Science: Biology: Two Notes on Progress in BSE-Crisis
by Professor Dr. Dr. hc Randolph Riemschneider Berlin, Germany Background: Bovine spongiform encephalopathy (BSE) and some other
diseases like scrapie (sheep), Creutzfeldt-Jakob disease (human) and kuru
(human) have one thing in common: both are
transmissible chronic degenerative diseases of the brain with characteristic
changes of the brain structures. It is
estimated that between 1977 and 1995 over 900,000 British cattle were infected
with the BSE agent, of which some 165,000 head in the United Kingdom developed
BSE by the end of 1996, while the other animals were slaughtered before the
outbreak of the clinical symptoms (commonly known as mad cow disease). Feeding
infected bone meal is now considered the most important way of transmitting the
pathogen. The question of whether the BSE derives from the scrapie of sheep and
goats, or whether it has always occurred in cattle, is to date unresolved. The
pathogens are currently believed to be Prions. Prion according to
Prosinger (1982), derived from Proteinaceous infectious particle:
Prions are membrane-bound protein molecules which can self-replicate and lead
to the formation of vacuoles of so-called amyloid plaques. Evidences: Chemical
and physical processes which modify or degrade nucleic acids, do not
destroy the agent’s infectivity. On the other hand, chemical and physical
processes which modify or degrade proteins do destroy the agent’s infectivity;
however, the thermic inactivation of, for example, BSE prions requires approx
18 minutes at 134-138° C, with
differences by breed in cattle. BSE prions are resistant to formalin; the usual
heat sterilization with 70% alcohol does not achieve the aim. BSE agents resist
ultraviolet or ionizing radiation which in viruses results in the complete
destruction of their infectivity by damaging their genomes. By reason
of these characteristics, the American microbiologist Griffith in 1967 surmised
that these pathogens could be pure proteins. Prusinger took this idea up at the
end of the 70's and formulated the basis of the prion theory in 1982. It
assumes that a pathologically reconfigured protein, the prion protein, is the
infective agent, which postulates a fundamentally new class of pathogens (in
addition to having a protein sheath, viruses also contain a core of DNA or
RNA). There is as yet no conclusive proof of this theory. There is
also discussion about whether a virus, which only uses the prion protein as a
receptor for entering the cell, could be responsible for these diseases. On the
other hand, supporters of the virion theory postulate that a small viral
nucleic acid is not surrounded by the virus’s own proteins but by prion
protein. However, to date, it has not been possible to demonstrate such a pathogen-specific
nucleic acid. The
function of the prions – now known as prion proteins (PrP) - is to date just as
unclear as the mechanism of their infectivity. Their existence is no longer
disputed. It is now recognized, even if not undisputed, that not bacteria or
viruses - but rather these prions, a completely new type of pathogen – are
responsible for causing these prion diseases, e.g. new variant
Creutzfeldt-Jakob disease (nvCJD) in humans, bovine spongiform encephalopathy
(BSE) in cattle, scrapie in sheep, and others. Prions are
the body’s own quite normal, non-vital proteins (PrPc - c for
cellular), whose function is still unclear. They occur in all tissues but are
mainly located on the outer wall of nerve cells in the brain. They are harmless
in their original physiological form and trigger no disease. They can only
cause diseases when infective prions reconfigure them into harmful prions
(so-called PrPSc - sc for scrapie-specific). The two isoforms PrPc
and PrPSc differ only in
their spatial structure, i.e. the way in which the prion amino acid chain is
folded: a- helix structure or a-helix and b-folding structure. It is
assumed that a single PrPSc molecule, functioning as a template,
docks onto a PrPc and thus reconfigures it into the pathological form.
These newly created PrPSc in their turn can supposedly affect the
reconfiguration of normal PrPc into PrPSc. Subsequently a
sort of chain reaction commences which leads to an accumulation of PrPc
building blocks and finally results in the destruction of the nerve cells. This
manifests itself as perforated, spongy brain tissue. The body’s
own healthy proteins, i.e. PrPc, can be degraded and destroyed by
proteases (not, however, the PrPSc pathogens) – an important
prerequisite in the assumed infection via food, e.g. through BSE-infected meat. The central
event is the reconfiguration of a host-encoded amyloidogenic protein (PrPc)
into an abnormal isoform (PrPSc) which accumulates as amyloid in BSE
brain. Two Notes on Progress in BSE-Crisis:I Substitution of organ extracts prepared from fresh glands by BSE-free cell lines extracts II A new
probiotic animal food additive based on plant material useful in BSE-crisis I. The BSE problem, which arose in Great Britain in 1985/86, has reached
in the meantime most other European countries. Since December 2000, overseas
countries have stopped the import of European animal material, medical and
cosmetic preparations of bovine origin, including Asia, for instance, on
December 12, 2000.
