Abstract
Alzheimer's disease (AD) is the leading cause of senile dementia, and is a complex disorder. The pathological hallmarks of AD were discovered by Dr. Alois Alzheimer in 1907, and include deposits of amyloid or senile plaques and neurofibrillar tangles. Plaques are composed of a peptide, termed the Aß peptide, that is derived by proteolytic processing of the amyloid precursor protein (APP), while neurofibrillar tangles result from a hyperphosphorylation of the tau protein. Mechanisms associated with the formation of plaques and neurofibrillar tangles and their respective contributions to the disease process have been intensely investigated. Proteolytic processing of APP that results in the generation of the Aß peptide is now well understood and is influenced by several proteins. Recent evidence suggests that the Aß levels are carefully regulated, and several proteases play an important role in removing the Aß peptide. Finally, it is becoming apparent that several members of the LDL receptor family play important roles in the brain, and may modulate the course of AD.
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Makarova, A., Williams, S.E. & Strickland, D.K. Proteases and lipoprotein receptors in Alzheimer's disease. Cell Biochem Biophys 41, 139–178 (2004). https://doi.org/10.1385/CBB:41:1:139
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DOI: https://doi.org/10.1385/CBB:41:1:139