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- WASHINGTON (Reuters) - Proteins
linked with Alzheimer's and the human version of mad cow disease have some
striking similarities -- and thus might be susceptible to similar treatments,
a researcher said on Wednesday.
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- Both diseases are marked by a gradual deterioration of
the brain and both are associated with rogue proteins. Both are always
fatal.
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- Chi Ming Yang, a professor of chemistry at Nankai University
in Tianjin, China, said he used a computer model to map the prion protein
associated with Creutzfeldt-Jakob disease (CJD), the human equivalent of
mad cow disease, and the amyloid precursor protein associated with Alzheimer's.
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- Proteins are made up of amino acids, and Yang told a
meeting of the American Chemical Society in Washington that he found a
similar pattern of amino acids in the two proteins -- a reductive amino
acid followed by three non-reductive amino acids.
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- ``This suggests a common molecular mechanism underlying
the initiation stages of sporadic Alzheimer's disease and both sporadic
and genetic prion diseases,'' he said in a statement.
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- Reductive amino acids are more prone to damage by free
radicals -- the molecules than can damage cell DNA in the same chemical
process that underlies rusting.
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- Alzheimer's is the most common cause of dementia, affecting
an estimated 12 million people worldwide. The cause is not known but hallmarks
of the disease include messy ``tangles'' of nerve fibers and ``plaques''
rich in the amyloid proteins.
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- CJD is the human version of bovine spongifirm encephalitis
(BSE or mad cow disease). It occurs naturally in about one in a million
people but a new version linked with eating BSE-infected meat has turned
up in Britain.
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- Prion proteins that do not fold normally are believed
to cause BSE and CJD.
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