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From Bench to Bedside: BACE1, Beta-Site Amyloid Precursor Protein Cleaving Enzyme 1, From Basic Science to Clinical Investigation
Abstract
Alzheimer’s disease (AD) is a constantly progressive and highly complex neurodegenerative disease, and there are many ways to molecularly characterize the various stages. Morphologically, AD patients are characterized by neurofibrillar abnormalities associated with pathological hyperphosphorylation of tau protein, and deposits of ß– amyloid peptides (Aß). There is an overwhelming amount of information to support the hypothesis that generation, formation, and ß-amyloid deposits play key mechanistic roles in the early development of AD. It is known that the cause of early-onset familial AD (FAD) is due to mutations in three genes which cause an increase in the production of the toxic peptide, Aß42. The molecules that cause the proteolytic activities of beta and gamma secretase, two proteases that free the Aß-peptide by endoproteolyzing APP, have recently been discovered. Homologous to BACE1, BACE2 was also a recent discovery (Lin et al, 2000; Vassar et al, 1999; Yan et al, 1999), and together these two enzymes make up a new family of transmembrane aspartic proteases. The key enzyme, BACE1, initiates the formation of Aß, represents a candidate biomarker, as well as a drug target for AD, exhibit all the functional properties of ß–secretase. This chapter will review the biology of BACE1 and focus attention to BACE1 as a candidate biomarker for the early detection, prediction, and biological activity in AD.
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