Cancer chemo(toxico)therapy revisited and alternative ways of healing.A thesis presented to the Anglo-American Institute of Drugless Therapy and leading to the Degree of Doctor of Naturopathy (N.D.).
© 1990 by Dr. Henri Rosenberg.
Introduction 2
Chapter I : Chemo(toxico)therapy 3
Chapter II : Amygdalin - Vitamin B 99
Chapter III : The Synthetic Physiatrons 128
Chapter IV : Trypanosoma Therapy 140
Chapter V : Selenium Therapy 146
Chapter VI : The beer's yeast cure 156
Chapter VII : Tumor related indicators 164
Chapter VIII : The Thymus Therapy 188
Chapter IX : The H-11 Therapy 194
Chapter X : Antineoplaston 202
Chapter XI : Gelum Oral RD® 205
Chapter XII : Neoblastine® 212
Chapter XIII : The WIEDERMANN cure 219
Chapter XIV : Beetroot (juice) as cancer therapy 225
Chapter XV : Integral Fasting Therapy 229
Chapter XVI : The Iron Cancer Cure 235
Neoblastine®
Medication with the enzyme preparation NEOBLASTINE® attempts to achieve a triple object. This object consists a) of favourably influencing the physical constitution by stimulating all the body's metabolic processes; b) to halt mitosis and to break down intratumorally carcinoma containing substances to prevent migration and finally c) to bring about the lysis or necrosis of the cancer cells.
Prior to attacking the actual tumor the organ in which the tumor is embedded must return to performing its functions so that it can support the attack on the tumor itself.
The enzymes from the oxidation and lipid metabolism in the affected body are weakened. Moreover there is excessive protein production in the cancer tissue, and the andrenergic-cholinergic equilibrium in the body is disturbed. These four affected processes, which appear to be essential to the development of the cancer, are elucidated further below.1. Oxidation Metabolism
Many of the enzymes taking part in the oxidation metabolism are sulphhydryl enzymes. According to CRABTREE (1) the first development of a cancer consists of fixing the carcinogen to the sulphhydryl group (SH - group) of an enzyme protein. BARRON (2), DICKMANN and SINGER have demonstrated furthermore that ionizing radiation, ranging from X - rays up to and including ultra-violet rays lead to the irrevocable oxidation of the sulphhydryl groups.
Phosphorglyceraldehyde dehydrogenase and ATP-ase are also inactivated by this.
In turn GREENSTEIN and JENRETTE (3) have found that liver nucleoproteins possess free thiol groups. Myosin (ATP) and urease also have free thiol groups while papayine has only slow groups. The reactivity of these groups now depends on the distance in between the SH groups and the proximity of negatively charged groups.
There are three sorts of groups which are activated by these thiol groups:
a. pyuvic: these are hydrolitic enzymes such as amylase, cathepsin, carboxylase, and are often metallic or Mg proteins. The thiol groups form the link between the proteins and the metals.
b. oxidation-reduction enzymes. Most oxidizing and dehydro-genase enzymes belong to this category. Most of these are catalyzed by D.P.N. or flavoproteins. In this category the thiol groups transfer electrons from the substrate to the co-enzyme.
c. transfer enzymes, activated by ATP. This group includes the phospho-glucomutasen, ATP-ase, hexokinase, citrogenase, etc. In the transferases the thiol groups bond the proteins by means of co-enzymes.In the body these thiol enzymes are reactivated by glutothione or cystine, which themselves are both sulphhydryl compounds. They can reduce virtually all other SH enzymes because of their low redox potential. According to BARRON (3) the soluble thiol enzyme is one of the regulators of cell metabolism. During cell division the thiol content of the cell rise markedly until mitosis and then falls off again. Furthermore tumor cells, like embryo cells, have a high glutathion content.
As remarked above, in the first instance the carcinogen puts this sulphhydryl enzyme out of action with all the consequences that this involves.2. Lipid metabolism
The lipid metabolism is also weakened by cancer. According to GRIFFIN and others (4) tumor development is coupled to a shift in the lipids metabolism. It has been observed that tumors causes lipemia and a fall in the fatty acid content of the body. On the other hand it causes fatty acids to become even more unsaturated and thus influences the lipids metabolism, so that the ratio of saturated to unsaturated acids in the organism becomes the same as that in the tumor.
