Refolding or misfolding of another protein endogenous to human brain tissue, P-amyloid, is also a prominent feature of Alzheimer's disease. While the root cause of Alzheimer's disease remains elusive, the characteristic senile plaques and neurofibrillary bundles contain aggregates of the protein P-amyloid, a 4.3-kDa polypeptide produced by proteolytic cleavage of a larger protein known as amyloid precursor protein. In Alzheimer's disease patients, levels of P-amyloid become elevated, and this protein undergoes a conformational transformation from a soluble a helix-rich state to a state rich in P sheet and prone to self-aggregation. Apolipopro-tein E has been implicated as a potential mediator of this conformational transformation.
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