA is nothing but a record of proteins. Proteins are the only output of
nucleic acids (aside from more DNA or RNA). A special RNA is sent forth from
the nucleus to bind to amino acids which are constructed into proteins. It is
suspected that most of the proteins encoded on DNA are enzymes.
A conservative estimate of the protein content averaged over all cells in the
human body, excluding structural proteins, is 10 per cent of mass. If .01 per
cent of this were enzymes, each cell may contain 1000 enzymes (Sumner and
Somers, 1943,p. 4). Each cell produces enzymes according to need. For example,
if a cell is cultured in the absence of galactose, it may only contain 5
galactosidase enzymes. If a galactoside sugar is introduced in high quantity, a
new assay may reveal that the cell now contains up to 4,000 copies of this
enzyme. This feedback mechanism of protein expression is called induction or it
could be termed adaptative expression (internet, 20).
Proteins are made up of individual amino acids. Humans use about 20 amino acids
for protein synthesis. Nine of these are essential, and must be in the diet.
The other eleven can be synthesized from the essential amino acids. A general
consensus defines a protein as having 30 or 40 amino acids linked together. Two
amino acids would be a di-peptide. Three a tri-peptide (like glutathione).
Short chained peptides are sometimes referred to as oligo-peptides (3 to 10
amino acids). Longer chains are polypeptides.
The term amino refers to the presence of nitrogen. The general formula for an
amino acid is HNCHRCO2. The R (radical) refers to the distinguishing groups of
atoms attached to the amino group.
An amino acid is characterized as a central carbon (alpha carbon) bearing an
amino group (nitrogen bound to two hydrogens), a hydrogen, an acid group
(carboxyl COOH) and a side chain (R). It is the R-groups or side chains that
distinguish one amino acid from another. Amino acids are bonded between the
carboxyl or acid group of one to the nitrogen (amine) group of another. The
distinguishing characteristic of proteins from sugars is the nitrogen atom and
the side chains attached to amino groups can contain such molecules as sulphur
which play a role in protein folding.
Free Amino Acids and Chromium GTF (Glucose Tolerance Factor)
In enzyme therapy, especially in late stage cancers, it is vital that free
essential amino acids be provided to allow the synthesis of new enzymes. Part
and parcel to such synthesis is the necessity for the health of the whole
pancreas. The pancreas has two major functions: production of insulin
(endocrine pancreas) and the production of the digestive enzymes (exocrine
pancreas). A very important role of insulin is the attachment to free amino
acids for delivery to the pancreas and other systems in the body. The specific
mineral that allows insulin to bind to these amino acids is chromium 3+, or
glucose tolerance factor (GTF). The body preferentially utilizes chromium
nicotinate for this function, not picolinates. This is a very important
distinction in chromium supplementation. All of our enzyme preprarations
contain GTF, or chromium nicotinate. Other minerals proved to be important for
endocrine pancreas health are magnesium, vanadium, zinc and manganese.
Polypeptides and proteins spontaneously fold into complex three-dimensional
configurations, forming internal cross-linkages or bonds. While the particular
amino acid sequences in a protein are important, most of any protein's active
properties comes of this folded shape. When functional proteins, like enzymes,
lose this folding they are said to be denatured, and will not perform their
function.
Most enzymes are made up of more than 100 amino acids, but some may consist of
thousands of amino acids.
Pancreatic Enzymes
The primary digestive enzymes are classed into four main groups:
Carbohydrases
Proteinases or proteases
Lipidases or lipases
Nucleases
Carobhydrases
Amylase
The first acting enzyme of the body in digestion is amylase, a carbolytic
hydrolase, secreted primarilly by the salivary glands and pancreas. In the
mouth it begins working on carbhohydrates, releasing maltose and a little
glucose and dextrins.
Carbohydrates are characterized chemically as consisting of polysaccharides, or
many sugar units. The most basic formula for sugars is a polymer of Carbon,
Hydrogen and Oxygen molecules (CnHnOn). The most basic sugar molecule is
glucose (C6H12O6). Two sugar molecules are termed a di-saccharide, three a
tri-saccharide, then oligo-saccharides (3-10) and polysaccharides. Complex or
Branching polysaccharides such as glycogen are typical storage forms of sugar
in the human body. Amylase does digest glycogen somewhat, but the principle
enzyme that attacks glycogen is phosphorylase, a liver enzyme that breaks down
glycogen in the presence of phosphate to form glucose-1-phosphate or Cori
Ester.
Salivary amylase is known to continue acting in the upper part of the stomach
before the pH drops drastically. At low pH, (acid) the enzyme is denatured, or
unfolded as noted above, unless protected by special coatings (enterically
coated) or involved in food boluses that protect the enzyme from denaturation
and digestion by pepsin.
This suggests another possible benefit of high fiber in our dietary. The human
body does not digest fiber, not possessing the enzyme cellulase. Fiber
conglomerations could conceivably absorb these enzymes along with water, later
releasing them again in the intestines or colon where they may play a role in
colon health. For this reason, our formulations do not contain cellulase, the
enzyme that digests fiber.
Enteric coatings are such as to prevent dissolution of the tablet in the low pH
of the stomach, but such coatings are dissolved by the alkaline environs of the
small intestines.
Recent studies have shown that this unfolding or denaturation of ingested
proteins by low pH is reversible when the pH is raised again, as it is when the
food passes into the small intestines. This presumes that the protein chain
comprising the enzyme is not cleaved by pepsin. In other words, that the enzyme
itself is not attacked by the pepsin enzyme in the stomach.
Because of the presence of foods to act as interferrance in the dance of these
proteins with each other, amylase may survive digestion in the stomach, and
whole denatured amylase may renature in the small intestine. Presumably,
amylase taken on an empty stomach will simply be digested at the various amino
acid-linkages susceptible to pepsin action. Therefore, for people using
non-enteric coated enzymes, it might be wise to also use an antacid like
magnesium oxide. This will raise the pH, deactivate pepsin, and allow the
amylase to pass unaltered into the small intestines. Ant-acids with aluminum
should be avoided. In 1925 Sherman, Caldwell and Naylor showed that amino acids
had a protective effect on amylase. One could take them with amino acids,
antacids and soluble fiber when lacking enteric coated forms. For this reason,
none of our preparations contain the enzyme cellulase, which breaks down fiber.
Many formulations do contain this enzyme because they derive their enzymes from
micro-organisms or molds. Dr. Nicholas Gonzalez, who is an expert on
immuno-enzyme therapy in cancer, has found that the animal derived enzymes are
the most effective enzymes in cancer therapy. The human body only produces
amylase in the alpha form. Plant amylases can be found in both alpha and beta
forms (they attack both alpha and beta linkages in carbohydrates). However, the
proteolytic enzymes derived from papaya (papain) and pineapple (bromelain) have
shown good supportive function in immuno-enzyme therapy, and we use these
enzymes as well.