3. Protein production
The difference between the metabolism of normal and wild tissue, is that in the latter protein (albumen) synthesis is dominant. In non-pathological tissue there is an equilibrium between the production and breakdown of protein. This means that the enzyme systems (proteogenic and proteolytic) which govern the protein metabolism in normal tissue are also in equilibrium in normal tissue, but which in tumor tissue are used for protein production (5).
The factors which govern the protein mechanisms are not known with certainty. It may, however, be assumed that the destruction of protein by proteinase is catalyzed in normal cells. In wild tissue, however, it appears that this enzyme is present in its inactive proenzyme form, zymogen.What is certainly known is that the wild growth of primary tumours is stimulated by hypophysial growth hormone and by gonadotrophic hormone. The action of adrenalin controls the action of both hormones through the sympathetic nervous system.
In tumor tissue protein synthesis dominates which because of the influence of the redox potential makes bonding with cystine molecules impossible. This redox potential is, nevertheless, dependent on the pH. The question therefore is how to influence this intracellular pH to such an extent that the cystine bonding capacity can restore. The enzymes are organized in the intracellular space into functional groups in the cell organelles. The operation and direction of the reaction are determined by the surrounding ion ratios, that is to say by the pH of the organelles. These ion ratios are governed by local variations in permeability in the membranes of the organelles, resulting in the exchange of Na+, K+, Cl-, SO-. These exchanges cause considerable shifts in pH, and consequently bring about changes in the function of enzymes in the organelles. (see Gelum)
Now changes in membrane permeability are induced by the tissue hormones, adrenalin and noradrenalin, acetylcholine (precursor of the antineoplasmic choline), histamine and perhaps other as yet unknown ergones. Excessive adrenalin secretion can therefore stimulate the growth of cancerous cells through the process described above. In contrast choline has anti-carcinogenic properties. Basically therefore, the approach attempts to restore the adrenergic-cholinergic equilibrium, thus reducing adrenalin secretion (with all the consequences this has for pH, cystine bonding capacity, and so on) and stimulating choline synthesis. This is to be achieved by enzymatic means (NEOBLASTINE), as described below.Action of NEOBLASTIN*
The high glucose consumption (for energy) of the tumor leads to glucose deficiency in the non-cancerous tissue. In the long run the entire glycogenic reserves of the body are mobilized and slowly exhausted, so that the hydrolisis of proteins containing sugar and glycoproteins is stimulated in order to satisfy the demand of the cancer cells for sugar. Increasingly the tumor will increase the hydrolosis of glycoproteins. The products of this hydrolysis, i.e. amino and nucleic acids which are broken down by the liver and kidneys, can immediately be used by the tumor for cell synthesis.
The liver and kidneys are soon overburdened by the rising glycoprotein content. As a result they are only able to break down a small proportion of these hydrolisis products. The greater part of these metabolites are, however, used up by the primary and metastased tumors.
As the tumor uses both the glucose and the amino acids up, lipid production progresses only partially and with difficulty. From the above it is apparent that the mere stimulation of the organism with all its metabolic processes (with a view to improved oxidation, etc.), without taking simultaneous measures to reduces the energy demand of the cancer cells is a waste of time.
By stimulating the organism ATP and CTP reserves (the two stores of oxidizing energy) will probably rise and the synthesis to hydrolysis ratio of nucleoproteins and lipids could move towards a recovery, but the tumor will (also) profit from the improved conditions to grow (even) faster. It is therefore necessary to suppress the metabolism of the tumor and to stimulate the entire metabolism of the body (only) together with this.
