Molecular advances in understanding inherited prion diseases |
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Authors: | Brown David R |
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Institution: | (1) Department of Biology and Biochemistry, Bath University, BA2 7AY Bath, UK |
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Abstract: | The prion diseases are neurodegenerative disorders that have attracted great interest because of the possible link between
bovine spongiform encephalopathy (BSE) and variant Creutzfeldt-Jakob disease (CTD) in humans. Possible transmission of these
diseases has been linked to a single protein termed the prion protein. This protein is an abnormal isoform of a normal synaptic
glycoprotein. The majority of prion diseases does not appear to be caused by transmission of an infectious agent but occur
spontaneously with no known cause. The strongest supporting evidence that the prion protein is the causative agent in prion
disease comes from specific inheritable forms of prion disease which are linked to single point mutations in the prion protein
gene. Paradoxically, these point mutations, although autosomal dominant with 100% penetrance do not lead to disease until
late in life. Molecular techniques are now being used extensively to determine how these point-mutations alter the prion protein’s
normal structure and activity. This review deals with the latest insights into how inherited mutations in the prion protein
gene lead to neurodegenerative disease. |
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Keywords: | Prion TSE Gerstmann-Str?ussler-Scheinker Creutzfeldt-Jakob Fatal Familial Insomnia neurodegeneration peptide |
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