The optimum pH range of pancreatic amylase is between 6.78 to 7.2, but
continues to act in higher pH.
Calcium ions are necessary for activation of amylase (Dixon, Webb, 1979).
Electrolytes, chlorides and iodides increase amylase activity, while fluorides
decrease it (Sumner and Somers, 1943). On this basis alone, one should avoid
using fluoridated toothpastes. Such toothpastes or fluoride drops or teflon
coated pans or other sources of fluoride should be avoided during enzyme
therapy (more on this under enzyme inhibitors to avoid).
Amylase is regularly found in the active state in plasma of the blood. The
origin of all blood plasma amylase has not been fully delineated. Some say
amylase in the blood stream is from an internal deposition from the pancreas
directly to the blood, some say it is from the salivary glands. Some is known
to be pancreatic enzymes reabsorbed from the small intestines
(entero-pancreatic circulation), and it is also known that oral supplemented
amylase is also absorbed from the intestines (Seifert, 1986). Studies indicate
that re-absorption of pancreatic amylase is preferred over plant amylases
(Santillo, 1993). Most of plasma amylase is from the pancreas. Probably all
these means contribute to the plasma total amylase pool. Physiologists have not
understood its purpose in the blood, but from the perspective of enzyme therapy
in cancer, it is seen to serve partly as an anti-cancer surveilant factor,
which we will discuss in detail below. It is likely that such exportation of
amylase via the parenteric pathway is partly involved in deriving energy from
glycogen stores. Amylase is used by various white blood cells in digesting
pathogens and cellular debris.
Other carbohydrases are produced in the body of significane in immuno-enzyme
therapy include: beta-glucosidase (saliva, lysosomes, gut, food sources)
lysozyme (tears, nasal fluid, lysosomes), beta-glucuronidase (liver, spleen),
beta-galactosidase or lactase.
The Proteinases or Proteases
The chief pancreatic proteinases are trypsin, chymotrypsin, the
carboxypeptidases and elastase.
Trypsin digests amino acid complexes only at specific linkages involving
arginine and lysine. Trypsin is a chromium 3+ (trivalent chromium) containing
enzyme. So important is Chromium to trypsin function, that its absence reduces
trypsin to merely 5 per cent of its normal catalytic potency (Saner, 1980). It
should be pointed out again that chromium supplements should be taken in the
form of nicotinates or niacin bound form. An ideal food source is brewer's
yeast, which carries the form dinicotinic acid glutathione chromium.
Picolinates have been shown to induce damage to the genes (Tufts University,
1996; USDA, 1996; George Washington U, 1995), and other forms of chromium,
chelates or citrates have to be converted to nicotinates to function ideally.
Chymotrypsin attacks linkages involving tyrosine, phenylalanine, and
tryptophan. These same bonds are attacked by pepsin. But pepsin is only active
in the highly acid environment in the stomach, and becomes inactive in the
small intestine.
Carboxypeptidases. These are zinc containing enzymes. There are two different
carboxypeptidases secreted by the pancreas: Carboxypeptidase A and B. The A
type cleaves hydrophobic (water shunning) amino acids on the carboxy-side; the
B type cleaves basic amino acids (Lysine and Arginine) at the carboxy-side of a
polypeptide or protein. Together carboxypeptidases cleave amino acids one by
one from any chain beginning at the carboxy terminal end of the chain. They are
perhaps the most important of the proteinases for this thorough property.
Mast cells make homologues of trypsin (tryptase) and chymotrypsin (chymase),
and one makes a carboxypeptidase. (Internet, 3)
Elastase hydrolyses peptide bonds on the carboxyl side of uncharged amino acids
such as those of alanine, serine and glycine.
Trypsin, chymotrypsin, and elastase are also called endopeptidases because they
cleave peptide bonds within the protein length. Carboxypeptidases are called
exopeptidases because they cleave peptide bonds from one end of the protein
length (the carboxyl termini).
Fat Digesting Enzyme or Lipolytic enzymes
Lipids are characterized by long chains of carbon appended with hydrogens, and
an acid terminus (COOH). These chains are called fatty acids. The hydrogen
saturated terminus is called the methyl or omega end, and the acid end is
called the carboxyl group. Fatty acids are usually bonded in threes to glycerol
to form a tri-glyceride. When a phosphate is attached to glycerol, a
phospho-lipid is formed, and thus possesses only two fatty acids. Such
phospholipids are constituents in cell membranes and the phosphate may be
bonded to other functional groups.
Lipase hydrolyzes the fatty acids off the 1 and 3 positions of food
triglycerides to produce 2 free fatty acids and a monoglyceride. The
monoglycerides are directly absorbed. Co-lipase is also secreted and prevents
bile salts from inhibiting lipolysis of triglycerides. It binds with lipase in
a 1:1 ratio, and brings lipase to the surface of lipid drops covered by bile
acids. Bile salts solubilize the lipids, while bile acids permits the water
soluble enzymes to act on the lipids at water-oil interfaces of the tiny
globules. Thus bile is a form of detergent and the globulization is called
emulsification that greatly increases the surface area of the lipids for
thorough digestion.
Phospholipase A hydrolyzes the fatty acid off the 2 position of lecithin and
phosphatidyl ethanolamine.
Cholesterol esterase breaks down cholesterol.
Nucleases.
Ribonuclease and deoxyribonuclease hydrolyze liberated nucleic acids (RNA and
DNA) into their component nucleotides.
As noted above, all these enzymes are hydrolases, meaning they insert water or
terminate divided chains with a hydrogen on one side and a hydroxyl or -OH on
the other.
The Enzymes in Cancer Therapy
From these observations and those which are to follow, it will become evident
that the gamut of pancreatic enzymes are important in cancer therapy, as cancer
cells and their products consist of all the designated substrates of these
enzymes. Naturally one may wonder how intestinal or ingested enzymes could
apply to cancers other than those in the stomach or intestinal tract.
Systemic Enzymes and Intestinal Enzyme Absorption
Pancreatic and food enzymes are absorbed into the blood and lymphatic
circulatory systems from the intestines. Many studies have been conducted
showing that pancreatic and food derived or supplemental oral enzymes are
absorbed from 12 to 20 per cent (Seifert, 1990); other specialized formulations
have been reported as having up to 40 per cent absorption (Lopez et al. 1994).
That this re-abosorbtion is not contested, that they may be re-absorbed by the
pancreas itself is contested. We do not believe that the pancreas re-absorbs
its own enzymes, rather, the systemic circulation of these enzymes is what is
important and a proven fact. It is in this systemic circulation we see an
immunologic role for the pancreas.