A way out has been offered by the author, who has developed a new
manufacturing method for BSE-free organ extracts derived from BSE-free cell
lines. In some publications (1,2) the author compared the analytical data of
classic organ extracts derived from fresh glands with the new ones from cell
lines. Practical experience with cell line based organ extracts has been
collected in Asia for more than 10 years, e.g. medical remedies similar to
Cellryl or cosmetic additives like Placenta or Thymus extracts. The new
manufacturing method is secured by the author’s patents in Europe and overseas
countries (2). II. To handle the
animal feeding problem related to BSE the animal nutrition was changed as much
as possible to vegetarian fodder and the use of antibiotics was limited. Useful
can be the new plant based food additive H 2000 which was developed in the 80s
and has been tried since. H 2000 is an environment friendly natural agent based
on Actinomycetae cell preparations (3).
Extensive field experiments with more than 500,000 chickens, more than
300,000 piglets and cattle proved that H 2000 is useful in concentrations of
0.1%-0.2% concerning food saving and the health of the animals. These
experiments were done at first in Brazil, then in the USSR, Poland, Hungary and
Switzerland. Toxicological laboratory tests in the 80s and the positive results
of the above mentioned field experiments prove the non-toxicity of H 2000. How does it work? H 2000 is activating, in principle, energy producing
reactions like cell-respiration and glycolysis so delivering more energy for all
metabolic reactions consuming energy. The patented manufacturing process does neither imply any chemistry nor
does it use organic solvents. References: (1)
R.
Riemschneider, Relata Technica Web Site http://www.very.com/relata,
Issues, Articles 2001 (2)
For
instance: DE 19624476 A I from Dec. 12, 1997 (69 pages) (3)
R.
Riemschneider: “The animal food additive H 2000” (1990); see APPENDIX Appendix: The animal food additive
H 2000 H 2000 is a new biological plant-based <<animal food
additive>>, tested during the last ten years in large scale on chicken,
pigs, sheep, calves, rabbits, dogs, etc. in many countries like Brazil, Japan,
Poland, USSR, Hungary, Switzerland and Germany under the names: -
Proval
(Pro from probiotic, val from value) (Proval sometimes Socoproval) -
H 2000
(H from Hefe) -
Y (Y
from yeast) -
S 2000
(S from Saccaromyces cerevisiae). The
decisive viewpoint for the development of H 2000 was to use vegetal starting
material. Starting
from yeast like Saccaromyces – applying several combined physical influences in
the manufacturing process, we came to new << yeast cell-preparations
>>, not anymore reproductive and not anymore fermentating, but
activating the yeast-fermentation of glucose and activating the
cell-respiration in a high degree: more scientifically spoken: activating
anaerobic and aerobic reactions of the cell-metabolisms in general. H 2000 is
really something new: H 2000 is not to be confused with the normal food-yeast which
is used since long time as donator for proteins and B-vitamins. H 2000 is
added to animal food in very low concentration of 0,1%-0,2%. Such low
concentrations are sufficient to activate the cell metabolism in different ways
– so increasing the effectivness of foodstuff. The patented manufacturing
process does not imply any chemistry, no organic solvents are necessary. H 2000
shows no toxicity. One not can observe any mortality determination DL50 mouse,
using 15gr H 2000 pro kg mouse. In the
mentioned filed-experiments with thousands and thousands of chicken, hundreds
of pigs and other animals – never was the observed mortality higher than in the
control experiments, if any. Activation
of cell-metabolism by H 2000: The
cell-metabolism activation of H 2000 can be demonstrated: anaerobic by
increased fermentation (I), aerobic by increased cell-respiration (II), for
instance by WARBURG-method. I: Manometric
measurement of increased CO2-production of fermenting yeast under H 2000
influence or II: Manometric
measurements of increased O2 – consumption of liver homogenate under H 2000
influence. The
activation of the anaerobic and aerobic cell-metabolism in cytoplasma and in
mitochondriae means increasing the ATP-production of the cells. So more energy
is available for all energy depending reactions. For instance more
energy for synthetic reactions (protein biosynthesis), for catabolic reactions,
energy for maintaining concentration-differences between the cell compartments
etc. The
cell-metabolism-activation by H 2000 can also be demonstrated by growth
experiments in laboratory-tests with guppy-fish or with tadpoles (Xenopus), or
in practical animal nutrition experiments. BWW Society Member Dr. Randolph G.A.
Riemschneider is a graduate of the University of Berlin and has a carer of more
a than half-century of scientific research. His areas of study include Polyacyl
Chemistry, specifically o-Diacetylbenzene; his other research areas include
work with natural, synthetic and cell-cultured BSE-free organ extracts.
Metabolism activation, stereochemistry and other specialized work.
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