Ran across this flounder and I don't know if I have posted it before., but its a prime example of how independent scientific research is blocked by corporate agriculture..... if they have nothing to hide why not allow the man to research............. look how many people lost an income because of BSE (not only in Europe, but Canada as well) and by using DMSO they could have inactivated it??
http://www.earthclinic.com/CURES/mad_cow.html
"Bovine spongiform encephalopathy (BSE), commonly known as mad-cow disease, is a fatal, neurodegenerative disease in cattle, that causes a spongy degeneration in the brain and spinal cord and red eyes. BSE has a long incubation period, about 4 years, usually affecting adult cattle at a peak age onset of four to five years, all breeds being equally susceptible. In the United Kingdom, the country worst affected, more than 179,000 cattle have been infected and 4.4 million slaughtered during the eradication programme.
It is believed, but not proven, that the disease may be transmitted to human beings who eat the brain or spinal cord of infected carcasses. In humans, it is known as new variant Creutzfeldt-Jakob disease (vCJD or nvCJD), and by April 2008, it had killed 163 people in Britain, and 37 elsewhere with the number expected to rise because of the disease's long incubation period. Between 460,000 and 482,000 BSE-infected animals had entered the human food chain before controls on high-risk offal were introduced in 1989." (Wikipedia)
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TED'S REMEDIES
09/22/2006: Ted from Bangkok, Thailand writes: "Whenever people having a severe wasting away of brain, certain disease such as Alzheimers, or mad cow's disease, there is a possibility that these might be caused by a protein prions. One such possible treatment in the future involves the use of potassium thiocyanate (LD 50 is about 800 mg/kg) so my estimate is using assuming we weigh only 1 kilogram and take 800 mg, might be possible to use this as a way to treat such conditions in the future. Of course, this is a speculation and since this is rarely occurs in human we can only speculate as to the possibilities, before a mad cow's epidemic suddenly grabbed us. It is therefore best that we prepare ourselves and know the findings before it happens.
Here is the literature that sites inactivation of a scapie agent (mad cow's disease) shown below:"
Proc Natl Acad Sci U S A. 1981 July; 78(7): 46064610. Copyright notice
Thiocyanate and hydroxyl ions inactivate the scrapie agent.
S B Prusiner, D F Groth, M P McKinley, S P Cochran, K A Bowman, and K C Kasper
This article has been cited by other articles in PMC. Abstract
To probe the macromolecular structure of the scrapie agent and explore conditions for monomerization, the stability of the agent in low concentrations of inorganic ions was determined. A reduction by a factor of 10(5) in scrapie titer was found on exposure of the agent to 1 M KSCN or 0.3 M NaOH. In addition to the inactivation by thiocyanate ions, other chaotropic ions such as guanidinium and trichloroacetate inactivate the scrapie agent. Removal of thiocyanate ions by dialysis or glass permeation chromatography prevented the reduction in scrapie agent infectivity. Addition of equimolar amounts of (NH4)2SO4, a nonchaotrope, to preparations containing 1 M KSCN also prevented the loss of scrapie infectivity. In contrast, neutralization of the alkali-treated fractions with HCl did not restore infectivity. Acidification of partially purified fractions did not cause inactivation of the agent but did result in precipitation of the infectious agent. Inactivation by relatively low concentrations of chaotropic ions is consistent with many observations, all of which suggest that the scrapie agent contains a protein component that is essential for the maintenance of infectivity. Thus, it is unlikely that the agent is composed only of a "naked" nucleic acid. Certainly, if the agent were a naked nucleic acid, its lability in alkali virtually eliminates the possibility that it is composed of a single-stranded molecule of DNA." Ted also write us: "There is actually a treatment for Mad Cow Disease. Well, the prions won't go away, but it is no longer active. So in effect, there is a cure if you can make the prions no longer active. However, you must take it continuously.
The idea is to put DMSO (dimethyl sulfoxide) in your drinking water a couple of drops per liter to inactivate prions. Dimethyl sulfoxide is found in nature and in rainwater and is quite safe. I also drink it regularly. What DMSO does is in very low concentration (higher might be more effective), it deactivates prions. However when DMSO is no longer there, the prions is again activated.
(Source) http://www.priondata.org/data/A_DMSO.html )
The idea is if anybody having mad cow (or MIGHT GET ONE FROM EATING BEEF!!) drinks water with small amounts of DMSO for the rest of his life, mad cow will go away and hence a cure.
My idea is when DMSO is inactivated, if you managed to change the diets you are eating where manganese (and organaophospate insecticide) is no longer in the excess or eat food with less manganese for a long period of time or taking calcium EDTA (a common treatment for managanese toxicity), it is possible along with DMSO, to effect the further progression and possibly remission of Mad Cow.
As you know, the cause of mad cow is actually caused by organaophospate insecticide where the food is rich in manganese is what causes mad cow in the first place
Also, EVIDENCE OF DMSO inactivating Prions is located here:
Source: http://www.priondata.org/data/A_DMSO.html
Prion disease: an opportunity?
The fact that prion rods are dissolved in quite low concentrations of DMSO, and lose their infectivity in the process is interesting. However the fact is that the infectivity is returned when the DMSO is taken away and the rods reform (Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R. Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods. J Biol Chem 2001 Apr 27;276(17):14324-8 see abstract.
Considering its structure it is remarkably low toxicity and the possibility remains that the drug could be used to lower the amount of amyloid in the brain after other drugs had been used to actually stop the production of new PrPsc (e.g. Glivek?). This may lead to a progressive loss of infectivity in the brain and a lower risk to the brain from the stimulation of microglia and hence damage to the cellular structure that the chemicals that these cells release are causing.
Patients describe the drug as not being particularly toxic but others around them describe an 'awful' smell of the compound in the breath and fluids of the patient.
Ruth Gabizon at the Prion Therapeutics conference in December 2002 in Paris said that the phenomenon of DMSO dissolving of the prion fibrils should not be forgotten and, although this chemical was relatively toxic, there may be others that are not and DMSO could in fact be used for a short period in a long term therapy program.
Medical Abstract of Prions inactivated by DMSO is located here:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11152454&dopt=Abstract
And this is the Abstract:
Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods.
Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R.
Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, Jerusalem 91120, Israel.
The scrapie isoform of the prion protein, PrP(Sc), is the only identified component of the infectious prion, an agent causing neurodegenerative diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Following proteolysis, PrP(Sc) is trimmed to a fragment designated PrP 27-30. Both PrP(Sc) and PrP 27-30 molecules tend to aggregate and precipitate as amyloid rods when membranes from prion-infected brain are extracted with detergents. Although prion rods were also shown to contain lipids and sugar polymers, no physiological role has yet been attributed to these molecules. In this work, we show that prion infectivity can be reconstituted by combining Me(2)SO-solubilized PrP 27-30, which at best contained low prion infectivity, with nonprotein components of prion rods (heavy fraction after deproteination, originating from a scrapie-infected hamster brain), which did not present any infectivity. Whereas heparanase digestion of the heavy fraction after deproteination (originating from a scrapie-infected hamster brain), before its combination with solubilized PrP 27-30, considerably reduced the reconstitution of infectivity, preliminary results suggest that infectivity can be greatly increased by combining nonaggregated protease-resistant PrP with heparan sulfate, a known component of amyloid plaques in the brain. We submit that whereas PrP 27-30 is probably the obligatory template for the conversion of PrP(C) to PrP(Sc), sulfated sugar polymers may play an important role in the pathogenesis of prion diseases.