Consequently, these enzymes become systemic or circulating enzymes, and any
digestive action by them in the system is referred to as "parenteral"
digestion, to distinguish it from enteric digestion or digestion in the
alimentary canal or digestive tract.
In the system, these enzymes are weakly inhibited by circulating macroglobulins
(except amylase). These macroglobulins (especially alpha-2-macroglobulin) are
transport and regulatory molecules derived from the monocytes and macrophages
of the immune system. They deliver and regulate cell messengers (cytokines). In
the presence of a suitable substrate, the enzymes can separate from these
delivery molecules and digest the substrates (Gebauer et al., 1993). This is
proven by the fact that the circulating substrates are degraded and their
products are observable in the urine and by blood analyses.
The Pancreas a component of the Immune system
From the data collected from numerous clinical and labratory studies on the
systemic or parenteral role of the pancreatic enzymes or their homologues
(enzymes similar to pancreatic enzymes but from other sources), we can say that
the pancreas and its enzymes are a true component of the immune system. For
this reason, this form of treatment is sometimes called immuno-enzyme therapy.
The Cause of Birth and its relation to Cancer Control and Remission
Early in this century the embryologist John Beard reasoned that the same
mechanisms the body uses to reject the placenta, thus causing birth, must also
apply in cancer therapy (Beard, 1911). His reasons for thinking this began with
his observation of the striking similarities of behaviour and appearance
betweem placental cells and cancer cells. One is normal to the life cycle, the
other an aberration. The placental cells are called TROPHOBLAST cells.
The placental or trophoblast cells in pregnancy are characterized as being rich
in one or both subunits of a hormone called human chorionic gonadotropin or
hCG. This hormone is the basis of the standard pregnancy test.
Trophoblast cells are the first differentiated cells after creation of the
zygote in reproduction. Once these cells make contact with the uterous, they
express special adhesion molecules (oncofetal fibronectin), begin digestion and
erosion of tissues, rapid expansion, fusion with normal cells, inhibition of
certain body hormones and enzymes, expression of new ones: hormones to develop
new vascularization (Vascular Endothelial Growth Factor or VEGF); enzymes to
digest body cells and connective tissue, and they form metastases. Trophoblast
or placental cells are commonly found in the mother's lungs, liver and even the
brain. But after birth, all these metastasized cells are either already dead or
quickly consumed.
Beard observed that after the 56th day or so of pregnancy, the cellular
trophoblasts stop growing. In fact they begin to regress and differentiate to
more benign forms. At this time in pregnancy the onset of morning sickness also
occurs. Beard saw that this coincided with the activation period of the fetal
pancreas. Beard reasoned that the combined digestive action of the fetal
pancreatic enzymes and the maternal systemic pancreatic enzymes marks the onset
of the degradation of the placental or trophoblast cells. Even so, it will
recquire 7 and a half more months for this digestion to progress to the point
that the mother's body lets go, and the baby is born. By that time the
placental trophoblasts are practically all benign.
The Unitarian Basis of all Cancers
Like the placental or trophoblast cells, the cancer cell is also characterized
by being rich in human chorionic gonadotropin beta (hCG-Beta) (Acevedo et al.
1995). This hormone, a glyco-protein, is built into the cancer cell surface,
and is also secreted into the system to varying degrees in different cancers.
Its ostensible purpose structurally is presumably to protect the cancer cells
from attack by the immune system and systemic proteases, just as pregnancy
trophoblasts use hCG to preserve themselves and to preserve the swollen uterine
tissues from digestion by body proteases.
Cancer utilizes all the same mechanisms for survival that a developing placenta
uses in pregnancy: expression of oncofetal fibronectin, digestion and erosion
of tissues, rapid expansion, fusion with normal cells; inhibition of certain
body hormones and enzymes, expression of new ones, hormones to develop new
vascularization (Vascular Endothelial Growth Factor or VEGF), enzymes that
degrade body tissues, and the formation of metastases.
All the factors needed to accomplish these ends by the cancer cell are subject
to digestion under appropriate circumstances by the systemic pancreatic enzymes
and their homologues, including digestion of the entire cancer cell itself.
This unity between trophoblasts and cancer is what Beard perceived way back in
1900. The susceptibility of cancerous tissues to these enzymes that are so
important in pregnancy were Beard's test for cancer: if a living tissue reacts
to these enzymes or are digested by them, it must be cancer. Normal live
somatic tissues are not digested by these enzymes. Beard's thesis became the
basis of what is known today as the Unitarian basis of all cancers.
The Definitive Cancer biomarker: hCG
hCG beta is unique to only one natural component of the life cycle: placental
cells or trophoblasts. Outside of pregnancy, hCG is a cancer biomarker.
Trophoblasts appearing outside pregnancy are cancer. Because all cancers
display hCG, all cancers are defined as trophoblastic, and this single datum
proven by the strictest principles and methods of science, transformed Beard's
original thesis to the unitarian fact of cancer.
However, hCG is not the only defining factor. There are dozens of other
properties shared between normal pregnancy trophoblasts and cancer cells of all
types but not by normal cells. This broad spectrum of "onco-" traits between
pregnancy trophoblasts and cancers is defining when it comes to therapy. For
whatever is at work in causing birth (or abortion) by action on trophoblasts
will most likely also work on cancer.
hCG: cancer's defensive hormone
As the term "glyco-protein" suggests, hCG is part protein, part carbohydrate.
hCG is found in all cancers, in part or as an entire molecule. Two major
components make up hCG, both of which are glyco-proteins: Alpha hCG and Beta
hCG. When combined, it is called hCG-holo (whole). These parts are termed
"moieties".
Because trophoblast cells normally only arise from the zygote which is the
primary truly totipotent cell (cells that can produce all tissues: body tissues
and placental tissues), it follows that if cancer appears in the body, it
suggests the presence of totipotent cells in the body, or stem cells. There is
an abundance of research over the past 50 years that confirm the presence of
totipotent cells (stem cells), most recently studies at the University of
Michigan (Al-Hajj M, et al., 2003, and internet,17 and 18). We now have a means
of identifying such totipotent cells by isolation of a specific gene
responsible for unlocking these potentials (Tir non Og set or nonog cluster)
(Internet, ).
As a secretion, hCG has been recognised as a potent enzyme inhibitor (Milwidsky
et al. 1993). Because hCG affects the serine enzymes such as trypsin,
chymotrypsin, urease, etc., hCG is called a SERPIN (serine protease inhibitor).
