Neutrophil-activating peptide

NAP Neutrophil-activating peptide NAPQI N-acetyl-p-benzoquinone imine... 

Katancik JA, Sharma A, de Nardin E. Interleukin 8, neutrophil-activating peptide-2 and GRO-alpha bind to and elicit cell activation via specific and different amino acid residues of CXCR2. Cytokine 2000 12(10) 1480-1488. 

Schroder JM, Mrowietz U, Morita E, Christophers E. Purification and partial biochemical characterization of a human monocyte-derived, neutrophil-activating peptide that lacks interleukin 1 activity. J Immunol 1987 139 3474-3483. 

Koch AE, Volin MV, Woods JM, et al. Regulation of angiogenesis by the C-X-C chemokines interleukin-8 and epithelial neutrophil activating peptide 78 in the rheumatoid joint. Arthritis Rheum 2001 44(1) 31 40. 

Moser B, Schumacher C, von Tschamer V, Clark-Lewis I, Baggiolini M. Neutrophil-activating peptide 2 and gro/melanoma growth-stimulatory activity interact with neutrophil-activating peptide 1/interleukin 8 receptors on human neutrophils. J Biol Chem 1991 266(16) 10666-10671. 

Arenberg DA, Keane MP, DiGiovine B, et al. Epithelial-neutrophil activating peptide (ENA-78) is an important angiogenic factor in non-small cell lung cancer. J Clin Invest 1998 I02(3) 465 172. 

Interleukin 8 (IL-8) Neutrophil-activating peptide 2 Platelet factor IV... 

Chemokines-connective tissue-activating peptide-III (CTAP-III) Epithelial neutrophil-activating peptide-78 (ENA-78)... 

Clark-Lewis, I., Moser, B., Walz, A., Baggiolini, M Scott, G. J., and Aebersold, R. (1991) Chemical synthesis, purification, and characterization of two inflammatory proteins, neutrophil activating peptide I (interleukin-8) and neutrophil activating peptide 2. Biochemistry 30, 3128. 

Schroder, J. M. (1997) Isolation and purification of neutrophil-activating peptide-4 a chemokine missing two cysteines. Methods Enzymol. 287, 216. 

Foster, S. J., Aked, D. M., Schroder, J. M., and Christophers, E. (1989) Acute inflammatory effects of a monocyte-derived neutrophil-activating peptide in rabbit skin. Immunology 67, 181-183. 

M. Baggiolini, P. Imboden, and P. A. Detmers, Neutrophil Activation and the Effects of Interleukin-8 / Neutrophil-Activating Peptide-1 (IL-8/NAP-1), Cytokines, 4 (1992) 1-17. 

Mielke, V., Bauman, J.G., Sticherling, M., lbs, T., Zomershoe, A.G., Seligmann, K., Henneicke, H.H., Schroder, J.M., Sterry, W. and Christophers, E. (1990). Detection of neutrophil-activating peptide NAP/IL-8 and NAP/IL-8 mRNA in human recombinant IH alpha- and human recombinant tumor necrosis factor-alpha-stimulated human dermal fibroblasts. An immunocytochemical and fluorescent in situ hybridization study. J. Immunol. 144, 153-161. 

Schroder, J.M. and Christophers, E. (1989). Secretion of novel and homologous neutrophil-activating peptides by LPS-stimulated human endothelial cells. J. Immunol. 142, 244-251. 

Baggjolini, M., Walz, A. and Kunkel, S.L. (1989). Neutrophil activating peptide-1/ interleukin 8, a novel cytokine that activates neutrophils. J. Clin. Invest. 84, 1045-1049. 

Walz, A., Dewald, B., von Tscharner, V., and Baggiolini, M. (1989). Effects of the neutrophil-activating peptide NAP-2, platelet basic protein, connective tissue-activating peptide III and platelet factor 4 on human neutrophils. J. Exp. Med. 170, 1745-1750. 

Early studies suggested that IL-1 and TNF were chemotactic for PMN. However, it has become apparent that this activity resides in a family of molecules of 10 kDa, called neutrophil activating peptides (NAP) or IL-8 (L15). IL-1 and TNF induce the release of these molecules from mononuclear cells, fibroblasts, endothelial cells, and keratinocytes and they act on a specific receptor expressed by PMN. The main activity ascribed to these molecules is PMN chemotaxis, but the molecules may cause oxygen radical and enzyme release by PMN and mobilize PMN into the circulation. The common feature that identifies members of this family of peptides is alignment of four cysteine residues. IL-8 is the most potent chemotactic member of this family. Synthesized as a 99-amino-acid precursor, lL-8 is released as a 79-amino-acid molecule, IL-8a, which itself is further cleaved to 77- and 72-amino-acid forms, IL-8P and IL-8y. IL-8y is predominantly found to be associated with macrophages and may reflect the proteolytic enzymes released by macrophages. Receptors for IL-8 have been identified on PMN and approximately 20% of lymphocytes. The three-dimensional structure of IL-8 (NAP-1) has been reported (C27). 

C30. Colditz, 1. G., Zwahlen, R. D., and Baggiolini, M. Neutrophil accumulation and plasma leakage induced in vivo by neutrophil-activating peptide-1. J. Leukocyte Biol. 48, 129-137 (1990). 

N-acetyl-B-D-glucosaminidase, alpha N-acetyl-B-D-glucosaminidase, beta N-acetyl-muramyl-L-alanine amidase Neuron-specific enolase Neutrophil-activating peptide 2 Osteocalcin Osteonectin... 

Brandt E, Van Damme J, Flad HD. Neutrophils can generate their activates neutrophil-activating peptide 2 by proteolytic cleavage of platelet-derived connective... 

Harter L, Petersen F, Flad HD, Brandt E. Connective tissue-activating peptide III desensitizes chemokine receptors on neutrophils. Requirement for proteolytic formation of the neutrophil-activating peptide 2. J Immunol 1994 153 5698-5708. 

Ahuja SK, Murphy PM. The CXC chemokines growth-related oncogene (GRO) alpha, GRO beta, GRO gamma, neutrophil-activating peptide-2, and epithelial cell-derived neutrophil activating peptide-78 are potent agonists for the type B, but not the type A, human interleukin-8 receptor. J Biol Chem 1996 271 20545-20550. 

Schroder, J. M. and Christopher, E. (1986) Identification of C5ades arg and an anionic neutrophil-activating peptide (ANAP) in psoriatic scales. J. Invest. DermatoL 87,53-58. 

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