PMID: 11152454 [PubMed]
Here is some more citations using DMSO and mad cow:
source links:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12914974&query_hl=7
1: Brain Res. 2003 Sep 5;983(1-2):137-43. Related Articles,Links
Dimethyl sulfoxide delays PrP sc accumulation and disease symptoms in prion-infected hamsters.
Shaked GM, Engelstein R, Avraham I, Kahana E, Gabizon R.
Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, 91120, Jerusalem, Israel.
PrP(Sc), an aberrantly folded protein, is the only identified component of the prion, an agent causing fatal neurodegenerative diseases such as scrapie and bovine spongiform encephalopathy. Dimethyl sulfoxide (DMSO) has been shown to reduce the accumulation of PrP(Sc) in scrapie-infected (ScN2a) cells, and to inhibit its aggregation in vitro. In humans, DMSO was used successfully in the treatment of various peripheral amyloidotic diseases. Here we show that administration of DMSO to scrapie-infected hamsters significantly prolonged disease incubation time, as well as delayed the accumulation of PrP(Sc) in Syrian hamster brains. Interestingly, administration of DMSO to scrapie sick hamsters resulted in increased clearance of protease-resistant PrP in their urine. We conclude that although DMSO by itself may not be sufficient to cure prion diseases, it may be considered as a component in a 'cocktail' drug approach for these disorders. Also, urine PrP testing should be considered for the assessment of treatment efficacy.
PMID: 12914974 [PubMed - indexed for MEDLINE]
Disaggregating effect - or dispersion and possibly reversal of the conditions can also be helped using DMSO and a weak ethanol solution:
source links:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12719126&query_hl=7
Int J Biol Macromol. 2003 Mar;32(1-2):10-6. Related Articles,Links
Disaggregating effects of ethanol at low concentration on beta-poly-L-lysines.
Sabate R, Estelrich J.
Departament de Fisicoquimica, Facultat de Farmacia, Universitat de Barcelona. Avda. Joan XXIII s/n, Catalonia, Spain.
Protein aggregation is involved in a number of disorders, such as Alzheimer's disease, cystic fibrosis, and prion diseases. Such aggregates are formed by peptides in beta-conformation. The study of the processes of aggregation or its inhibition makes it necessary for the peptide to remain in a monomeric state at the beginning of aggregation assays. Using three poly-L-lysine as a model of beta-peptide, we measured the spectral changes occurring in the visible spectrum of Congo Red (CR), a diazo dye, in two solvent media, namely, an aqueous solution of ethanol 10% (v/v), and an aqueous solution of dimethyl sulfoxide (DMSO) 5% (v/v). Aggregation constants show that the presence of ethanol at low concentration produces a disaggregating effect, regardless of the degree of polymerisation of the peptide. This effect is considered to be due to the direct binding of ethanol molecules to the peptide. This binding undergoes an enhancement of the electrostatic repulsion among charged lysine chains.
There are many documented studies in DMSO in the treatment of Mad Cow (technically its Bovine Spongiform Encephalopathy (BSE) and Creutzfeldt-Jakob disease (CJD)). And it can really technical if you want more documented details. It will take me several hundred pages to cover everything on this topic to do it justice, and it goes beyond my available time. However, I can refer you to several places which will help you further research and discover yourself that there are answers out there.
Here is an article excerpt as well as the link source to the full article with all the citations, and scientific studies:
source: http://www.doewatch.com/gws.html
"...Even the factors of high rates of ALS seen in the GW vets is directly associated with the GSH and SOD enzymes. ALS is associated with upsets of copper and manganese that form these enzymes. The problems of Mad Cow and Prion linked illnesses are caused by these same factors. Mad Cow effects come from a systemic shift toward Mn-SOD from the Cu-Zn-SOD. When sulfur bearing compounds like DMSO are applied to Mad Cow affected brain tissues, the plaques dissipate, and DMSO appears to act as GSH in supplying the sulfur to remove the toxic metals from the brain that attract the SOD needed for myelin repair.."
The following are research citations of using DMSO at www.pubmed.org in the treatment of mad cow (CJD):
1: Brain Res Mol Brain Res. 2004 Apr 7;123(1-2):37-44. Related Articles,Links
Doxycycline and protein folding agents rescue the abnormal phenotype of familial CJD H187R in a cell model. Gu Y, Singh N.
Institute of Pathology, Case Western Reserve University, 2085 Adelbert Road, Cleveland, OH 44106, USA.
Familial Creutzfeldt-Jakob disease (CJD) comprises a group of neurodegenerative disorders for which currently there is no treatment. In this study, we evaluated the efficacy of drugs approved for human use, and protein folding agents in reversing the mutant phenotype of familial CJD H187R in a cell model. For an efficient experimental readout, green fluorescent protein (GFP)-tagged mutant prion protein (PrP(187R-GFP)) and wild-type PrP (PrP(C-GFP)) were expressed in human neuroblastoma cells. We report that unlike PrP(C-GFP) that is expressed on the cell surface, PrP(187R-GFP) accumulates in the lysosomes of transfected cells. Treatment of PrP(187R-GFP) cells with quinacrine or doxycycline, agents known to inhibit the replication of PrP-scrapie (PrP(Sc)) in experimental models, gave conflicting results; doxycycline reverted the mutant phenotype of PrP(187R-GFP) cells, whereas quinacrine had no effect. The concentration of doxycycline used in these studies is well within the plasma concentration of patients receiving a 250-600 mg dose two to three times daily. Interestingly, exposure of PrP(187R-GFP) cells to low temperature (28 degrees C) or to the chemical chaperones dimethyl sulphoxide (DMSO) and glycerol also reversed the mutant phenotype. These data suggest that doxycycline and protein folding agents may hold promise as therapeutic agents for familial CJD H187R and other familial disorders that share similar pathogenic mechanisms.
PMID: 15046864 [PubMed - indexed for MEDLINE]
Below, the citation Me2SO4 is another name for DMSO, since full name is DimethylSulfoxide.
1: J Biol Chem. 1999 Jun 18;274(25):17981-6. Related Articles,Links
Protease-resistant and detergent-insoluble prion protein is not necessarily associated with prion infectivity.
Shaked GM, Fridlander G, Meiner Z, Taraboulos A, Gabizon R.
Department of Neurology, Hadassah University Hospital, Jerusalem 91120, Israel.
PrPSc, an abnormal isoform of PrPC, is the only known component of the prion, an agent causing fatal neurodegenerative disorders such as bovine spongiform encephalopathy (BSE) and Creutzfeldt-Jakob disease (CJD). It has been postulated that prion diseases propagate by the conversion of detergent-soluble and protease-sensitive PrPC molecules into protease-resistant and insoluble PrPSc molecules by a mechanism in which PrPSc serves as a template. We show here that the chemical chaperone dimethyl sulfoxide (Me2SO) can partially inhibit the aggregation of either PrPSc or that of its protease-resistant core PrP27-30. Following Me2SO removal by methanol precipitation, solubilized PrP27-30 molecules aggregated into small and amorphous structures that did not resemble the rod configuration observed when scrapie brain membranes were extracted with Sarkosyl and digested with proteinase K. Interestingly, aggregates derived from Me2SO-solubilized PrP27-30 presented less than 1% of the prion infectivity obtained when the same amount of PrP27-30 in rods was inoculated into hamsters. These results suggest that the conversion of PrPC into protease-resistant and detergent-insoluble PrP molecules is not the only crucial step in prion replication. Whether an additional requirement is the aggregation of newly formed proteinase K-resistant PrP molecules into uniquely structured aggregates remains to be established.
