Siman R, Christoph G
Cephalon, Inc., West Chester, PA 19380.
Biochem Biophys Res Commun. 1989 Dec 29;165(3):1299-304. doi: 10.1016/0006-291x(89)92744-7.
The beta-amyloid peptide is generated by proteolytic processing of a family of beta-amyloid precursor proteins. Here we report that beta-amyloid precursor proteins have a primary structure motif known as a PEST sequence, which is predictive of the class of most protease-sensitive rapidly turning over proteins. Consistent with this, the precursors were extraordinarily susceptible to degradation by the calcium-dependent protease calpain I. The identification of beta-amyloid precursors as PEST sequence-containing proteins has implications for both the normal cellular function of beta-amyloid precursor proteins and the mechanisms regulating their expression and processing.
