Abstract
In recent years evidence has been accumulated that platelets besides their function in coagulation play an important role in inflammation and wound repair. Upon activation platelets release a variety of mediators, among which members of the α-chemokine subfamily of proinflammatory cytokines have been identified. These platelet-derived polypeptides do not only comprise members of the so-called ß-thromboglobulin family, such as platelet basic protein (PBP), connective tissue-activating peptide III (CTAP-III), and neutrophil-activating peptide 2 (NAP-2)1, but also platelet factor 4 (PF4)2,3 and the ß-chemokine RANTES (Regulated upon activation normal T cell expressed and probably secreted)4. While ß-chemokines have been shown to activate monocytes, T lymphocytes and eosinophils, α-chemokines such as IL-8, NAP-2 and melanoma growth-stimulating activity (MGSA/gro-α) appear to represent rather selective activators of polymorphonuclear leukocytes (PMN)5. Importantly, their biological activity, such as chemotaxis and degranulation-inducing capacity, has been demonstrated to be closely connected with the presence of an N-terminal glutamic acid-leucine-arginine (ELR) motif. Only recently, attention has been paid to the regulatory properties of α-chemokines. In the present article we will focus on two aspects of regulation of PMN functions, namely 1. the proteolytic processing of platelet-derived α-chemokines as a regulatory event in the induction and modulation of PMN activation, and 2. the phenotypic and functional consequences for the PMN under the constraints of such regulatory events.
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Flad, HD. et al. (1997). Regulation of Neutrophil Activation by Proteolytic Processing of Platelet-Derived α-Chemokines. In: Ansorge, S., Langner, J. (eds) Cellular Peptidases in Immune Functions and Diseases. Advances in Experimental Medicine and Biology, vol 421. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9613-1_29
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DOI: https://doi.org/10.1007/978-1-4757-9613-1_29
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