PMID: 10364247 [PubMed - indexed for MEDLINE]
People treating mad cow using hyperbaric chambers:
source links:
http://www.sptimes.com/2004/01/12/State/South_Florida_mad_cow.shtml
The best way is prevention, and you need to know the source of mad cow. There are some government policy questions that people need to be aware of not to be infected with mad cow:
source link: http://www.consumerfed.org/releases2.cfm?filename=madcowcredibility.txt
Carol Tucker Foreman served as assistant secretary for food and consumer services, US Department of Agriculture, 1977-81. Her responsibilities included meat, poultry and egg inspection.
I hope this answers some of your questions regarding the issues of prions, mad cow diseases, policy issues, the use of DMSO.
The likely cause of mad cow theory is best explained by Mr. Purdey:
http://www.mercola.com/2000/dec/17/bovine_spongiform_disease.htm
Insecticide Causes Mad Cow Disease
by Fintan Dunne Research by Kathy McMahon
Reprinted from eionews.com, email - [email protected]
Pharmaceutical interests in the UK are ignoring new scientific research that shows the insecticide used in the UK government's own warble-fly campaigns triggered the UK surge of 'Mad Cow' disease.
Latest experiments by Cambridge University prion specialist, David R. Brown, have shown that manganese bonds with prions. Other researchers work shows that prions in the bovine spine -- along which insecticides are applied -- can be damaged by ICI's Phosmet organophosphate(OP) insecticide -causing the disease.
British scientists have led the current theory that an infectious prion in bonemeal fed to cattle causes bovine spongiform disease (BSE).
Infectious prions are also claimed to cause new variant Creutzfeld-Jakob Disease (CJD) in humans -from ingesting beef. But the infectious prion theory serves to obscure a tragic chemical poisoning scandal behind the majority of BSE cases.
The new work proves that the prions can bond with manganese in animal feeds or mineral licks. These manganese prions cause the neurological degeneration seen in BSE. By a similar process, prions in human brains are damaged by lice lotions containing organophosphate. This can result in neurological diseases like CJD and Alzheimers -later in life.
Many might be surprised to hear that organophosphates were developed by Nazi chemists during the course World War Two, as a chemical weapon nerve agent. One formulation of the insecticide -- Maneb, or Mancozeb -- actually contains manganese in addition to organophosphate.
The marginalized research has devestating financial implications for ICI. It would provide a firm basis for litigants -who could include CJD sufferers, farmers across the world and families of the many British farmers who committed suicide during this BSE debacle.
Phosmet organophosphate has been used at high doses in British warble fly campaigns. In 1996, ICI subsidiary Zeneca sold the phosmet patent to a PO Box company in Arizona called Gowan -just one week before the UK government admitted to a link between BSE and nvCJD.
The politically well-connected British pharmaceuticals group, ICI has the financial and political clout to block research into any cause other than the infective model. Indeed no substantive alternative research has been done. British BSE disease management and research bodies have taken decisions that do not seem guided by spirited scientific enquiry. Mysterious prions that jump species is the preferred research arena.
Scientist and organic farmer, Mark Purdey gave evidence to the UK BSE inquiry, that warble fly insecticide was the cause of the disease. The scientist wheeled out to rubbish Purdy's evidence -Dr. David Ray, later turned out to have been receiving funding from the insecticide manufacturer ICI.
A lobby group that includes Bayer, Monsanto, Novartis, Pfizer, Roche and Schering-Plough was behind the effort to discredit Purdey. In December 1999, the same David Ray was appointed to the UK Veterinary Products Committee (VPC) -a government body that licences animal medicines.
Purdey has been consistently denied even exploratory funding to extend his privately supported research. Yet the Purdey/Brown chemical poisoning model matches with the epidermiological spread of CJD clusters in humans. It also predicts the incidence of BSE-type diseases in animals. The accepted infectious model fits neither. The pharmaceutical industry is all the more determined to hide the chemical source of BSE and CJD, because a spotlight on chemicals would expose the role the insecticides in Alzheimer's -- another neurodegenerative disease -- that might lead to claims which would dwarf those from BSE and CJD litigants. In fact, two leading brain researchers into CJD and Alzheimers have died in suspicious circumstances in recent years.
In the United States, the Environmental Protection Agency is already reviewing Phosmet's safety. The Centers for Disease Control in the US has recently conducted experiments on mice that confirm the organophosphate risk. Not only is the EC beef slaughter campaign futile -because BSE disease is mostly non-infectious, but unless the underlying chemical cause is addressed, BSE will simply reappear from chemical causes. A new warble fly campaign is already underway in France using the organophosphate insecticide.
Of greater concern is that some lotions for scabies and head lice are now priming children and adults, for CJD and Alzheimers in later life.
Bonding The Prion
Cambridge University prion biochemist, David R. Brown is dismissive of the science behind the infectious model of BSE. He terms it "a very limited amount of science by a few assumed- reputable scientists." He insists there is "no evidence an infectious agent is present in either meat or milk."
"Simple tests on udder walls of cows -- which could easily detect an infectious prion -- have not been done, why I don't understand."
A number of researchers have found that organophosphate(OP) in systemic warble fly insecticide can deform the prion molecule, rendering it ineffective at buffering free radical effects in the body. Worse still, the prion is then partial to bond with manganese and become a 'rogue' prion. A chain reaction whereby rogue prions turn others to rogues also, can explain the bovine spongiform disease mechanism.
Brown showed how prion protein bonds benignly with copper, but lethally with manganese. Even natural variations in relative environmental availability of manganese versus copper can trigger prion degradation.
The CJD and BSE symptoms mirror 'manganese madness', an irreversible fatal neuro-psychiatric degenerative syndrome that plagued manganese miners in the first half of the last century
Shining a Light on Spongiform
Organic dairy farmer and peer-review-published independent scientist, Mark Purdey, says the accepted theory of transmission from BSE-infected cattle to human CJD -by bonemeal or meat, is dependent on a mutant prion that has never been isolated under the scientific protocol called Koch's postulates.
Purdey's insistence on sticking to the letter of this scientific law earned him the condemnation of UK officialdom when he first mooted his theory. But Purdey pointed to CJD clusters downwind of a British Phosmet production plant to back his case.
He gave evidence to the UK Government BSE inquiry and was supported by Conservative MP, Thessa Gorman. His views were discounted, but his subsequent research and the new Cambridge prion work have confirmed the alternative theory. Despite this, and the backing of a British peer, he is denied even exploratory funding.
Speaking from his rural English Somerset farm yesterday -as plans forge ahead for the European cattle cull, he asks:
"Why does CJD degeneration in humans begin in the retina, and why are CJD disease clusters found in high altitude locations?"
The question is rhetorical, and Purdey has an eye-opening answer. He argues that the prion molecule has a known natural role as a shock adsorber of damaging energy from ultraviolet rays and other oxidizing agents.
