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Abstract
The basic pathogenesis of numerous neurodegenerative disorders is now thought to be related to abnormal protein conformation. The common theme in all these diseases is the conversion of a normal cellular andor circulating protein into an insoluble, aggregated, β-sheet rich form which is deposited in the brain, sometimes in the form of amyloid. These deposits are toxic and produce neuronal dysfunction and death. The most common of these illnesses is Alzheimer's disease (AD), in which a central event is the conversion of the normal soluble amyloid p (SAP) peptide to amyloid p (AP) within neuritic plaques and cerebral vessels. A unique category of the conformational conditions areprion related diseases (or prionoses), where the etiology is thought to be related to conversion of the normal prion protein, PrPC, into an infectious and pathogenic form, PrPSc. In the case of AD and the prionoses, the conformational change can be influenced by the presence of mutations in various gene products, as well as by chaperone proteins. Apolipoprotein E is thought to act as such a chaperone protein in AD; however, among the prionoses such a protein has been hypothesized to exist only by indirect evidence and is called “protein X”. Our growing understanding of the mechanisms involved in this category of diseases, raises the possibility of therapeutic approaches based directb on the prevention and reversal of pathologic protein conformation.