Thyreogen acts as a tissue specific bioregulator to regenerate, repair and restore organ functions. Thyreogen has been shown to help treat both hyperthyroidism, (weight loss, anxiety, heat loss etc) and hypothyroidism (weight gain, lethargy, cold intolerance etc). Also a poorly performing thyroid gland can lead to autoimmune thyroiditis.
Bioregulator Thyreogen - is a thyroid gland extract and contains the major peptides of the thyroid gland. For the extraction of peptides only thyroid gland tissue are used derived from calves and pigs younger than 11 months old. All young animals come from farms in which no diseases were registered, which are dangerous to humans, including BSE.
Remove Metabolic Disorders
Prevent the Thyroid Diseases
Treat Hyperthyroidism and Hypothyroidism
Erradicate Thyroid Nodules
Remove Autoimmune Diseases
Professor KhavisoInterview with Vladimir Khavinsonn is president of the European Academy of Gerontology and Geriatrics (IAGG), advisor to various Ministries of Health and holds honorary distinctions from several universities.
Thyreogen - is a peptide complex, isolated from the thyroid gland of young, healthy animals. The isolated thyroid gland peptides have a selective effect on different cells of the human thyroid gland, normalize metabolism in these cells, regulate their functional activity and thus contribute to the regulation of the thyroid gland.
The optimal function of the human endocrine system is directly related to the state of the thyroid cells. For the optimal function of the cells is their optimal supply of nutrients such as vitamins, minerals, and with peptides required. The peptides are components of the protein molecules and are released during protein metabolism (Disintegration of the protein into smaller fractions = peptides). The peptides are information molecules, which influence gene expression and start the process of protein synthesis. Formation of proteins is a vital process. This is necessary for the growth of the cells and performing its key features.
Safety of natural peptide bioregulators
Figure 1. Gel chromatography of Cortexin solution.
Edited by Prof. Vladimir Kh. Khavinson,
Associate Member of the Russian Academy of Medical Sciences
Written by G.A. Ryzhak
Safety of Natural Peptide Bioregulators. – St. Petersburg: IKF Foliant, 2002. – 20 p.
The proposed scientific publication presents the results of a detailed study on peptide bioregulators isolated from animal organs and tissues and on the risk of their contamination with infectious agents, functionally active protooncogenes, nucleic acids, and prion proteins. The medical application of this class of pharmaceuticals has been proven entirely safe.
Introduction The contemporary epoch is marked by an extraordinary diversity of unfavourable factors affecting the human organism: natural conditions, unbalanced nutrition, environmental factors, external damaging agents including ionising and microwave radiation and toxic substances. It results in the depletion of adaptation and compensation mechanisms, occurrence of various diseases and pathologic states, and, finally, in premature ageing.
The above problems necessitate the development and clinical implementation of new effective therapeutic agents and the methods of functional correction, intensification of resistance to adverse factors, inhibition of ageing, and prolongation of life span.
Long-term experience of applying peptide bioregulators extracted from the organs and tissues of young animals has confirmed the high efficacy of this class of substances in various diseases and pathologic states including those not responsive to the treatment with other medications.
However, the active application of animal-derived peptide bioregulators in medicine requires special control over the quality and safety of these substances, since raw material used in their production can contain components hazardous for the human organism. In this view, it becomes ever more significant to devise technologies securing the safety of such substances and to work out effective control methods proving the absence of infectious agents, protooncogenes, prion proteins or other objectionable components in them.
natural peptide bioregulators The concept of bioregulation therapy based on the pathogenetic application of peptide bioregulators in various diseases, pathologic states, and ageing has been proposed and grounded in the course of 30-years’ research conducted at the Military Medical Academy (St. Petersburg) and St. Petersburg Institute of Bioregulation and Gerontology. Vyacheslav Morozov and Vladimir Khavinson were the first to isolate peptide bioregulators of multicellular systems from the hypothalamus, epiphysis, and vessel walls in 1971 . These substances have been brand-named cytomedins.
The technology of obtaining cytomedins includes acetic extraction of polypeptide fractions from cattle and pig tissues, their precipitation and subsequent multistage purification. The final product is in the form of lyophilised powder for injection solutions.
These developments have enabled the creation of new pharmaceuticals – peptide bioregulators, which form a group of pharmacologically active substances with molecular weight within 1-10 kDa. Their administration to the organism results in the functional restoration of the very organs, which the cytomedins have been isolated from.