Once this prion defence system is rendered ineffective by organophosphates - for example in human head lice lotions, these oxidizing effects have an unmediated impact on tissues. Eventually, UV radiation damages the retina and oxidative stress destroys the brain tissues of CJD patients. This theory would expect to find higher CJD incidence in mountain regions -where UV radiation levels are elevated. That prediction holds true.
A similar but accelerated mechanism could be driving BSE. ICI's Phosmet organophosphate warble fly insecticide -applied on the backs of animals along the spinal column, similarly degrades prions. "Systemic versions of the insecticide are designed to make the entire cow carcass toxic to warble fly," explains Purdey. "Unfortunately it's toxic to prions too -especially those prions located just millimeters from the point of application."
The damaged prions are then ready to react with manganese in animal feed, or manganese sprayed on land or in mineral licks -to become the driving force of BSE neurodegeneration. Purdey says manganese-tipped prions set off lethal chain reactions that neurologically burn through the animal.
Chickens notoriously excrete most of the supplements fed to them -including manganese. And their manganese-rich excreta have been blended into cattle feed in the UK. Natural variations in the relative environmental availability of copper and manganese can also spur prion degeneration says Purdey.
From this research, any prudent person would conclude there is a significant risk attaching to the use of organophosphate in humans. Preparations for head lice and scabies are known to be overused in practice and might be priming users for CJ disease.
Purdey believes his bias for field work is the key to his success. He bemoans the "reductionism" of much lab-centered science. "I have traveled the world to investigate known clusters of spongiform disease -something mainstream researchers don't seem remotely interested in doing."
Since first postulating an environmental -rather than infectious- theory of spongiform diseases, Purdey has built evidence from around the world that explains and predicts the incidence in humans and animals: a cluster of CJD in Slovakia, Eastern Europe -around a manganese plant; Rocky Mountain deer with Chronic Wasting Disease (CWD), who were found to be eating pine needles rich in manganese; the futile slaughter of sheep in Cyprus -only for BSE to reemerge within years.
"The reappearance of BSE in Cyprus obviously points to an environmental cause," says Purdey, who is sanguine when reflecting on the condemnation of him by mainstream scientists.
"I suppose they have mortgages and kids who need to go to university," he muses. "Privately, some were agreeing with me, but then they would denounce me publicly. It was quite strange really."
The Money Trail
Critical scientists like Purdey are unlikely to prevail. The pharmaceutical industry holds most research purse strings, and would hardly energetically explore an avenue of research that could expose them to litigation for causing BSE. The official theory is lavishly funded, alternative theories rarely, if at all.
There are more explosive implications to his -and other's latest research. Purdey says similar organophosphate-induced protein deformation could also underlie Alzheimer's disease. If that were true, the litigation fallout would destroy some pharmaceutical giants, and a lot of very influential noses would be out of joint.
Disturbingly, Purdey and other brain researchers seem to have had an undue share of unfortunate accidents. Purdey's house was burned down and his lawyer who was working with him on Mad Cow Disease was driven off the road by another vehicle and subsequently died. The veterinarian on the case also died in a car crash -locally reported as: 'Mystery Vet Death Riddle. Dr. C. Bruton, a CJD specialist -- who had just produced a paper on a new strain of CJD -- was killed in a car crash before his work was announced to the public. Purdey speculates that Bruton might have known more than what was revealed in his last scientific paper. In 1996, leading Alzheimer's researcher Tsunao Saitoh, 46 and his 13 -year-old daughter were killed in La Jolla, California, in what a Reuters report described as a "very professionally done" shooting.
What Alzheimer's Disease, Mad Cow Disease, and CJ Disease have in common, is abnormal brain proteins and a putative link to organophosphates. Even Gulf War syndrome among returning veterans has been attributed, in part to the insecticide. But the sidelined scientists' suspicions are still largely ignored.
In their favour at the moment, is a growing unease on the part of the public. As BSE forges on and Governments panic, Science may be out to lunch on BSE, compromised by bovine spongythinking myopathy.
Do Not Use Systemic Organophosphate Insecticides
Do NOT treat children with OP head lice products - they may cause CJD and Alzheimer's
Do NOT treat your pets with OP anti-flea products
Do NOT treat cattle or animals with OP products - they may cause BSE
Do NOT give manganese to cattle previously dosed with a systemic OP
The relative availability of the metals copper and manganese in you local environment is a major factor in BSE & CJD
Additional Notes:
I contacted Mr. Purdey and there is possibility of chelation therapy or fulvic acid might be one possible method of reducing the metal toxins thus starving the source of the manganese from the renegate prions.
Majority of the public are not aware of Mr. Purdey's finding from insecticide, and environmental excess manganese, much less the treatment of such.
If you want to dig deeper please go to www.pubmed.org for more information. What is unusual is that there is news reports that Mad Cow has been misdiagnosed for Alzheimers and other similar conditions such as Parkinson's Disease and true figures may be much worse, however since incubation times are long, it may be too late before we can actually do the treatment.
Mycoplasma (fungus-like) is another possible leads as to the cause or a cofactor towards mad cow but this is just a hypothesis, which can be tested by examination of cows with the disease and test for present of fungus or mycoplasma of the brain. However,some indirect evidence is seen in certain people who died of Alzheimer were found to have fungus or algae in the brain. So this is circumspective and proof of hypothesis is sorely needed. If this is indeed confirmed anti-fungal drugs might be of some use in the treatment of mad cow. It is disappointing however, that no major funding for research on the nature, cause, and treatment of mad cow.
Suggestions for Farmers:
1. Checking of manganese level in feed. 2. Don't use organophosphate insecticide that has to do with warble flies. 3. Don't allow the Cows to feed on dead carcasses and chicken feces (chicken feces are high in manganese). 4. DMSO is currently used as a potential treatment for mad cows, however, preventive approach is recommended in adding small amounts of DMSO to feed which might deactivate prions before the feed is given to the cow. The possible uses of DMSO is important and can be used in possible sterilization of process food treatment before it reaches the public. Currently prions are not easily destroyed by either heat or acid. Therefore, DMSO (dimethyl sulfoxide appears a potential food additive to feed or processing of foods). A wider range of uses of DMSO may be in order. DMSO has more uses in cleaning and sterilization of carcasses as well. This is the only way to "deactivate" the prion that we know of based on all the studies.
5. I currently use DMSO to clean meat products, and small amounts to drinking water now and then, especially if the need arises to eat beef or meat products.
6. The use of GMO feed for cows is potentially deadly. Some studies point to the fact that prions which causes mad cow are much more deadly and spread much more quickly if GMO foods (such as G.M.O. soybeans is used). ONE OBVIOUS reasons that many are not aware of is corporations create GMO to better resist herbicide and pesticide, which implies higher organophosphate in these plants. However, getting into a debate with corporations that organophosphate content in plant is a waste of time. They will deny it anyway. The best method of attack is Genetically Modified plants are potentially dangerous is the best point of attack. There is a DNA exchange that is common in nature wherby GMO DNA do not exist in nature and can be exchanged with human DNA and this may bring about unestimable damage to the human genome. The science of this is fairly well known in academic circles but totally foreign from the press."