However, it doesn't just inhibit proteases, for it is well known as an
inhibitor of the enzyme rhodanese, the enzyme responsible for detoxifying
cyanide. The importance of this fact will be realized further on when we
discuss in detail the process of reactivating inhibited enzymes.
In pregnancy, besides acting as a hormone inhibitor (for preserving the uterine
lining) hCG probably protects the uterine tissues by inhibiting the body
enzymes which digest those uterine tissues and which digestion causes the
expression of blood in the period.
A Two step Defensive Attack against hCG
Amylase is accentuated in our formulations because of its role in cleaving the
carbohydrates from hCG, deactivating it as a hormone on one hand; while also
helping towards unraveling of the cancer cell itself. We also believe it plays
a role in re-activating the hCG-inhibited serine enzymes trypsin, chymotrypsin
and carboxypeptidase.
It is believed that hCG sugars probably act on the enzyme away from the active
site as a noncompetitive inhibitor. Amylase can cleave the carbohydrate moiety
from the protein part of the hCG, perhaps permitting the protein product to
leave the enzyme or at least permit the enzyme to regain some flexibility. It
is possible that the large carbohydrate portion blocks the enzyme from a
co-enzyme or helper molecule. By cleaving the carbohydrate portions, thereby
their masking properties and reducing the size of the entire hCG molecule, the
hCG-inhibited enzyme may be re-activated. Certainly in the circulating form of
hCG, amylase can prevent inhibition of trypsin and the other protease enzymes
by cleaving the carbohydrates away from the protein before trypsin or another
protease would act on the hCG protein.
This inhibitor action of this hormone is also suggested by the finding that hCG
samples have been found to bind other enzymes including lysozyme, ribonuclease
A and ribonuclease U. (Lee-Huang et al. 1999) Since a large part of the hormone
is sugars, it is reasonable to assume that this is what is mostly responsible
for inhibition. Also, the sugars would not enter the active site of a protease.
Research proves that amylase can deactivate hCG, by cleaving the carbohydrate
part away from the protein part (Krebs, Bartlett, 1949).
hCG prevents immune reaction
The carbohydrate moiety of hCG has a large electro-negative charge conferred
upon it by the presence of sugars called sialic or neuraminic acid. hCG-beta
protein is bound by six carbohydrate units with two side chains of sialic acid
each. This large negative charge on the sugars repulses the white blood cells
which also are negatively charged. This prevents contact by the white blood
cells with the trophoblast proteins, as well as protecting the cancer cell from
any proteases. The result is that this sialomucinous coating confers upon
cancer cells, as it does placental cells, "immunologic privelege".
Some of the white blood cells play a role in digesting and clearing the cancer
cell debris after cellular digestion. These white blood cells also secrete
amylase and other hydrolases. However their output is limited in comparison
with that of the pancreas or by means of supplemental enzymes.
The carbohydrate moiety of hCG is also susceptible to digestion by
beta-glucosidase, beta-galactosidase and even lysozyme. Many of these sugar
digesting enzymes are products of the granular cells of the white blood cell
complement, and are found in the cellular lysosomes, all of which accentuates
the importance of the efficient delivery of amino acids to every cell, and
consequently the importance of free amino acid and chromium nicotinate
supplementation for cancer patients.
After amylase clears the carbhohydrate coating, the protein digesting enzymes
can come in and digest the protein back-bone of the cell membrane, just as it
does the circulating hormone. Naturally, lipase and phospholipase and
cholesterase are also a very important systemic enzymes in this therapy, since
the cell membrane consists of such. Afterwards the RNase and DNase can come in
and degrade the genetic material of these destroyed cells.
Importance of Amylase Accentuation found early
The importance of amylase in enzyme therapy was discovered experimentally early
in the 20th century. Physicians experimenting with Beard's enzyme threatment of
cancer utilized only proteinases, primarilly trypsin. They noted the cancer
patients experiencing symptoms of high arterial pressure, fainting, low back
pain, malaise, nausea and altogether symptoms similar to morning sickness in
pregnancy. Beard reasoned these symptoms might be due to the lack of amylase,
since the fetus does not produce amylase during gestation, but it does produce
proteinases.
We know now that proteinases can only partially digest this hormone hCG that is
bound with a large carbohydrate moiety. The permanent binding of the hormone to
the enzyme also represents a detritus the body doesn't know what to do with.
Higher protein content in the blood burdens the kidneys (low back pain),
results in higher osmotic pressure which in turn causes extravasation, causes
constrictions, edema and other bad effects.
Without understanding the finer points of the biochemistry of these secretions
of the cancer cell (which he called anti-enzymes) and their interactions with
the enzymes, Beard realized that the lack of fetal amylase might be the cause
of "cancer eclampsia", since the cancer patient's symptoms so resembled morning
sickness. He instructed the clinicians he worked with to begin using amylase
along with trypsin, and the symptoms dissapeared. Indeed, from that point on,
he suggested that the ideal use of these enzymes in cancer treatment was to
apply double the weight of amylase over that of trypsin (Internet, 4)
Amylase levels in the blood are definitely controlled by the adrenal cortex
(Logsdon et al. 1985; Cope et al. 1939). Such functional connectivity in the
body is never found without a purpose. Ultimately, natural selection does not
preserve inefficient processes or deleterious ones. Amongst the glucocorticoids
secreted by the adrenal cortex which increase amylase levels, dexamethasone
(DXM) seems to have the greatest effect, both cellularly and in the acinar
cells of the pancreas. The fact that hCG is antithetical to DXM (Soliman,
Walker, 1977) suggests that amylase is antithetical to hCG. In this datum we
see further why accentuation of supplementary amylse is essential in modern
immuno-enzyme therapy.
Amylase safety
Plasma amylase is not active against pituitary hormones similar to hCG
(Abromowitz and Hisaw, 1939), indicating its safety. Even in disease conditions
that cause a striking rise in the system of amylase, as in pancreatitis or
multiple myeloma, the enzyme itself does not produce toxic effects.
Pancreatic protease safety
With regard to absorbed enzyme safety, the same pertains to the proteases. For
example, while it has long been known that pancreatic carboxypeptidase does not
digest pituitary gonadotropin, it does digest the protein portions of mare hCG,
deactivating it. (Chow, Greep & Van Dyke, 1939; Evans and Hauschildt, 1943).
While this is not a direct confirmation using human hormone, the fact that
normally functional human pituitary hormone constantly intermixes with systemic
pancreatic enzymes bears out its safety as well as its specificity against hCG.
Dr. Nicholas Gonzalez and other enzyme therapists have been using these enzymes
over many years, and have never noted any toxic reaction to them. Some patients
may receive several ounces of enzymes each day, with no untoward effects.
