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

T. Yamada, J. J. Liepnieks, B. Kluve-Beckerman, Merrill Benson

Research output: Contribution to journalArticle

42 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)94-97
Number of pages4
JournalScandinavian Journal of Immunology
Volume41
Issue number1
DOIs
StatePublished - 1995

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Serum Amyloid A Protein
Cathepsin B
Amyloid
Digestion
Leukocyte Elastase
Amyloid Plaques
Sulfhydryl Compounds
Polyacrylamide Gel Electrophoresis
Peptide Hydrolases

ASJC Scopus subject areas

  • Immunology

Cite this

Cathepsin B generates the most common form of amyloid A (76 residues) as a degradation product from serum amyloid A. / Yamada, T.; Liepnieks, J. J.; Kluve-Beckerman, B.; Benson, Merrill.

In: Scandinavian Journal of Immunology, Vol. 41, No. 1, 1995, p. 94-97.

Research output: Contribution to journalArticle

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