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(good grief!!! I had to edit this for the past hour, because of all the repetition and I think I've gotton it all)
http://www.earthclinic.com/CURES/mad_cow.html
"Bovine spongiform encephalopathy (BSE), commonly known as mad-cow disease, is a fatal, neurodegenerative disease in cattle, that causes a spongy degeneration in the brain and spinal cord and red eyes. BSE has a long incubation period, about 4 years, usually affecting adult cattle at a peak age onset of four to five years, all breeds being equally susceptible. In the United Kingdom, the country worst affected, more than 179,000 cattle have been infected and 4.4 million slaughtered during the eradication programme.
It is believed, but not proven, that the disease may be transmitted to human beings who eat the brain or spinal cord of infected carcasses. In humans, it is known as new variant Creutzfeldt-Jakob disease (vCJD or nvCJD), and by April 2008, it had killed 163 people in Britain, and 37 elsewhere with the number expected to rise because of the disease's long incubation period. Between 460,000 and 482,000 BSE-infected animals had entered the human food chain before controls on high-risk offal were introduced in 1989." (Wikipedia)
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TED'S REMEDIES
09/22/2006: Ted from Bangkok, Thailand writes: "Whenever people having a severe wasting away of brain, certain disease such as Alzheimers, or mad cow's disease, there is a possibility that these might be caused by a protein prions. One such possible treatment in the future involves the use of potassium thiocyanate (LD 50 is about 800 mg/kg) so my estimate is using assuming we weigh only 1 kilogram and take 800 mg, might be possible to use this as a way to treat such conditions in the future. Of course, this is a speculation and since this is rarely occurs in human we can only speculate as to the possibilities, before a mad cow's epidemic suddenly grabbed us. It is therefore best that we prepare ourselves and know the findings before it happens.
Here is the literature that sites inactivation of a scapie agent (mad cow's disease) shown below:"
Proc Natl Acad Sci U S A. 1981 July; 78(7): 46064610. Copyright notice
Thiocyanate and hydroxyl ions inactivate the scrapie agent.
S B Prusiner, D F Groth, M P McKinley, S P Cochran, K A Bowman, and K C Kasper
This article has been cited by other articles in PMC. Abstract
To probe the macromolecular structure of the scrapie agent and explore conditions for monomerization, the stability of the agent in low concentrations of inorganic ions was determined. A reduction by a factor of 10(5) in scrapie titer was found on exposure of the agent to 1 M KSCN or 0.3 M NaOH. In addition to the inactivation by thiocyanate ions, other chaotropic ions such as guanidinium and trichloroacetate inactivate the scrapie agent. Removal of thiocyanate ions by dialysis or glass permeation chromatography prevented the reduction in scrapie agent infectivity. Addition of equimolar amounts of (NH4)2SO4, a nonchaotrope, to preparations containing 1 M KSCN also prevented the loss of scrapie infectivity. In contrast, neutralization of the alkali-treated fractions with HCl did not restore infectivity. Acidification of partially purified fractions did not cause inactivation of the agent but did result in precipitation of the infectious agent. Inactivation by relatively low concentrations of chaotropic ions is consistent with many observations, all of which suggest that the scrapie agent contains a protein component that is essential for the maintenance of infectivity. Thus, it is unlikely that the agent is composed only of a "naked" nucleic acid. Certainly, if the agent were a naked nucleic acid, its lability in alkali virtually eliminates the possibility that it is composed of a single-stranded molecule of DNA." Ted also write us: "There is actually a treatment for Mad Cow Disease. Well, the prions won't go away, but it is no longer active. So in effect, there is a cure if you can make the prions no longer active. However, you must take it continuously.
The idea is to put DMSO (dimethyl sulfoxide) in your drinking water a couple of drops per liter to inactivate prions. Dimethyl sulfoxide is found in nature and in rainwater and is quite safe. I also drink it regularly. What DMSO does is in very low concentration (higher might be more effective), it deactivates prions. However when DMSO is no longer there, the prions is again activated.
(Source) http://www.priondata.org/data/A_DMSO.html )
The idea is if anybody having mad cow (or MIGHT GET ONE FROM EATING BEEF!!) drinks water with small amounts of DMSO for the rest of his life, mad cow will go away and hence a cure.
My idea is when DMSO is inactivated, if you managed to change the diets you are eating where manganese (and organaophospate insecticide) is no longer in the excess or eat food with less manganese for a long period of time or taking calcium EDTA (a common treatment for managanese toxicity), it is possible along with DMSO, to effect the further progression and possibly remission of Mad Cow.
As you know, the cause of mad cow is actually caused by organaophospate insecticide where the food is rich in manganese is what causes mad cow in the first place
Also, EVIDENCE OF DMSO inactivating Prions is located here:
Source: http://www.priondata.org/data/A_DMSO.html
Prion disease: an opportunity?
The fact that prion rods are dissolved in quite low concentrations of DMSO, and lose their infectivity in the process is interesting. However the fact is that the infectivity is returned when the DMSO is taken away and the rods reform (Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R. Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods. J Biol Chem 2001 Apr 27;276(17):14324-8 see abstract.
Considering its structure it is remarkably low toxicity and the possibility remains that the drug could be used to lower the amount of amyloid in the brain after other drugs had been used to actually stop the production of new PrPsc (e.g. Glivek?). This may lead to a progressive loss of infectivity in the brain and a lower risk to the brain from the stimulation of microglia and hence damage to the cellular structure that the chemicals that these cells release are causing.
Patients describe the drug as not being particularly toxic but others around them describe an 'awful' smell of the compound in the breath and fluids of the patient.
Ruth Gabizon at the Prion Therapeutics conference in December 2002 in Paris said that the phenomenon of DMSO dissolving of the prion fibrils should not be forgotten and, although this chemical was relatively toxic, there may be others that are not and DMSO could in fact be used for a short period in a long term therapy program.
Medical Abstract of Prions inactivated by DMSO is located here:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=11152454&dopt=Abstract
And this is the Abstract:
Reconstitution of prion infectivity from solubilized protease-resistant PrP and nonprotein components of prion rods.
Shaked GM, Meiner Z, Avraham I, Taraboulos A, Gabizon R.
Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, Jerusalem 91120, Israel.
The scrapie isoform of the prion protein, PrP(Sc), is the only identified component of the infectious prion, an agent causing neurodegenerative diseases such as Creutzfeldt-Jakob disease and bovine spongiform encephalopathy. Following proteolysis, PrP(Sc) is trimmed to a fragment designated PrP 27-30. Both PrP(Sc) and PrP 27-30 molecules tend to aggregate and precipitate as amyloid rods when membranes from prion-infected brain are extracted with detergents. Although prion rods were also shown to contain lipids and sugar polymers, no physiological role has yet been attributed to these molecules. In this work, we show that prion infectivity can be reconstituted by combining Me(2)SO-solubilized PrP 27-30, which at best contained low prion infectivity, with nonprotein components of prion rods (heavy fraction after deproteination, originating from a scrapie-infected hamster brain), which did not present any infectivity. Whereas heparanase digestion of the heavy fraction after deproteination (originating from a scrapie-infected hamster brain), before its combination with solubilized PrP 27-30, considerably reduced the reconstitution of infectivity, preliminary results suggest that infectivity can be greatly increased by combining nonaggregated protease-resistant PrP with heparan sulfate, a known component of amyloid plaques in the brain. We submit that whereas PrP 27-30 is probably the obligatory template for the conversion of PrP(C) to PrP(Sc), sulfated sugar polymers may play an important role in the pathogenesis of prion diseases.