Nevertheless, this does require an adjustment period, as the tumor begins to
break down, if the mass is large, to accomodate the excretory system and immune
clearance. Part and parcel to this clearance after the accomodation period is
more enzymes, for these can aid in destroying the toxic immune-complexes that
form with exposure of anti-genic proteins into the system by enzymatic therapy.
Sometimes these antigens are bound by antibodies and they are not cleared by
macrophages. This may be due to insufficient numbers of macrophages, monocytes,
etc. Or possibly due to the inefficiency of these immune cells due to a
deficiency in their own imported or synthesized enzymes or helper molecules
like magnesium and other elements. If such anti-body-antigen complexes
accumulate in various areas they may lead to blockage, as well as to
inflammation. High enzyme follow-up keeps this from occuring, and provides a
good method of unburdening the excretory and immune systems.
Nevertheless, when immuno-enzyme therapy begins, patients do report feeling
worse for a period of time. Very often this may be due to a larger output of
free-radicals from the white blood cells when they finally recognize the
de-shielded cancer cells. We do not advocate super high levels of free-radical
scavengers (FRSs), because free radicals are actually helping kill cancer
cells. Most cells have natural buffers against these. A rational use of
free-radical scavengers is to derive them from foods: citrus fruits,
blue-berries (highest natural content of FRSs) and other natural sources. Super
high doses of vitamin C is not recommended.
In studies over a period of 50 years by immuno-enzymologists, in which millions
of doses of enzymes have been used, have shown most side-effects of enzymes are
of the nuisance type: slight rash, itching or burning sensations (using enemas
of enzymes or injections), altered odor in stools, gas. Most reactions related
to itching and burning or mild allergic reactions to these preparations come of
plant or fungal derived enzymes. Of the millions of reports on enzyme therapy,
only three have reported anaphylactic reactions (Lopez, et al., p.136), and
these only occured when used in conjunction with local anaesthetics (ibid.).
Since we do not sell injectible enzyme mixtures, we will not delve further into
this subject.
Enzyme Inhibitors
For any enzyme, any substrate can be an inhibitor. While the substrate is
attatched to the enzyme, the enzyme is not able to act on other substrates. For
this reason, when there is a large ratio of substrate versus enzyme, the
enzymatic transformation is limited. The best way to overcome this is to
increase the amount of enzymes. At the peak of enzymatic therapy, a patient may
be consuming up to 180 tablets a day.
Also, some substrates can have parts that attach to other parts of the enzyme
slowing release of the product by altering the flexure of the enzyme. This is
called non-competitive inhibition. Various substances can act to help the
turnover of substrate from the enzyme and release of the inhibitors.
The cancer cell secretes a number of substances that reversibly inhibit the
proteases of the body, usually glyco-proteins. Pancreatic enzymes must work
over time to overcome this inhibition. Usually this is too much of a burden for
the pancreas without risking enlargement, inflammation and dysfunction. The
only alternative is to supplement the enzymes involved along with enzyme
reactivators.
Amylase always circulates in its active state in the body. In other words, is
not weakly inhibited as are the serine enzymes, although there are amylase
inhibitors in wheat and anionic detergents can deactivate amylase, as do heavy
metals.
It is important to avoid toxic heavy metals. The heavy metals mercury, silver,
copper and lead ions are able to deactivate these enzymes. For trypsin and
other proteases, phosphate esters (constituents in detergents),
organo-phosphates (constituents in insecticides) can also do this. Below we
discuss briefly methods of reversing such poisoning.
Cofactors and Accessory factors that act as adjuncts to enzyme therapy.
It was observed by researchers in the early 20th century that hydrocyanic acid
(HCN) had a "remarkably favorable effect" on proteolytic activity. (Vines,1903;
Mendel and Blood, 1910).
In early researches on papain, the chief protease of papaya, a means of keeping
substrate samples sterile was required. Sodium fluoride was tried for a time,
but it was found to inhibit the enzymes. Chloroform, salicylic acid, thymol,
toluene and formalin all had this inhibitory effect and were deemed
unsatisfactory antiseptics. However, HCN did not have this effect, and in fact
was seen to accelerate proteolysis by papain; while others found the same for
trypsin (Chittenden and Cummins, 1884-1885). This effect was so strong, that
papain was seen as inactive in various concentrations unless HCN was added,
leading them to regard it as behaving like a vitamin:
"..nothing remains but to compare the behaviour of HCN with that of the
so-called co-enzymes." (Mendel and Blood, 1910. p212).
HCN had this accelerating effect even in the presence of inhibitors. Thus it
not only acts as an accelerator, but reactivates inhibited enzymes.
HCN has the ability to reverse the inactivation of some enzymes by heavy metals
like lead (Sumner and Somers, 1943, p.28), evidently by preferential
displacement of the poisons from the enzyme by HCN.
As noted above, Mendell and Blood found HCN to have a favorable effect on
proteolysis or digestion of proteins. The only comparable molecule to HCN they
studied was hydrogen sulfide. Hydrogen sulfide is too toxic to use in therapy
except in minute amounts. Other sulfur bearing compounds are known for their
protective or reactivating effects on enzymes, as for example cysteine,
glutathione or magnesium sulfate.
HCN is detoxified in the body by the enzyme rhodanese (thiosulfate
transulferase), converting HCN to thiocyanate (SCN). Thiocyanate is also
cabable of accelerating proteolysis, though to a lesser degree than HCN.
Glutathione also is known to provide a protective effect on amylase (Sumner and
Somers, 1943, p.84).
While it is common for people to regard HCN as highly poisonous, it is a
required compound in metabolism, as for example as forming part of the
structure of vitamin B12.
Besides the enzyme rhodanese for detoxifying HCN to thiocyanate, the red blood
cells contain an enzyme called thiocyanate oxidase which releases HCN again
from thiocyanate (Goldstein and Rieders, 1953, quoted by Oke, 1969 p. 175).
Such mechanisms prove the metabolic necessity for free HCN in the body. This is
further supported by the fact that the vitamin B12 cycle of the body requires
free CN- to convert hydroxocobalamin (pro-B12 or B12a or B12b) to
cyanocobalamin (B-12).
Thiocyanate oxidase and rhodanese represent together the functional necessity
and utility of HCN metabolically. The cyanide is tightly bound to cobalt in
B12, nevertheless, the body possesses mechanisms for liberating the CN- from
B12. Other functions for CN- include acting as a carbon donor for the synthesis
of choline and other compounds and for the conversion of homocysteine to
methionine (Oke, 1969, pp190-191)
With this in mind, it is then logical to regard this molecule HCN and its
principle dietary sources as an important adjunct to enyzyme therapy along with
all the other vitamins and minerals necessary for normal health. The safest way
to derive HCN is from the dietary nitrilosides, or cyanophoric glucosides.
