Human neutrophil migration in vitro induced by secretory phospholipases A(2): a role for cell surface glycosaminoglycans

Human neutrophil migration in vitro induced by secretory phospholipases A(2): a role for cell surface glycosaminoglycans

Autor Gambero, A. Google Scholar
Landucci, ECT Google Scholar
Toyama, M. H. Google Scholar
Marangoni, S. Google Scholar
Giglio, JR Google Scholar
Nader, H. B. Google Scholar
Dietrich, C. P. Google Scholar
De Nucci, G. Google Scholar
Antunes, E. Google Scholar
Instituição Universidade Estadual de Campinas (UNICAMP)
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
Resumo The purpose of this study was to examine the ability of type I- (porcine pancreas and Naja mocambique mocambique venom), type II- (bothropstoxin-I, bothropstoxin-II, and piratoxin-I). and type III- (Apis mellifera venom) secretory phospholipases A(2) (sPLA(2)s) to induce human neutrophil chemotaxis, and the role of the cell surface proteoglycans, leukotriene B-4 (LTB4), and platelet-activating factor (PAF). in mediating this migration. the neutrophil chemotaxis assays were performed by using a 48-well microchemotaxis chamber. Piratoxin-I, bothropstoxin-I. N. m. mocambique venom PLA(2) (10-1000 mug/mL each), bothropstoxin-II (30-1000 mug/mL), porcine pancreas PLA(2) (0.3-30 mug/mL), and A. mellifera venom PLA(2) (30-300 mug/mL) caused concentration-dependent neutrophil chemotaxis. Heparin (10-300 U/mL) concentration-dependently inhibited the neutrophil migration induced by piratoxin-I, bothropstoxin-II, and N. in. mocambique and A. mellifera venom PLA(2)s (100 mug/mL each), but failed to affect the migration induced by porcine pancreas PLA(2). Heparan sulfate (300 and 1000 mug/mL) inhibited neutrophil migration induced by piratoxin-I, whereas dermatan sulfate and chondroitin sulfate (30-1000 mug/mL each) had no effect. Heparitinase I and heparinase (300 mU/mL each) inhibited by 41.5 and 47%. respectively, piratoxin-l-induced chemotaxis, whereas heparitinase 11 and chondroitinase AC failed to affect the chemotaxis. the PAF receptor antagonist WEB 2086 (3-[4-(2-chlorophenyl)-9-methyl-6H-thienol-[3,2-f] [1,2,4]-triazolo-[4.3-a] [1,4]-diazepine-2-yl]-1-(4-morpholynil)-1-propionate) (0.1-10 muM) and the LTB4 synthesis inhibitor AA-861 [2-(12-hydroxydodeca-5,10-diynyl)-3,5,6-trimethyl-1,4-benzoquinone] (0.1-10 muM) significantly inhibited the piratoxin-I-induced chemotaxis. Piratoxin-I (30-300 mug/mL) caused a concentration-dependent release of LTB4 Our results suggest that neutrophil migration in response to sPLA(2)s is independent of PLA activity, and involves an interaction of sPLA(2)s with cell surface heparin/heparan binding sites triggering the release of LTB4 and PAF. (C) 2002 Elsevier Science Inc. All rights reserved.
Assunto phospholipase A(2)
neutrophil chemotaxis
Flavobacterium heparinum lyases
leukotriene B-4
platelet-activating factor
Idioma Inglês
Data 2002-01-01
Publicado em Biochemical Pharmacology. Oxford: Pergamon-Elsevier B.V., v. 63, n. 1, p. 65-72, 2002.
ISSN 0006-2952 (Sherpa/Romeo, fator de impacto)
Editor Elsevier B.V.
Extensão 65-72
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000173153700008

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