PMID: 11152454 [PubMed]
Here is some more citations using DMSO and mad cow:
source links:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12914974&query_hl=7
1: Brain Res. 2003 Sep 5;983(1-2):137-43. Related Articles,Links
Dimethyl sulfoxide delays PrP sc accumulation and disease symptoms in prion-infected hamsters.
Shaked GM, Engelstein R, Avraham I, Kahana E, Gabizon R.
Department of Neurology, The Agnes Ginges Center for Human Neurogenetics, Hadassah University Hospital, 91120, Jerusalem, Israel.
PrP(Sc), an aberrantly folded protein, is the only identified component of the prion, an agent causing fatal neurodegenerative diseases such as scrapie and bovine spongiform encephalopathy. Dimethyl sulfoxide (DMSO) has been shown to reduce the accumulation of PrP(Sc) in scrapie-infected (ScN2a) cells, and to inhibit its aggregation in vitro. In humans, DMSO was used successfully in the treatment of various peripheral amyloidotic diseases. Here we show that administration of DMSO to scrapie-infected hamsters significantly prolonged disease incubation time, as well as delayed the accumulation of PrP(Sc) in Syrian hamster brains. Interestingly, administration of DMSO to scrapie sick hamsters resulted in increased clearance of protease-resistant PrP in their urine. We conclude that although DMSO by itself may not be sufficient to cure prion diseases, it may be considered as a component in a 'cocktail' drug approach for these disorders. Also, urine PrP testing should be considered for the assessment of treatment efficacy.
PMID: 12914974 [PubMed - indexed for MEDLINE]
Disaggregating effect - or dispersion and possibly reversal of the conditions can also be helped using DMSO and a weak ethanol solution:
source links:
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=12719126&query_hl=7
Int J Biol Macromol. 2003 Mar;32(1-2):10-6. Related Articles,Links
Disaggregating effects of ethanol at low concentration on beta-poly-L-lysines.
Sabate R, Estelrich J.
Departament de Fisicoquimica, Facultat de Farmacia, Universitat de Barcelona. Avda. Joan XXIII s/n, Catalonia, Spain.
Protein aggregation is involved in a number of disorders, such as Alzheimer's disease, cystic fibrosis, and prion diseases. Such aggregates are formed by peptides in beta-conformation. The study of the processes of aggregation or its inhibition makes it necessary for the peptide to remain in a monomeric state at the beginning of aggregation assays. Using three poly-L-lysine as a model of beta-peptide, we measured the spectral changes occurring in the visible spectrum of Congo Red (CR), a diazo dye, in two solvent media, namely, an aqueous solution of ethanol 10% (v/v), and an aqueous solution of dimethyl sulfoxide (DMSO) 5% (v/v). Aggregation constants show that the presence of ethanol at low concentration produces a disaggregating effect, regardless of the degree of polymerisation of the peptide. This effect is considered to be due to the direct binding of ethanol molecules to the peptide. This binding undergoes an enhancement of the electrostatic repulsion among charged lysine chains.
There are many documented studies in DMSO in the treatment of Mad Cow (technically its Bovine Spongiform Encephalopathy (BSE) and Creutzfeldt-Jakob disease (CJD)). And it can really technical if you want more documented details. It will take me several hundred pages to cover everything on this topic to do it justice, and it goes beyond my available time. However, I can refer you to several places which will help you further research and discover yourself that there are answers out there.
Here is an article excerpt as well as the link source to the full article with all the citations, and scientific studies:
source: http://www.doewatch.com/gws.html
"...Even the factors of high rates of ALS seen in the GW vets is directly associated with the GSH and SOD enzymes. ALS is associated with upsets of copper and manganese that form these enzymes. The problems of Mad Cow and Prion linked illnesses are caused by these same factors. Mad Cow effects come from a systemic shift toward Mn-SOD from the Cu-Zn-SOD. When sulfur bearing compounds like DMSO are applied to Mad Cow affected brain tissues, the plaques dissipate, and DMSO appears to act as GSH in supplying the sulfur to remove the toxic metals from the brain that attract the SOD needed for myelin repair.."
The following are research citations of using DMSO at www.pubmed.org in the treatment of mad cow (CJD):
1: Brain Res Mol Brain Res. 2004 Apr 7;123(1-2):37-44. Related Articles,Links
Doxycycline and protein folding agents rescue the abnormal phenotype of familial CJD H187R in a cell model. Gu Y, Singh N.
Institute of Pathology, Case Western Reserve University, 2085 Adelbert Road, Cleveland, OH 44106, USA.
Familial Creutzfeldt-Jakob disease (CJD) comprises a group of neurodegenerative disorders for which currently there is no treatment. In this study, we evaluated the efficacy of drugs approved for human use, and protein folding agents in reversing the mutant phenotype of familial CJD H187R in a cell model. For an efficient experimental readout, green fluorescent protein (GFP)-tagged mutant prion protein (PrP(187R-GFP)) and wild-type PrP (PrP(C-GFP)) were expressed in human neuroblastoma cells. We report that unlike PrP(C-GFP) that is expressed on the cell surface, PrP(187R-GFP) accumulates in the lysosomes of transfected cells. Treatment of PrP(187R-GFP) cells with quinacrine or doxycycline, agents known to inhibit the replication of PrP-scrapie (PrP(Sc)) in experimental models, gave conflicting results; doxycycline reverted the mutant phenotype of PrP(187R-GFP) cells, whereas quinacrine had no effect. The concentration of doxycycline used in these studies is well within the plasma concentration of patients receiving a 250-600 mg dose two to three times daily. Interestingly, exposure of PrP(187R-GFP) cells to low temperature (28 degrees C) or to the chemical chaperones dimethyl sulphoxide (DMSO) and glycerol also reversed the mutant phenotype. These data suggest that doxycycline and protein folding agents may hold promise as therapeutic agents for familial CJD H187R and other familial disorders that share similar pathogenic mechanisms.
PMID: 15046864 [PubMed - indexed for MEDLINE]
Below, the citation Me2SO4 is another name for DMSO, since full name is DimethylSulfoxide.
1: J Biol Chem. 1999 Jun 18;274(25):17981-6. Related Articles,Links
Protease-resistant and detergent-insoluble prion protein is not necessarily associated with prion infectivity.
Shaked GM, Fridlander G, Meiner Z, Taraboulos A, Gabizon R.
Department of Neurology, Hadassah University Hospital, Jerusalem 91120, Israel.
PrPSc, an abnormal isoform of PrPC, is the only known component of the prion, an agent causing fatal neurodegenerative disorders such as bovine spongiform encephalopathy (BSE) and Creutzfeldt-Jakob disease (CJD). It has been postulated that prion diseases propagate by the conversion of detergent-soluble and protease-sensitive PrPC molecules into protease-resistant and insoluble PrPSc molecules by a mechanism in which PrPSc serves as a template. We show here that the chemical chaperone dimethyl sulfoxide (Me2SO) can partially inhibit the aggregation of either PrPSc or that of its protease-resistant core PrP27-30. Following Me2SO removal by methanol precipitation, solubilized PrP27-30 molecules aggregated into small and amorphous structures that did not resemble the rod configuration observed when scrapie brain membranes were extracted with Sarkosyl and digested with proteinase K. Interestingly, aggregates derived from Me2SO-solubilized PrP27-30 presented less than 1% of the prion infectivity obtained when the same amount of PrP27-30 in rods was inoculated into hamsters. These results suggest that the conversion of PrPC into protease-resistant and detergent-insoluble PrP molecules is not the only crucial step in prion replication. Whether an additional requirement is the aggregation of newly formed proteinase K-resistant PrP molecules into uniquely structured aggregates remains to be established.
