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• W2055334477 abstract "We have investigated the conditions that lead to the generation of the neutrophil-activating peptide 2 (NAP-2) from its precursor, the platelet-derived connective tissue-activating peptide III (CTAP-III). Lysed platelets were found to contain predominantly CTAP-III in the cytosolic fraction, but further truncated derivatives, among these NAP-2, occurred tightly bound to the membrane fraction of fresh platelets. NAP-2 biological activity, as measured by the induction of enzyme release in human neutrophils [polymorphonuclear leukocytes (PMN)] was released by stimulated platelets to a low degree. Much higher activities were formed in the presence of peripheral blood leukocytes. Coincubation of CTAP-III with PMN resulted in the almost complete conversion of the precursor to NAP-2, as did incubation of CTAP-III with PMN-conditioned medium. In both situations, the generation of NAP-2 could by prevented by serine-protease inhibitor phenylmethylsulfonyl fluoride but not by inhibitors specific for Ca2+-dependent or thiol proteases. From several PMN-derived proteases tested, only cathepsin G had the capacity to cleave CTAP-III into NAP-2 with high specificity and in a relatively short period of time (30 min). Our data indicate that NAP-2, released by platelets in small quantities, could cause PMN to enter into a positive feedback cycle by initiating the secretion of serine proteases, which in turn could convert platelet-derived CTAP-III into biologically active NAP-2." @default.
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• W2055334477 date "1991-07-01" @default.
• W2055334477 modified "2023-09-29" @default.
• W2055334477 title "Neutrophils can generate their activator neutrophil-activating peptide 2 by proteolytic cleavage of platelet-derived connective tissue-activating peptide III" @default.
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• W2055334477 doi "https://doi.org/10.1016/1043-4666(91)90499-4" @default.
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