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Neutrophil lysosomal degradation of human CRP: CRP-derived peptides modulate neutrophil function.

Authors
  • Shephard, E G
  • Anderson, R
  • Beer, S M
  • Van Rensburg, C E
  • de Beer, F C
Type
Published Article
Journal
Clinical and experimental immunology
Publication Date
Jul 01, 1988
Volume
73
Issue
1
Pages
139–145
Identifiers
PMID: 3168329
Source
Medline
License
Unknown

Abstract

Hydrolysis of human C-reactive protein (CRP) at pH 4.5 and pH 7.4 with neutrophil-derived lysosomal enzymes yielded 10% trichloroacetic acid soluble peptides (Mr less than 14,000). These peptides inhibited neutrophil superoxide production, chemotaxis, degranulation and phagocytosis at 2 micrograms/ml. This inhibition was not observed with native CRP or intermediate peptides (Mr greater than 14,000). CRP peptides (Mr less than 14,000) also caused a dose-related inhibition of Quin-2 fluorescence indicating interference with intracellular calcium movements during cell activation. These results point to a potential regulatory role for CRP-derived degradation products on neutrophils during inflammation.

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