The Institute possesses 15 pharmaceuticals. All of them have undergone thorough trials. Some cytomedins have been approved for clinical use over 15 years before (Epithalamin® – the endocrine system bioregulator, Thymalin® – the thymus bioregulator, and Prostatilen® – the prostate bioregulator) . In 1999, the Russian Ministry of Health certified the clinical application of Cortexin® (the cerebral cortex bioregulator) and Retinalamin® (the retina bioregulator) [15, 4]. Other bioregulators are undergoing various stages of clinical and experimental studies.
The technology of bioregulators manufacture and the methods of treatment with their use are covered by 70 licenses and USSR, Russian, and foreign patents. The majority of the developments have no analogues in the world.
Long-term experience of applying peptide bioregulators in healthcare has revealed their high effectiveness in various diseases and pathologic states including those not responsive to the treatment by other therapeutic means.
A new class of parapharmaceuticals – cytamins – has been created to expand the sphere for the application of bioregulators. Cytamins are balanced tissue-specific nucleoprotein complexes isolated from animal organs and tissues .
Today, 17 Cytamins are produced: extracted from the brain, liver, prostate, heart, thymus, bronchi, cartilages, pancreas, vessels, stomach, testes, epiphysis, thyroid, adrenal glands, kidneys, ovaries, and eye tissues.
Cytamins exert a targeted (organotropic) effect immediately upon the organs and tissues they have been isolated from. Being not drugs per se they produce a mild physiological regulatory influence on various functional systems of the organism, which enables their use as natural adaptogenes. Cytamins promote optimal functioning and full-value nourishment of organs and tissues, they do not contain any conservatives or other alien substances, produce no side effects, have no contraindications, and are compatible with any other nutrients and medications.
The patented technology of cytamins manufacture includes alkaline hydrolysis from tissue cells, consecutive precipitation of nucleoprotein complexes, their purification from ballast substances, and manufacture of the ready form as enterosoluble tablets or capsules.
Thus, two new classes of peptide bioregulators have been developed: pharmaceuticals cytomedins and parapharmaceuticals cytamins applied on a wide scale in medical practice to prevent various disease and pathologic states and treat for them.
safety of cytomedins and cytamins Historical background of the prion diseases concept
The history of the prion diseases concept is set forth in detail in monograph by V.A. Zuev et al. “Prion diseases in humans and animals” . Below we resort to some excerpts from this book.
The problem of prion diseases arose within the framework of the slow developing infections theory on the basis of the results of long-term investigations on mass diseases in sheep imported to Iceland from Germany in 1933. Despite some obvious clinical differences and uneven localisation of lesions in the animals’ organs and tissues, a principal similarity was revealed. This similarity can be summed up in four major signs of slow developing infections:
Among the studied sheep pathologies, scrapie was investigated. This disease of sheep and goats was well known in many countries.
Three years later, in a geographically opposite region – New Guinea – a new disease, now known as kuru, was revealed among Papua cannibals and described. Its mass development pointed at its infectious nature.
These and a number of other diseases were united by a common typical symptom. All of them were manifested only as lesions to the central nervous system: a typical picture of so-called spongiform transformation of the grey and/or white brain substances and, sometimes, of the spinal marrow based upon primary degenerative processes (without inflammation signs) and, in some cases, accompanied by the formation of amyloid plaques and expressed gliosis.
This peculiarity of the pathomorphologic picture marked out the name for the entire group of diseases – transmissible spongiform encephalopathies. Their pathognomonic feature consisted in the transmissibility of spongiform alterations solely within the central nervous system.
For decades, any attempts to discover pathogenes of these diseases ended in a failure though their infectious nature was convincingly confirmed. Yet, in early 80s Stanley Prusiner, an American biochemist from the California University, claimed that this pathogene was a nucleon-free low molecular protein (27-30 kDa), which he named “the infectious prion protein” . Prusiner proposed the term “prion” – an anagram from “proteinaceous infectious (particle)” as an infectious unit consisting of the infectious prion protein molecules. Prusiner was awarded a Nobel Prize in Biology or Medicine in 1997 for his prolonged investigations on slow developing prion infections.
Results of the studies carried out over the recent 15 years confirmed the prion nature of transmissible spongiform encephalopathy pathogenes completely. Consequently, these diseases were defined as prion ones.
The non-infectious (cellular) prion protein is vitally important. It is found in all mammals including humans. Among its distinguishing features is its high sensitivity to the digestive activity of protease K, which destroys this protein.
The infectious prion protein is preserved after the digestive impact of protease K. Its molecular weight equals 27-30 kDa.