These substances are abundant in nature in natural food stuffs, with the
richest sources found in the seeds of apricots, peaches, cherries, plums and
the bitter almond. Other foods that are rich in nitrilosides include lima
beans, lentils, chick-peas (garbonzo beans), vicia fava, mung beans, wheat
grass and cassava (Krebs, 1964). Nitriloside rich foods make up the majority in
the dietary of many cultures (Oke, 1968, 1969).
Thus HCN is an essential cofactor if not a co-enzyme, and should not be labeled
as a poison any more than we would label B12 a poison, or vitamin A, which can
be highly toxic taken out of the context and quantities required for normal
metabolism.
Purified amygdalin is used in many clinics as an alternative therapy in cancer.
However, it is popularly regarded in those settings as a selective cytotoxin,
and the enzyme protocols may be regarded and treated by these clinics as
biochemically unconnected to the HCN fraction as cofactor or co-enzyme. In some
of these clinics, they may introduce thousands of milligrams of amygdalin
without a concomittant large load of enzymes. Mendell and Blood found that a
mere .15 per cent concentration was sufficient to accomplish remarkable results
on the enzyme turnover numbers (1.7 per cent HCN per 70 cc water with 2 per
cent papain in 700 cc water acting on 135 grams protein).
This is what we would expect of a true vitamin or cofactor. However, with very
high loads of amygdalin, the liver will have to work overtime to process the
whole molecule for physiological function or in making it excretable. This in
turn can have deleterious effects by dissipating detox molecules needed in the
tumor arena. Seen as a co-enzyme, HCN probably binds 1:1 (one to one) with each
enzyme molecule. It would be pointless to have a thousand molecules of HCN to
only one hundred enzyme units, assuming the HCN acts immobilly on each enzyme.
Much less would be needed if it acts dissociably.
It should also be noted that HCN probably does act as a cellular cyto-static,
meaning it drives the cancer cell towards a state in which it will not divide.
Cancer cells require oxygen during mitosis. Since the cancer cell is rich in
hCG, which inhibits the enzyme rhodanese (thiosulfate transulferase) which
detoxifies HCN, the cancer cell will be susceptible during their aerobic phase
(oxygen metabolism) to inhibitory effects of HCN. HCN deactivates the
mitochondrial enzyme cytochrome oxidase.
While HCN will inactivate cytochrome oxidase in cancer cells, in normal cells
rhodanese is present in active form to detoxify it before it reaches the
mitochondria.
However the cancer cell is facultatively anaerobic. This term means the cancer
cell can and does use oxygen, but when aerobic metabolism is threatened by HCN
or other means, it will merely undergo transformation to anaerobic or
fermentative metabolism. Thus this potency of HCN would be more like the
Pasteur effect, such as the effect oxygen has on anaerobic organisms,
inhibiting their growth. Probably the benzaldehyde molecule of amygdalin is a
true cyto-toxin, since this molecule has been shown to have a very powerful and
selective anti-cancer potency (internet, 5, 6) by its inhibiting action on
mitochondrial ATPase (Racker, 1972; Erwin et al. 1975). Together HCN,
thiocyanate and benzaldehyde would cover all the bases of a cancer cell's
energy production: aerobic and anaerobic.
Thus, seen as a cytotoxin, HCN would only be useful in killing or more probably
slowing cancer cells for part of their life cycle. On the other hand, as
adjunctive to enzyme digestion of cancer cells, HCN will always be useful, no
matter what phase the cancer cell is in, assuming sufficient free active enzyme
is available. The rational use of nitrilosides is therefore never as a
mono-therapy, but in conjunction with pancreatic enzymes.
Interestingly, thiocyanate has been shown to successfully prevent the crisis of
sickle-cell anemia (Houston, 1973) , as has cyanate (OCN-) (Ceramin and
Peterson, 1975) .
Vegetarian versus Meat diets in Therapy
The safe use of nitrilosides in diet and therapy presupposes the availability
of sulphur in the metabolic pool. Vegan diets and certain forms of
vegetarianism can put a strain on this sulfur pool and alter the metabolism
unfavorably especially with regard to enzyme synthesis wherein sulfur amino
acids are essential. Certainly a vegan or vegetarian diet can be safely
maintained with sulfur rich food sources and nitrilosides (for B12 synthesis),
but the cancer patient must conserve these resources and a vegetarian regimen
may be too much. Eating meat will not "dissipate" the enzymes we are using.
Indeed, systemic amylase levels are actually higher in meat eaters than in
vegetarians, while protease levels in the blood are higher in vegetarians.
Because low amylase levels can result in poor reactions to enzymatic therapy,
we want amylase levels to be higher. Most of the poor responses in patients to
enzyme therapy in terms of how they feel, or discomfort levels, is due to too
high an intake of proteinases versus amylase.
HCN/Amylase interractions
In some enzyme texts, HCN is noted as an inhibitor of amylase. In order to test
this, I subjected starch to salivary amylase digestion in the presence of soda
(to pH 7) and normal saline with and without amygdalin. Amygdalin is a
glucoside, specifically a nitriloside known as
laevo-mandelonitrile-beta-glucoside. It is known that saliva also carries the
glucoside digesting enzyme beta-glucosidase. Beta-glucosidase does digest
amygdalin releasing the sugar from the mandelonitrile moiety and allowing the
spontaneous generation of HCN and benzaldehyde (possibly suggesting the
presence of a nitrilase). Using standard determination techniques, salivary
amylase digestion of starch was accelerated in the starch-amylase-amygdalin
samples, and not inhibited. The samples without amygdalin did not show positive
reactions for maltose at the same time, though equivalent parallel samples did
show positive reactions later. Naturally, further studies by other researchers
must be performed to confirm this datum.
The Efficacy of Immuno-Enzyme Therapy in Cancer
Lab studies
Amongst an abundance of literature that show that circulating pancreatic and
homologous enzymes act against cancer cells, we will only refer to three lab
studies.
In one, dealing with leukemia, a study by researchers in Israel showed that
proteolytic enzymes of the serine type (trypsin, chymotrypsin and
carboxypeptidase for example) caused human myeloid leukemic cells to undergo
differentiation to benign and functionally normal leukocyte cells (Fibach et
al., 1985). This study suggests that leukemia represents a deficiency of
pancreatic enzymes leading to a state of arrested development in leukocytes.
The body uses a system of feedback to tell itself that something is lacking or
at appropriate levels. Possibly when active appropriate enzymes are lacking,
mature and active leukacytes are lacking. On one hand this is analogous to how
digestive enzymes are changed from a zymogen or pro-enzyme to active enzyme by
cleavage of a small peptide chain from one end of the zymogen by interokinases
or active trypsin. This allows the enzyme to unfold to its active state. We
might say that pro-leukocytes are waiting for proteolytic digestion for
activateion or to become mature leukocytes. Lacking mature leukocytes, to
compensate, the body continues producing more pro-leukocytes, as is found in
leukemia. When sufficient active leukocytes are present, production is cut off.