PMID: 10364247 [PubMed - indexed for MEDLINE]
People treating mad cow using hyperbaric chambers:
source links:
http://www.sptimes.com/2004/01/12/State/South_Florida_mad_cow.shtml
The best way is prevention, and you need to know the source of mad cow. There are some government policy questions that people need to be aware of not to be infected with mad cow:
source link: http://www.consumerfed.org/releases2.cfm?filename=madcowcredibility.txt
Carol Tucker Foreman served as assistant secretary for food and consumer services, US Department of Agriculture, 1977-81. Her responsibilities included meat, poultry and egg inspection.
I hope this answers some of your questions regarding the issues of prions, mad cow diseases, policy issues, the use of DMSO.
The likely cause of mad cow theory is best explained by Mr. Purdey:
http://www.mercola.com/2000/dec/17/bovine_spongiform_disease.htm
Insecticide Causes Mad Cow Disease
by Fintan Dunne Research by Kathy McMahon
Reprinted from eionews.com, email - [email protected]
Pharmaceutical interests in the UK are ignoring new scientific research that shows the insecticide used in the UK government's own warble-fly campaigns triggered the UK surge of 'Mad Cow' disease.
Latest experiments by Cambridge University prion specialist, David R. Brown, have shown that manganese bonds with prions. Other researchers work shows that prions in the bovine spine -- along which insecticides are applied -- can be damaged by ICI's Phosmet organophosphate(OP) insecticide -causing the disease.
British scientists have led the current theory that an infectious prion in bonemeal fed to cattle causes bovine spongiform disease (BSE).
Infectious prions are also claimed to cause new variant Creutzfeld-Jakob Disease (CJD) in humans -from ingesting beef. But the infectious prion theory serves to obscure a tragic chemical poisoning scandal behind the majority of BSE cases.
The new work proves that the prions can bond with manganese in animal feeds or mineral licks. These manganese prions cause the neurological degeneration seen in BSE. By a similar process, prions in human brains are damaged by lice lotions containing organophosphate. This can result in neurological diseases like CJD and Alzheimers -later in life.
Many might be surprised to hear that organophosphates were developed by Nazi chemists during the course World War Two, as a chemical weapon nerve agent. One formulation of the insecticide -- Maneb, or Mancozeb -- actually contains manganese in addition to organophosphate.
The marginalized research has devestating financial implications for ICI. It would provide a firm basis for litigants -who could include CJD sufferers, farmers across the world and families of the many British farmers who committed suicide during this BSE debacle.
Phosmet organophosphate has been used at high doses in British warble fly campaigns. In 1996, ICI subsidiary Zeneca sold the phosmet patent to a PO Box company in Arizona called Gowan -just one week before the UK government admitted to a link between BSE and nvCJD.
The politically well-connected British pharmaceuticals group, ICI has the financial and political clout to block research into any cause other than the infective model. Indeed no substantive alternative research has been done. British BSE disease management and research bodies have taken decisions that do not seem guided by spirited scientific enquiry. Mysterious prions that jump species is the preferred research arena.
Scientist and organic farmer, Mark Purdey gave evidence to the UK BSE inquiry, that warble fly insecticide was the cause of the disease. The scientist wheeled out to rubbish Purdy's evidence -Dr. David Ray, later turned out to have been receiving funding from the insecticide manufacturer ICI.
A lobby group that includes Bayer, Monsanto, Novartis, Pfizer, Roche and Schering-Plough was behind the effort to discredit Purdey. In December 1999, the same David Ray was appointed to the UK Veterinary Products Committee (VPC) -a government body that licences animal medicines.
Purdey has been consistently denied even exploratory funding to extend his privately supported research. Yet the Purdey/Brown chemical poisoning model matches with the epidermiological spread of CJD clusters in humans. It also predicts the incidence of BSE-type diseases in animals. The accepted infectious model fits neither. The pharmaceutical industry is all the more determined to hide the chemical source of BSE and CJD, because a spotlight on chemicals would expose the role the insecticides in Alzheimer's -- another neurodegenerative disease -- that might lead to claims which would dwarf those from BSE and CJD litigants. In fact, two leading brain researchers into CJD and Alzheimers have died in suspicious circumstances in recent years.
In the United States, the Environmental Protection Agency is already reviewing Phosmet's safety. The Centers for Disease Control in the US has recently conducted experiments on mice that confirm the organophosphate risk. Not only is the EC beef slaughter campaign futile -because BSE disease is mostly non-infectious, but unless the underlying chemical cause is addressed, BSE will simply reappear from chemical causes. A new warble fly campaign is already underway in France using the organophosphate insecticide.
Of greater concern is that some lotions for scabies and head lice are now priming children and adults, for CJD and Alzheimers in later life.
Bonding The Prion
Cambridge University prion biochemist, David R. Brown is dismissive of the science behind the infectious model of BSE. He terms it "a very limited amount of science by a few assumed- reputable scientists." He insists there is "no evidence an infectious agent is present in either meat or milk."
"Simple tests on udder walls of cows -- which could easily detect an infectious prion -- have not been done, why I don't understand."
A number of researchers have found that organophosphate(OP) in systemic warble fly insecticide can deform the prion molecule, rendering it ineffective at buffering free radical effects in the body. Worse still, the prion is then partial to bond with manganese and become a 'rogue' prion. A chain reaction whereby rogue prions turn others to rogues also, can explain the bovine spongiform disease mechanism.
Brown showed how prion protein bonds benignly with copper, but lethally with manganese. Even natural variations in relative environmental availability of manganese versus copper can trigger prion degradation.
The CJD and BSE symptoms mirror 'manganese madness', an irreversible fatal neuro-psychiatric degenerative syndrome that plagued manganese miners in the first half of the last century
Shining a Light on Spongiform
Organic dairy farmer and peer-review-published independent scientist, Mark Purdey, says the accepted theory of transmission from BSE-infected cattle to human CJD -by bonemeal or meat, is dependent on a mutant prion that has never been isolated under the scientific protocol called Koch's postulates.
Purdey's insistence on sticking to the letter of this scientific law earned him the condemnation of UK officialdom when he first mooted his theory. But Purdey pointed to CJD clusters downwind of a British Phosmet production plant to back his case.
He gave evidence to the UK Government BSE inquiry and was supported by Conservative MP, Thessa Gorman. His views were discounted, but his subsequent research and the new Cambridge prion work have confirmed the alternative theory. Despite this, and the backing of a British peer, he is denied even exploratory funding.
Speaking from his rural English Somerset farm yesterday -as plans forge ahead for the European cattle cull, he asks:
"Why does CJD degeneration in humans begin in the retina, and why are CJD disease clusters found in high altitude locations?"
The question is rhetorical, and Purdey has an eye-opening answer. He argues that the prion molecule has a known natural role as a shock adsorber of damaging energy from ultraviolet rays and other oxidizing agents.
