Cathepsin B generates the most common form of amyloid A (76 residues) as a degradation product from serum amyloid A

Scand J Immunol. 1995 Jan;41(1):94-7. doi: 10.1111/j.1365-3083.1995.tb03538.x.

Abstract

Amyloid A protein (AA), the chief constituent of reactive amyloid deposits, is derived from serum amyloid A (SAA) and most commonly corresponds to the amino-terminal 76 residues (AA76). Digestion of recombinant human SAA1 with a lysosomal thiol protease, cathepsin B, and analysis of the products by SDS-PAGE and amino-terminal sequencing revealed that AA76 was generated as a minor and transient degradation product. Digestion with neutrophil elastase generated intermediates different from AA76. This finding suggests that cathepsin B may play an important role in amyloid fibrilogenesis by converting SAA to AA.

Publication types

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

MeSH terms

  • Amino Acid Sequence
  • Amyloid / metabolism*
  • Animals
  • Base Sequence
  • Cathepsin B / metabolism*
  • Cattle
  • DNA Primers / chemistry
  • Humans
  • In Vitro Techniques
  • Leukocyte Elastase / metabolism
  • Molecular Sequence Data
  • Pancreatic Elastase / metabolism
  • Protein Precursors
  • Recombinant Proteins
  • Serum Amyloid A Protein / metabolism*

Substances

  • Amyloid
  • DNA Primers
  • Protein Precursors
  • Recombinant Proteins
  • Serum Amyloid A Protein
  • Pancreatic Elastase
  • Leukocyte Elastase
  • Cathepsin B