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 (M(r) < 14,000). These peptides inhibited neutrophil superoxide production, chemotaxis, degranulation and phagocytosis at 2 μg/ml. This inhibition was not observed with native CRP or intermediate peptides (M(r) > 14,000). CRP peptides (M(r) < 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.
|Number of pages||7|
|Journal||Clinical and Experimental Immunology|
|State||Published - 1988|
ASJC Scopus subject areas
- Immunology and Allergy