Once this prion defence system is rendered ineffective by organophosphates - for example in human head lice lotions, these oxidizing effects have an unmediated impact on tissues. Eventually, UV radiation damages the retina and oxidative stress destroys the brain tissues of CJD patients. This theory would expect to find higher CJD incidence in mountain regions -where UV radiation levels are elevated. That prediction holds true.
A similar but accelerated mechanism could be driving BSE. ICI's Phosmet organophosphate warble fly insecticide -applied on the backs of animals along the spinal column, similarly degrades prions. "Systemic versions of the insecticide are designed to make the entire cow carcass toxic to warble fly," explains Purdey. "Unfortunately it's toxic to prions too -especially those prions located just millimeters from the point of application."
The damaged prions are then ready to react with manganese in animal feed, or manganese sprayed on land or in mineral licks -to become the driving force of BSE neurodegeneration. Purdey says manganese-tipped prions set off lethal chain reactions that neurologically burn through the animal.
Chickens notoriously excrete most of the supplements fed to them -including manganese. And their manganese-rich excreta have been blended into cattle feed in the UK. Natural variations in the relative environmental availability of copper and manganese can also spur prion degeneration says Purdey.
From this research, any prudent person would conclude there is a significant risk attaching to the use of organophosphate in humans. Preparations for head lice and scabies are known to be overused in practice and might be priming users for CJ disease.
Purdey believes his bias for field work is the key to his success. He bemoans the "reductionism" of much lab-centered science. "I have traveled the world to investigate known clusters of spongiform disease -something mainstream researchers don't seem remotely interested in doing."
Since first postulating an environmental -rather than infectious- theory of spongiform diseases, Purdey has built evidence from around the world that explains and predicts the incidence in humans and animals: a cluster of CJD in Slovakia, Eastern Europe -around a manganese plant; Rocky Mountain deer with Chronic Wasting Disease (CWD), who were found to be eating pine needles rich in manganese; the futile slaughter of sheep in Cyprus -only for BSE to reemerge within years.
"The reappearance of BSE in Cyprus obviously points to an environmental cause," says Purdey, who is sanguine when reflecting on the condemnation of him by mainstream scientists.
"I suppose they have mortgages and kids who need to go to university," he muses. "Privately, some were agreeing with me, but then they would denounce me publicly. It was quite strange really."
The Money Trail
Critical scientists like Purdey are unlikely to prevail. The pharmaceutical industry holds most research purse strings, and would hardly energetically explore an avenue of research that could expose them to litigation for causing BSE. The official theory is lavishly funded, alternative theories rarely, if at all.
There are more explosive implications to his -and other's latest research. Purdey says similar organophosphate-induced protein deformation could also underlie Alzheimer's disease. If that were true, the litigation fallout would destroy some pharmaceutical giants, and a lot of very influential noses would be out of joint.
Disturbingly, Purdey and other brain researchers seem to have had an undue share of unfortunate accidents. Purdey's house was burned down and his lawyer who was working with him on Mad Cow Disease was driven off the road by another vehicle and subsequently died. The veterinarian on the case also died in a car crash -locally reported as: 'Mystery Vet Death Riddle. Dr. C. Bruton, a CJD specialist -- who had just produced a paper on a new strain of CJD -- was killed in a car crash before his work was announced to the public. Purdey speculates that Bruton might have known more than what was revealed in his last scientific paper. In 1996, leading Alzheimer's researcher Tsunao Saitoh, 46 and his 13 -year-old daughter were killed in La Jolla, California, in what a Reuters report described as a "very professionally done" shooting.
What Alzheimer's Disease, Mad Cow Disease, and CJ Disease have in common, is abnormal brain proteins and a putative link to organophosphates. Even Gulf War syndrome among returning veterans has been attributed, in part to the insecticide. But the sidelined scientists' suspicions are still largely ignored.
In their favour at the moment, is a growing unease on the part of the public. As BSE forges on and Governments panic, Science may be out to lunch on BSE, compromised by bovine spongythinking myopathy.
Do Not Use Systemic Organophosphate Insecticides
Do NOT treat children with OP head lice products - they may cause CJD and Alzheimer's
Do NOT treat your pets with OP anti-flea products
Do NOT treat cattle or animals with OP products - they may cause BSE
Do NOT give manganese to cattle previously dosed with a systemic OP
The relative availability of the metals copper and manganese in you local environment is a major factor in BSE & CJD
Additional Notes:
I contacted Mr. Purdey and there is possibility of chelation therapy or fulvic acid might be one possible method of reducing the metal toxins thus starving the source of the manganese from the renegate prions.
Majority of the public are not aware of Mr. Purdey's finding from insecticide, and environmental excess manganese, much less the treatment of such.
If you want to dig deeper please go to www.pubmed.org for more information. What is unusual is that there is news reports that Mad Cow has been misdiagnosed for Alzheimers and other similar conditions such as Parkinson's Disease and true figures may be much worse, however since incubation times are long, it may be too late before we can actually do the treatment.
Mycoplasma (fungus-like) is another possible leads as to the cause or a cofactor towards mad cow but this is just a hypothesis, which can be tested by examination of cows with the disease and test for present of fungus or mycoplasma of the brain. However,some indirect evidence is seen in certain people who died of Alzheimer were found to have fungus or algae in the brain. So this is circumspective and proof of hypothesis is sorely needed. If this is indeed confirmed anti-fungal drugs might be of some use in the treatment of mad cow. It is disappointing however, that no major funding for research on the nature, cause, and treatment of mad cow.
Suggestions for Farmers:
1. Checking of manganese level in feed. 2. Don't use organophosphate insecticide that has to do with warble flies. 3. Don't allow the Cows to feed on dead carcasses and chicken feces (chicken feces are high in manganese). 4. DMSO is currently used as a potential treatment for mad cows, however, preventive approach is recommended in adding small amounts of DMSO to feed which might deactivate prions before the feed is given to the cow. The possible uses of DMSO is important and can be used in possible sterilization of process food treatment before it reaches the public. Currently prions are not easily destroyed by either heat or acid. Therefore, DMSO (dimethyl sulfoxide appears a potential food additive to feed or processing of foods). A wider range of uses of DMSO may be in order. DMSO has more uses in cleaning and sterilization of carcasses as well. This is the only way to "deactivate" the prion that we know of based on all the studies.
5. I currently use DMSO to clean meat products, and small amounts to drinking water now and then, especially if the need arises to eat beef or meat products.
6. The use of GMO feed for cows is potentially deadly. Some studies point to the fact that prions which causes mad cow are much more deadly and spread much more quickly if GMO foods (such as G.M.O. soybeans is used). ONE OBVIOUS reasons that many are not aware of is corporations create GMO to better resist herbicide and pesticide, which implies higher organophosphate in these plants. However, getting into a debate with corporations that organophosphate content in plant is a waste of time. They will deny it anyway. The best method of attack is Genetically Modified plants are potentially dangerous is the best point of attack. There is a DNA exchange that is common in nature wherby GMO DNA do not exist in nature and can be exchanged with human DNA and this may bring about unestimable damage to the human genome. The science of this is fairly well known in academic circles but totally foreign from the press."
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(good grief!!! I had to edit this for the past hour, because of all the repetition and I think I've gotton it all)