TY - JOUR
T1 - Neutrophil lysosomal degradation of human CRP
T2 - CRP-derived peptides modulate neutrophil function
AU - Shephard, E. G.
AU - Anderson, R.
AU - Beer, S. M.
AU - Jansen Van Rensburg, C. E.
AU - De Beer, F. C.
PY - 1988
Y1 - 1988
N2 - 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.
AB - 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.
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M3 - Article
C2 - 3168329
AN - SCOPUS:0023784451
SN - 0009-9104
VL - 73
SP - 139
EP - 145
JO - Clinical and Experimental Immunology
JF - Clinical and Experimental Immunology
IS - 1
ER -