The mechanism of accumulating the infectious prion protein in an infected organism has not been defined by now. At the same time, it is obvious that in a healthy organism the infectious prion protein entails the transformation of the normal prion protein into its infectious form due to the conformation changes of the normal prion protein. Therefore, the infectious prion protein is accumulated not via de novo synthesis of its molecules in an infected organism, but due to the conformation alterations of already synthesised normal molecules of a prion protein under the effect of the infectious prion protein.
The modern classification of prion diseases distinguishes human and animal pathologies and includes four human and six animal ones.
The list of human prion pathologies starts with Creutzfeldt-Jacob disease – the main in this group, while kuru and Herstmann-Streussler-Scheinker syndrome are considered to be its variants.
Scrapie is the main animal prion disease viewed as the prototype for all human and animal prion diseases.
In 1986, the United Kingdom was struck by an epizootic of bovine spongiform encephalopathy. As it turned out, the infectious prion protein originated from meat/bone flour. The technological process of its manufacture in early 80s implied a considerably reduced process of carbohydrate dissolving extraction of fat from bones, pluck, and heads of caws and sheep. This technological modification enabled the preservation of the infectious prion protein in raw material and caused mass contamination of ruminants after adding meat/bone flour to their forage as a protein supplement.
Started with two cases in 1986, the epizootic developed rather intensively and reached the peak of 1,000 cases in caws in 1992. Then the rate of new occurrences decreased notably and progressively.
Over this period, 23 sporadic cases of the so-called the new variant of Creutzfeldt-Jacob disease were registered, chiefly in the United Kingdom. The disease broke out among young patients, which was untypical.
Creutzfeldt-Jacob’s is a rare and fatal disease of worldwide distribution. Its total annual incidence in different regions is nearly equal and makes 0.3-1 case per 1,000,000 people. There has been revealed no correlation between Creutzfeldt-Jacob disease and the development of scrapie as the most frequent animal prion pathology. Creutzfeldt-Jacob disease has the same incidence in the scrapie-endemic United Kingdom and in Australia and New Zealand where scrapie has not been registered for years.
Wide-scale research was conducted in the United Kingdom in response to the epizootic of bovine spongiform encephalopathy in this country. Results of these investigations revealed the principal risk of infecting humans with prions from contaminated animals. It must be noted that the epizootic did not influence the total incidence of Creutzfeldt-Jacob disease in the United Kingdom as compared to other countries where no cases of the pathology in cattle were observed. Only the young age of all patients with the new variant of Creutzfeldt-Jacob disease attracts attention: all these people were less than 40 years of age. At the same time, young patients with this diseases constituted as little as 2 % of the total population (usually it was registered in the older age group, its peak striking the 60-65-year-olds).
Consequently, natural raw material of animal origin can potentially include infectious agents, protooncogenes, and nucleic acids. That is why, in the manufacture of preparations from animal organs and tissues a special attention is to be given to the purification of the active substance from objectionable admixtures and, first of all, to the infectious safety of such preparations.
Technological aspects of peptide bioregulators safety
In the manufacture of peptide bioregulators only the Russian-raised cattle is employed – calves and pigs under 12 months of age from the regions and farms where no human-endangering infectious diseases including transmissive bovine spongiform encephalopathy has been registered. It is to emphasise that Russia is known for its epizootological and epidemiological safety in respect to prion diseases.
The technology of obtaining cytomedins implies the acetic extraction of polypeptide fractions from calf and pig tissues, their precipitation and subsequent multistage purification until the outcome of active fractions with the molecular weight of 1-10 kDa. The final product is in the form of lyophilised powder intended for injection solutions.
The technology of extracting Cytamins includes alkaline hydrolysis of tissue cells, subsequent precipitation of nucleic complexes and their purification from ballast substances, drying of the half-product and manufacture of the ready form as enterosoluble tablets or capsules.
Thus, the patented methods of obtaining cytomedins and cytamins secure the maximal protection of these preparations from the interference of infectious agents. The active substance is extracted from animal organs and tissues at 3-7°C, pH 3.0 (cytomedins) or 11.0 (cytamins) for 6 days. These conditions are sufficient to fully inactivate all microbes and viruses even if no extra impacts are applied [8, 10].
Analysis of peptide bioregulators molecular weight
Molecular weight of cytomedins was studied by two methods – gel chromatography in Sefadex G-25 and electrophoresis in 15 % polyacrylamide gel. The results of gel chromatography revealed one peak in each chromatograms of the Cytomedins in the region of molecular weight under 10 kDa (Figures 1, 2, 3).
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Copyright © 2005 - 2017