Therefore supplying supplemental enzymes of the type used in this study
(pancreatic enzymes) is a safer way of ameliorating this condition than using
exotic therapies like chemo and radiation.
Trophboblasts and tumor cells are characterized by certain adhesion molecules.
For example, oncofetal fibronectin which is found only in trophoblasts and
cancer cells (Siemianowicz, Gminski, et al., 2001 p.1291; Feinberg et al.,
1991;Matsuura and Hakomori 1985; internet 25; internet 26). Another adhesion
molecule expressed by trophoblast and cancer cells is CD44. CD44 is associated
with and is used as a predictor for metastatic phenotypes in cancers of many
types. CD44 is absent in first trimester trophoblasts, but is present in
pre-implantation trophoblasts, which have highly invasive characteristics
required in normal pregnancy for establishing the associated fetal cells (at
this stage, undetermined diploid totipotent cells or primitive individual cells
or stem cells, one of which will become the fetus) in the endometrial luminal
epithelium. German scientists found that the number of CD44 molecules
(epitotopes) on cancer cells from cultures of various types (leukemic,
melanoma, mammary carcinoma, histiocytic lymphoma) were reduced after exposure
to pancreatin, chymotrypsin, papain and bromelain (Gebauer et al., 1997). All
CDs, of which trophoblasts and cancers express several, are subject to
digestion by the pancreatic enzymes and other enzymes used in immuno-enzyme
therapy. Thus we see IET can not only digest cancer cells on site, but can
prevent them from moving beyond the local site of action by affecting their
adhesion motifs.
The first rational cure of cancer was developed by John Beard, as applied by
Dr. Lambelle. This case is reported in Beard's book, The Enzyme Treatment of
Cancer.(Beard, 1911; Lambelle, 1910). This was the first reported cure of
sarcoma by enzyme therapy.
However, we would not expect such an old case to provide evidence in today's
standards. Therefore, we can turn to modern studies, such as those provided by
Dr. Nicholas Gonzalez.
Other adjunctive factors to Enzyme therapy
Although the systemic enzymes all function optimally in basic or non-acid
environs, they can be activated by acids; and though the body temperature is
usually 98.6 F, these same enzymes actually improve in catalytic properties at
higher temperatures to the limits of fever temperatures. This suggests the
usefulness of hyperthermia therapy. (internet, 15)
As noted above, hCG confers upon a tumor cell a high electronegative charge
that repulses the white blood cells. It also aids in protecting the cell
membrane from digestion by proteinases like trypsin, chymotrypsin and
carboxypeptidase as well as the lipidases and phospholipidases. The negative
charge is on the carbohydrate molecule of hCG. The carbohydrate of hCG is
capped by many side chains of a sugar called sialic acid (neuraminic acid). The
human body does not produce the enzyme sialidase (neuarminidase), the enzyme
that breaks down these sugars, which enzymes are only expressed by virus and
some pathogens. However, studies have shown that vitamin A, retinoic acid,
seems to have the ability to strip this sugar from the carbohydrate part of hCG
(Hogan-Ryan and Fennelly,1978).
Similarly, studies done with the chelator EDTA (ethylenediaminetetraacetic
acid), show it has the ability along with trypsin to strip the cell coat of
cancers making them susceptible to both protease attack and immune
approach.(Anghileri and Dermietzel, 1976).
Inhibitors to be avoided in enzyme therapy
Dr. Nicholas Gonzalez has been treating patients successfully with enzymes for
over 20 years. In his experience, he has found it necessary to restrict his
patients from using soy products. This is because soy contains a natural form
of trypsin inhibitor. Most legumes have such inhibitors. Unless these foods are
cooked or sprouted (to one and three-quarter inches), they convey these
inhibitors into the blood stream or affect the enzymes in the digestive tract.
Similarly, many organo-phosphates or pesticides have been shown to inhibit or
destroy these enzymes, as well as do various detergents. Dish detergents are
highly negatively charged molecules that are not easily stripped from dishes
even with much rinsing.
Denaturents
In our state of civilization it is almost impossible to avoid heavy metals.
They perfuse the atmosphere and are incorporated into the plants and animals we
use as food. Heavy metals are especially destructive to enzymes, with the most
potent enzyme destroyers being mercury, lead, silver, copper and cadmium ions.
Ionic gold will also destroy enzymes. When these heavy metals are encountered
by the body, it will usually attempt to excrete them immediately or sequester
them if that fails. Thus these heavy metals will show up in the nails, hair,
and fatty tissues of the body. As an adjunctive therapy, chelation can be used
to ameliorate the deliterious effects of these heavy metals. Effective
chelators are EDTA, malic acid, N-acetyl Cysteine (NAC), BAL (British
Anti-Lewisite or penicillamine) and even the garnish cilantro has been shown to
possess chelating properties.
Naturally if a patient undergoes full scale chelation therapy, mineral
supplementation must be instituted to refortify the body with essential
minerals. By far the most effective means of getting these minerals is in the
form of foods wherein they are bound to proteins or other natural compounds or
naturally chelated. Not all therapists agree with this conclusion, prefering to
use solutions with free ions of these elements, such as Clark's Mineral formula
orally or as enema.
A very important adjunctive therapy for any patient (except those in danger of
renal failure) is magnesium chloride therapy. Dr. Raul Vergini has used this
therapy in his practice for many years with no untoward effects, but many
benefits for normal health and in cancer (internet 12, 14). It is no
exageration to say that magnesium is the quintessential mineral for homeostasis
and normalization of metabolism. It is hard to think of any metabolic process
that does not involve magnesium. In fact many experts contend that because of
its importance in over-all health and especially heart health and the high
incidence of heart disease, that magnesium deficiency in our country is
catastrophic (internet, 13, 21).
Toxic loading
Shutz law says that to double the digestion rate, the enzyme quantity must be
quadrupled. This naturally results in greater product loading of the excretory
mechanisms of the body. In therapy, it is suggested that a regular increase be
applied over a period of time, to accomodate the necessarily limited ability
the body has to eliminate the detritus or break-down products.
It is essential that liver and kidney function not be compromised by
over-digesting the tumor. At no time would enzyme supplements be removed, but
there is a logical patient-response/enzyme-quantity curve that must be
gradually steepened to maintain progress towards remission. If the increase is
too sharp, it can lead to a toxic overload. It would be pointless to completely
destroy a tumor only to kill the patient by kidney failure.
