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CJD/Alzheimer-Like
Amyloidotic Spongiform
BSE In Italy

From Patricia Doyle, PhD
2-19-4
 
Hello Jeff - Why were they able to find the anomolous mutated prion disease in the two cows? They found it because they test every cow over 30 months. If this had occurred in the US, which I am sure there are cases in the US, we would not have identified the cases. In short, prion disease, and the new mutations of, are easily able to slip through and meat from these cows ends up on our dinner table.
 
"Both the human and cattle diseases cause holes to form in the brain. The Italian researchers found that, in addition to the holes, 2 cows had an accumulation of amyloid plaque in their brains. Amyloid plaques are an indication of Alzheimer's disease in humans. They have also been found in people with sporadic CJD but had not been found in cattle, the researchers said. the Italian research workers named the new form with amyloid plaques as bovine amyloidotic spongiform encephalopathy (BASE). "Although observed in only 2 cattle, the BASE phenotype could be more common than expected," they reported. Monaco said that he believes that the incidence could be as high as 5 percent among cattle with mad cow symptoms."
 
Patricia
 
BOVINE AMYLOIDOTIC SPONGIFORM ENCEPHALOPATHY - ITALY
A ProMED-mail post
 
ProMED-mail is a program of the
International Society for Infectious Diseases
www.isid.org
 
Date: Wed 18 Feb 2004
From: ProMED-mail promed@promedmail.org
Source: Newsday.com, Tue 17 Feb 2004 [edited]
 
http://www.newsday.com/news/health/ats-ap_health
15feb16,0,6976781.story?coll=sns-health-headlines
 
BASE: A New Form of Mad Cow Disease Discovered in 2 Italian Cows
 
Italian scientists have found a 2nd form of mad cow disease that more closely resembles the human Creutzfeldt-Jakob Disease (CJD) than the usual cow form of the illness. The brain-wasting diseases bovine spongiform encephalopathy (BSE)-- also known as mad cow disease -- and human CJD are caused by different forms of mutant proteins called prions. A number of people, mainly in the United Kingdom, have also suffered from what is called variant CJD [abbreviated as CJD (new var.) or vCJD in ProMED-mail], a brain disease believed to be acquired by eating meat from infected cows.
 
Now a team of Italian researchers reports a study of 8 cows with mad cow disease that found 2 of them had brain damage resembling the human victims of CJD. They said the cows were infected with prions that resembled those involved in the standard form of the human disease, called sporadic CJD, not the variant caused by eating infected meat. Salvatore Monaco, lead author of the new study, said the findings may indicate that cattle can also develop a sporadic form of the disease, but it might also be a new foodborne form of the illness.
 
Dr. Paul Brown of the National Institutes of Health said the finding does not indicate an increased threat to humans. If a new form of the disease were affecting humans, there would be an increase in the incidence of CJD, said Brown, who was not part of the research team. However, scientists in Europe have studied all cases of sporadic CJD for the last decade, and the incidence has not changed, said Brown, an expert in the disease, who works at the National Institute of Neurological Disease and Stroke.
 
Both the human and cattle diseases cause holes to form in the brain. The Italian researchers found that, in addition to the holes, 2 cows had an accumulation of amyloid plaque in their brains. Amyloid plaques are an indication of Alzheimer's disease in humans. They have also been found in people with sporadic CJD but had not been found in cattle, the researchers said. the Italian research workers named the new form with amyloid plaques as bovine amyloidotic spongiform encephalopathy (BASE). "Although observed in only 2 cattle, the BASE phenotype could be more common than expected," they reported. Monaco said that he believes that the incidence could be as high as 5 percent among cattle with mad cow symptoms.
 
But while human CJD and BASE share several characteristics, the Italian researchers cautioned against assuming a link between them. The findings of the team led by Monaco, of the Department of Neurological and Visual Science, Policlinico G.B. Rossi, in Verona, Italy, are reported in this week's online edition of Proceedings of the National Academy of Science. [The full text of the Abstract of this paper is reproduced below. - Mod.CP] Dr. Paul Brown said there have also been some unpublished reports from Japan of cows with a different form of mad cow disease.
 
The 1st case of mad cow disease in the United States was reported in December 2003 in Washington state, involving a cow imported from Canada. An investigation seeking other cattle from the same herd ended last week with Agriculture officials saying they had located all but 11 suspect animals and concluding the rest could not be found.
 
[Byline: Randolph E. Schmid]
 
--
ProMED-mail
<promed@promedmail.org
 
[The reference to the paper referred to above and the full text of the Abstract are as follows:
 
"Proceedings of the National Academy of Science of the USA,
10.1073/pnas.0305777101
<http://www.pnas.org/cgi/content/abstract/0305777101v1
 
Title: Identification of a second bovine amyloidotic spongiform encephalopathy: Molecular similarities with sporadic Creutzfeldt-Jakob disease. Authors: Cristina Casalone and seven others from the Centro di Referenza Nazionale per le Encefalopatie Animali, Istituto Zooprofilattico Sperimentale del Piemonte, Liguria e Valle d'Aosta, Via Bologna, 148, 10195 Turin, Italy; Department of Neurological and Visual Science, Section of Clinical Neurology, Policlinico G.B. Rossi, Piazzale L.A. Scuro, 10, 37134 Verona, Italy; Istituto Zooprofilattico Sperimentale della Lombardia ed Emilia Romagna, Via Bianchi, 9, 25124 Brescia, Italy; and Istituto Nazionale Neurologico "Carlo Besta," Via Celoria 11, 20133 Milan, Italy.
 
Abstract: Transmissible spongiform encephalopathies (TSEs), or prion diseases, are mammalian neurodegenerative disorders characterized by a post-translational conversion and brain accumulation of an insoluble, protease-resistant isoform (PrPSc) of the host-encoded cellular prion protein (PrP/C). Human and animal TSE agents exist as different phenotypes that can be biochemically differentiated on the basis of the molecular mass of the protease-resistant PrP/Sc fragments and the degree of glycosylation. Epidemiological, molecular, and transmission studies strongly suggest that the single strain of agent responsible for bovine spongiform encephalopathy (BSE) has infected humans, causing variant Creutzfeldt-Jakob disease. The unprecedented biological properties of the BSE agent, which circumvents the so-called "species barrier" between cattle and humans and adapts to different mammalian species, has raised considerable concern for human health. To date, it is unknown whether more than one strain might be responsible for cattle TSE or whether the BSE agent undergoes phenotypic variation after natural transmission. Here we provide evidence of a second cattle TSE. The disorder was pathologically characterized by the presence of PrP-immunopositive amyloid plaques, as opposed to the lack of amyloid deposition in typical BSE cases, and by a different pattern of regional distribution and topology of brain PrPSc accumulation. In addition, Western blot analysis showed a PrP/Sc type with predominance of the low molecular mass glycoform and a protease-resistant fragment of lower molecular mass than BSE-PrP/Sc. Strikingly, the molecular signature of this previously undescribed bovine PrP/Sc was similar to that encountered in a distinct subtype of sporadic Creutzfeldt-Jakob disease."
 
It should be emphasized that both Italian cows, one 15 years old and one 11, appeared healthy. Their unusual strain was discovered only because Italy tests all cattle over 30 months old slaughtered for human food. By August 2003, it had tested 1.6 million and found 103 that tested positive for prions. - Mod.CP]
 
Patricia A. Doyle, PhD
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