NEUTROPHIL LYSOSOMAL DEGRADATION OF HUMAN CRP - CRP-DERIVED PEPTIDES MODULATE NEUTROPHIL FUNCTION

  • 1 July 1988
    • journal article
    • research article
    • Vol. 73  (1) , 139-145
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 < 14,000). These peptides inhibited neutrophil superoxide production, chemotaxis, degranulation and phagocytosis at 2 .mu.g/ml. This inhibition was not observed with native CRP or intermediate peptides (Mr > 14,000). CRP peptides (Mr < 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.