Alzheimer's beta-secretase cleaves a glycosyltransferase as a physiological substrate

Glycoconj J. 2004;20(1):59-62. doi: 10.1023/B:GLYC.0000016743.25495.45.

Abstract

Alzheimer's beta-secretase (BACE1) is a membrane-bound protease that cleaves the amyloid precursor protein (APP) in the trans-Golgi network, an initial step in the pathogenesis of Alzheimer's disease. Although BACE1 is distributed among various tissues including brain, its physiological substrate other than APP have not been identified. We have recently found that when BACE1 was overexpressed in COS cells together with alpha2,6-sialyltransferase (ST6Gal I), the secretion of ST6Gal I markedly increased, suggesting that BACE1 cleaves ST6Gal I as a physiological substrate. Thus BACE1 is the first identified protease that is responsible for the cleavage and secretion of glycosyltransferases.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alzheimer Disease / enzymology*
  • Alzheimer Disease / etiology
  • Amyloid Precursor Protein Secretases
  • Amyloid beta-Protein Precursor / metabolism
  • Aspartic Acid Endopeptidases / metabolism*
  • Endopeptidases
  • Golgi Apparatus / metabolism
  • Humans
  • Sialyltransferases / metabolism*
  • Substrate Specificity
  • beta-D-Galactoside alpha 2-6-Sialyltransferase

Substances

  • Amyloid beta-Protein Precursor
  • Sialyltransferases
  • Amyloid Precursor Protein Secretases
  • Endopeptidases
  • Aspartic Acid Endopeptidases
  • BACE1 protein, human
  • beta-D-Galactoside alpha 2-6-Sialyltransferase