Cathepsin B Generates the Most Common Form of Amyloid A (76 Residues) as a Degradation Product from Serum Amyloid A
- 1 January 1995
- journal article
- Published by Wiley in Scandinavian Journal of Immunology
- Vol. 41 (1) , 94-97
- https://doi.org/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.Keywords
This publication has 15 references indexed in Scilit:
- Fibril formation from recombinant human serum amyloid ABiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1994
- Neutrophil Proteases Associated with Amyloid FibrilsBiochemical and Biophysical Research Communications, 1993
- Human serum amyloid A. Three hepatic mRNAs and the corresponding proteins in one person.Journal of Clinical Investigation, 1988
- The distribution of cathespin b in human tissuesThe Journal of Pathology, 1985
- Transformation of Amyloid Precursor SAA to Protein AA and Incorporation in Amyloid Fibrils in VivoScandinavian Journal of Immunology, 1985
- The heterogeneity of protein AA in secondary (reactive) systemic amyloidosisBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Amyloid Deposits and AmyloidosisNew England Journal of Medicine, 1980
- An Unusually Large (83 Amino Acid Residues) Amyloid Fibril Protein AA from a Patient with Waldenström's Macroglobulinaemia and AmyloidosisScandinavian Journal of Immunology, 1980
- The Complete Amino‐Acid Sequence of Non‐Immunolobulin Amyloid Fibril Protein AS in Rheumatoid ArthritisEuropean Journal of Biochemistry, 1974
- The Amino Acid Sequence of a Major Nonimmunoglobulin Component of Some Amyloid FibrilsJournal of Clinical Investigation, 1972