Cathepsin B Generates the Most Common Form of Amyloid A (76 Residues) as a Degradation Product from Serum Amyloid A
| Autor: | Merrill D. Benson, Barbara Kluve-Beckerman, Toshiyuki Yamada, Juris J. Liepnieks |
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| Rok vydání: | 1995 |
| Předmět: |
Amyloid
Molecular Sequence Data Immunology In Vitro Techniques Cathepsin B Cathepsin L1 Amyloid precursor protein Animals Humans Amino Acid Sequence Serum amyloid A Protein Precursors Serum Amyloid A Protein DNA Primers Base Sequence Pancreatic Elastase biology Chemistry P3 peptide General Medicine Molecular biology Recombinant Proteins Biochemistry of Alzheimer's disease Amyloid A Protein Biochemistry biology.protein Cattle Leukocyte Elastase |
| Zdroj: | Scandinavian Journal of Immunology. 41:94-97 |
| ISSN: | 1365-3083 0300-9475 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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