By giving NEOBLASTINE*, and the complex of enzymes known as thioloxidase contained in it, the oxidizing sulphur metabolism is catalyzed and activating the sulphhydryl-enzymes. The numerous proteolytic (6) enzymes which form part of the SH enzyme group such as hydrolase, oxireductase, transferase, adenosine- phosphatase, amino-oxidase, amylase, asparaginase, catalase, hexokinase, and urease are stimulated. The tripeptide, glutathion, and the amino acid, cystine, are also stimulated. The experimental administration of thioloxidase to laboratory animals and clinical trials have shown that its action is primarily in the organ affected by the body, and not in the cancer tissue, where it has virtually no effect.
By administering (the sulphhydryl enzyme) monamin-oxidase (the second component of NEOBLASTIN*) direct action is taken against the tumor. The monaminoxidase given (only in present in very small quantities in cancer cell) is first activated (like the other sulphhydryl enzymes) by the thioloxidase. The monamin-oxidation physiolo-gically inactivates adrenalin by oxidative desamination, whereby intracellular pH shifts to its normal level, thus restoring the redox potential of the cancer cell so that cystine bonding with the intracellular zymogens can again take place. As a result these zymogens return to being active proteinase and which can resume the breakdown of protein by catalyzation in order to restore the original balance between the synthesis and breakdown of protein.
By administering monaminoxidase alone to laboratory animals (thus without the other components of NEOBLASTINE*) researchers have succeeded in making improvements to spontaneous tumors and postponing metastasis. However, by combining thioloxidase with the monaminoxidase administered to laboratory animals and human beings, an inhibiting effect on tumors and the reversal of migration has been observed.
The difference in effect on primary tumors and metastases, may well be related to the fact that primary cancers (rather like the foetus in the womb) are supplied by the hypophysis, while metastases are not.
Whatever the case may be the combined administration of thioloxidase and monaminoxidase have a synergic effect and is thus optimal.
Lipases in NEOBLASTINE* facilitate the penetration of the membrane of the cancer cell. These are necessary because without them the administered enzymes and the activated proteolytic enzymes would not be capable of penetrating the cancer cell. In this way the lipases support the breakdown of the cancer cells.Once the growth of the tumor has been brought to a halt by the damage to the cell and the reactivation of all the body metabolites the tumor will in many cases be reabsorbed by the organism.
If this is not the case, toxic breakdown products and wastes will arise as a result of the disintegration of the cancer tumour. Monaminoxide and glucoron acid promotes detoxification.
To sum up: we can say that the monaminoxidase inactivates the adrenalin, leading to a shift in intracellular pH towards the natural physiological pH. As a result the thioloxidase can catalyze the bonding between intracellular proteinase and consequently stimulate the breakdown of protein.
The lipases assist with the breakdown of cell. In non-pathological cells the sympa-thetic and parasympathetic mechanisms this process continues until a certain equilibrium is achieved, while in cancer cells, where sympathetic and parasym-pathetic mechanisms are absent or have been neutralized, breakdown continues until nothing remains.Composition
Thioloxydase 100 I.E. 1.8.3.2.
Mono-amino-oxidase 20 I.E. 1.4.3.4.
Triacylglycerol-lipase 20 I.E. 3.1.1.3
Ammonium sulfuricum 60 mg
Alkohol benzylicum 20 mg
Saccharidum amylaceum 20 mg
Aethanol 96% Vol 40 mg
Aqua dest. ad 2 ml one ampoule
Manufacturer
Enzypharm B.V.
P.O.B. 54
3760 AB Soest
Holland
phone : (02155) 12447
Distributor
Enzypharm Biochemicals Ltd.
P.O.B. 69
Harrogate, North Yorkshire HG1 2LE
England
phone : (0423) 60543
____________________________________________________
Footnotes :
(1)
(2)
(3) BARRON op cit.
(4) GRIFFIN, CUNNINGHAM, BRANDT, and KUPKE, Cancer, 4, page 410 - 415 (1951)
(5) The ratio of d and l amino acids shifts in favour of the d amino acids. The nucleus of tumor cells also possess more guanine nucleoprotein than normal cells.
(6)
Dr. Henri ROSENBERG, LL.D., Ph.D., N.D.
Doctor of Naturopathy
Permanent Member of the British
Guild of Drugless Practitioners.
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