Neutrophil lysosomal degradation of human CRP: CRP-derived peptides modulate neutrophil function.
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.
Shephard
E G
EG
Department of Internal Medicine, Faculty of Medicine, University of Stellenbosch, Tygerberg, South Africa.
Anderson
R
R
Beer
S M
SM
Van Rensburg
C E
CE
de Beer
F C
FC
D002097:C-Reactive Protein / Q000378:metabolism*; D002465:Cell Movement / Q000187:drug effects; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008247:Lysosomes / Q000201:enzymology*; D009504:Neutrophils / Q000187:drug effects / Q000378:metabolism / Q000502:physiology*; D010455:Peptides / Q000494:pharmacology*; D010587:Phagocytosis / Q000187:drug effects
D010455:Peptides; D002097:C-Reactive Protein