Cysteine 73 in bleomycin hydrolase is critical for amyloid precursor protein processing

Biochem Biophys Res Commun. 2001 May 18;283(4):994-9. doi: 10.1006/bbrc.2001.4860.

Abstract

Human bleomycin hydrolase (hBH) is a neutral cysteine protease that may regulate the secretion of soluble amyloid precursor protein (APP) and amyloid beta (A(beta)), which is a major constituent of the Alzheimer's disease-associated amyloid plaques. We have now determined that APP interacts with hBH by using yeast two hybrid methods and in vitro binding studies revealed that APP interacted with a 68 amino acid region that includes the catalytic domain of hBH. Ectopic expression of hBH increased the secretion of A(beta) but not of a second secreted protein, apolipoprotein A-I. Expression of hBH in which the catalytic cysteine 73 was mutated to serine failed to increase A(beta) secretion. These results indicate a critical role for cysteine 73 of hBH in mediating APP processing.

Publication types

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

MeSH terms

  • Amyloid beta-Protein Precursor / metabolism*
  • Animals
  • Apolipoprotein A-I / metabolism
  • Base Sequence
  • CHO Cells
  • Cricetinae
  • Cysteine / metabolism*
  • Cysteine Endopeptidases / chemistry
  • Cysteine Endopeptidases / genetics
  • Cysteine Endopeptidases / metabolism*
  • DNA Primers
  • Mice
  • Mutagenesis, Site-Directed
  • Protein Processing, Post-Translational*

Substances

  • Amyloid beta-Protein Precursor
  • Apolipoprotein A-I
  • DNA Primers
  • Cysteine Endopeptidases
  • bleomycin hydrolase
  • Cysteine