APP at a glance.

نویسندگان

  • Michael S Wolfe
  • Suzanne Y Guénette
چکیده

The characteristic cerebral plaques of Alzheimer disease (AD) are primarily composed of an aggregation-prone 39-43residue peptide called amyloid (A ), which is a proteolytic product derived from the amyloid precursor protein (APP), a type I integral membrane protein (Hardy and Selkoe, 2002). The discovery of the APP gene was followed by the identification of missense mutations associated with familial, early-onset AD (FAD). These mutations are found in and around the A region of APP, and affect the production or aggregation properties of A . Those APP mutations near the C-terminal region of the A sequence specifically lead to increased proportions of the highly aggregation-prone 42residue form of A (A 42). Although two other APP-like proteins – APLP1 and APLP2 – are known, the A regions are not well conserved, and no FAD mutations have been identified in these genes.

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عنوان ژورنال:
  • Journal of cell science

دوره 120 Pt 18  شماره 

صفحات  -

تاریخ انتشار 2007