Abstract
Neutrophil-activating peptide 2 (NAP-2) was isolated from stimulated cultures of human blood mononuclear cells (1). NAP-2 consists of 70 amino acids and is structurally related to NAP-1/IL-8 (2), a peptide produced by a variety of cells upon induction with interleukin-1 or tumor necrosis factor alpha (3), and to melanoma growth-stimulatory activity (MGSA) which was shown to be mitogenic for cultured human melanoma cells (4, 5). NAP-1/IL-8 and MGSA are potent chemotactic agents for human neutrophils in vitro and in vivo (6, 7), and induce cytosolic free calcium changes, the respiratory burst and exocytosis (8). The amino acid sequence of NAP-2 corresponds to part of the sequence of platelet basic protein (PBP) (9) and its derivative, connective tissue activating peptide III (CTAP-III, ref 10) and to other inactive cleavage products which were recently identified (11). NAP-2 also shows structural homology to platelet factor 4 (PF-4), another peptide contained in the platelet alpha granules (12).
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© 1991 Plenum Press, New York
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Walz, A., Zwahlen, R., Baggiolini, M. (1991). Formation and Biological Properties of Neutrophil Activating Peptide 2 (NAP-2). In: Westwick, J., Lindley, I.J.D., Kunkel, S.L. (eds) Chemotactic Cytokines. Advances in Experimental Medicine and Biology, vol 305. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-6009-4_5
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DOI: https://doi.org/10.1007/978-1-4684-6009-4_5
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