Proteolysis of human C-reactive protein by neutrophil-derived lysosomal enzymes generates peptides which modulate neutrophil function: Implication to the anti-inflammatory mechanism |
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Authors: | Eran J. Yavin Oren Rosen Michel Pontet Enid G. Shephard Mati Fridkin |
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Affiliation: | (1) Department of Organic Chemistry, The Weizmann Institute of Science, 76100 Rehovot, Israel;(2) Laboratoire de Biochimie, Hospital Jean Verdier, F-93143 Bondy Cedex, France;(3) MRC Liver Research Centre, Department of Medicine, University of Cape Town, Cape Town, South Africa |
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Abstract: | Summary Proteolysis of human C-reactive protein (CRP) by lysosomal enzymes derived from human neutrophils is shown to yield short peptides capable of modulating the production of superoxide ions by stimulated human neutrophils. Thus, fractionation of trichloroacetic acid-soluble digestion mixtures by HPLC yielded the following peptides: Ser-Tyr (1), Gly-Tyr (2), Phe-Glu-Val-Pro-Glu-Val-Thr (3), Trp-Asp-Phe-Val (4), Asn-Met-Trp-Asp-Phe-Val (5) and Gln-Leu-Trp-Pro (6). These peptides, corresponding to CRP sequences 18–19, 48–49 and/or 72–73, 84–90, 162–165, 160–165 and 203–206, respectively, have been synthesized and peptides 2, 3 and in particular peptide 6 were found to significantly inhibit neutrophilic function. The results suggest that CRP-derived peptides may be capable of regulating superoxide ion production by neutrophils in vivo during the acute phase response as part of a complex protective mechanism. |
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Keywords: | Acute phase response Superoxide ion |
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