To help stimulate toxic flushing, some therapies utilize colonic flushes and
coffee enemas. The coffee enema has been used in professional medicine for over
100 years, and is not just a folk remedy (internet 10,11). Rather, it properly
falls under the category of empirical medicine, which constitutes the origin or
basis of 90 per cent of all medicine even today. Modern science works to
convert such methods to rational grounds. That does not alter their origins. In
traumatic head injury at the turn of the century, to ameliorate shock, "black
coffee per rectum" was used along with hypodermic whiskey injections, saline
enemas, ice cap to head and heating of extremities (Cathey, 1918) with very
good effect.
Coffee enemas stimulate the release of glutathione-S-transferase, which aids
the detoxification of free-radicals.(internet, 10) They also have the
subjective effect of inducing a sense of well being. (internet, 11).
Enemas of enzymes can also be of great help in the absorption of same. For
prostate cancer, colon cancer, and urinary-genital cancers, enzyme enemas are
required. For prostate cancer, see internet references 5 and 6: fig slurries
will deliver benzaldehyde which has powerful anti-cancer effects and is
readilly absorbed by the colon.
In conclusion, it must be accentuated that enzymatic therapy is very complex,
and should be administered by a competent professional. Many other adjunctive
therapies have been proven to be useful towards remissions and regressions:
hyperthermic therapy (in which papain is very much advocated because of its
stability in high temperature along with HCN); Coley's toxins to induce fever
and augmentation of immune reaction; hydrazine sulfate therapy, etc. All of
these therapies can be rationalized within the context of the immuno-enzyme
therapy discussed herein. Nevertheless, all these other adjunctive therapies
used WITHOUT consideration of immuno-enzyme therapy are destined to be
categorized as merely hit-or-miss attempts at remission.
It goes without saying that this review of imporant molecules, enzymes, and
vitamins as well as other nutritional factors cannot be complete. Cancer falls
within the scope of diseases termed chronic and metabolic disease. In the
histroy of medicine, no chronic or metabolic disease has ever been resolved by
factors other than those normal to the animal economy: namely, factors of
nutrtion including air, water, proteins(including enzymes), fats,
carbohydrates, vitamins and minerals. This automatically excludes such exotic
factors as surgery, radiation and chemotherapy, unless we ammend chemotherapy
to include such factors normal to the animal economy.
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Internet References
--------------------------------
1.
http://www.hinduonnet.com/thehindu/seta/2003/01/02/stories/2003010200030200.htm
2.
http://www.unibas.ch/dbmw/biochemie/Forschungsgruppen/Ugo/Research.htmHYPERLINK
"http://www.navi.net/~rsc/krebs49b.htm"; Molecular Mechanisms of Multistage
Tumor Development
3. http://nic.sav.sk/logos/books/scientific/node13.html
4. http://www.navi.net/~rsc/beard066.htm
5. Dr. Ralph Moss, PhD on benzaldehyde: http://www.navi.net/~rsc/benz.html
6. Dr. Hans Nieper in Townsend Letters for Doctors and patients regarding other
chemotherapeutic adjuncts of use: http://www.tldp.com/issue/160/160modrn.htm
7. On chelation therapy:
http://www.townsendletter.com/Nov_2002/arlinebrecher1102.htm
8. Abstract of Gonzalez study:
http://www.dr-gonzalez.com/pilot_study_abstract_txt.htm
9. Ralph Moss' report on hCG, pp 9-10:
http://www.ralphmoss.com/html/FebChron.pdf
10. http://www.ralphmoss.com/html/coff.shtml
11. http://www.dr-gonzalez.com/history_of_treatment_txt.htm
From the above, references relating to the use and efficacy of colonic
irrigations:
Liebow, C, Rothman, SS: "Enteropancreatic Circulation of Digestive Enzymes."
Science 189(4201), 472-474, 1975.
McClain, ME: Scientific Principles in Nursing. St. Louis: CV Mosby Company,
1950, p.168.
Bastedo, WA: "Colon Irrigations." NEJM 199(18), 865-866, 1928.
Bastedo, WA: "Colon Irrigations." JAMA 98(9), 734-36, 1932.
Friedenwald, J, Morrison, S: "Value, Indications, Limitations and Technic of
Colonic Irrigation." Med Clin of N Am, p.1611-1629, 1935.
Marshall, JK, Thompson, CE: "Colon Irrigation in the Treatment of Mental
Disease." NEJM 207(10), 454-457, 1932.
Snyder, RG: "The Value of Colonic Irrigations in Counteracting
Auto-intoxication of Intestinal Origin." Med Clin N Am, p.781-88, 1939.
Garbat, AL, Jacobi, HG: "Secretion of Bile in Response to Rectal
Installations." Arch Int Med 44, 455-462, 1929.
Further information on Dr. Gonzalez history is available at:
http://www.dr-gonzalez.com/maver_article_txt.htm
12. www.navi.net/~rsc/mg12b_txt.html
13. http://www.mgwater.com/
14. http://www.mgwater.com/cancer.shtml
15. http://www.bsdmc.com/press_release_11_20_02.htm
16. http://www.navi.net/~rsc/fibach.html
17. http://www.med.umich.edu/opm/newspage/2003/tumorsc.htm
18. http://www.the-scientist.com/yr2000/nov/steinberg_p1_001113.html
19: The Nitrilosides in Plants and Animals, ET Krebs:
http://www.navi.net/~rsc/nitrilo1.htm
20. [find web site with beta-galactosidase info or link about induction ].
21. http://www.mgwater.com/history.shtml
22. http://www.mucos.cz/eng/onko/con_onco_com.htm
23. On breast cancer response to hydrolytic enzymes:
http://www.mucos.cz/eng/onko/setictobc.htm
24: On chromium nicotinate versus picolinates:
http://www.anndeweesallen.com/dal_ra01.htm?femalemuscle.com
25. On fibronectins:
http://virology.med.uoc.gr/OR/2001/volume8/number6/1289-1292.pdf
26. Oncofetal fibronectin expression in breast cancer cells:
http://molecular.biosciences.wsu.edu/faculty/mccabe.html
27. Thieme B., Koop F., Harbeck N., Kolben M., *Ugele B., Schneider KTM.,
Graeff H. and Schmitt M.: FLOW CYTOMETRIC CHARACTERIZATION OF HUMAN
TROPHOBLASTS AFTER ISOLATION FROM
FRESH PLACENTAL TISSUE. (Abstr. No. 29 in 9th Heidelberg Symposium on Cytometry
[Deutsche Gesellschaft für Zytometrie] Oct.17-19, 1996)
http://www.biochem.mpg.de/valet/dgzab96b.html
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