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Type: Artigo
Title: Pharmacological and immunohistochemical evidence for a functional nitric oxide synthase system in rat peritoneal eosinophils
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Author: Martins, A.R.
De Nucci, G.
Antunes, E.
Murad, F.
Ferreira, H.H.A.
Zanardo, R.C.O.
Costa, E.
Abstract: Eosinophil migration in vivo is markedly attenuated in rats treated chronically with the NO synthase (NOS) inhibitor NW-nitro-L-arginine methyl ester (L-NAME). In this study, we investigated the existence of a NOS system in eosinophils. Our results demonstrated that rat peritoneal eosinophils strongly express both type LI (30.2 +/- 11.6% of counted cells) and type IU (24.7 +/- 7.4% of counted cells) NOS, as detected by immunohistochemistry using affinity purified mouse mAbs. Eosinophil migration in vitro was evaluated by using 48-well microchemotaxis chambers and the chemotactic agents used were N-formyl-methionyl-leucyl-phenylalanine (fMLP, 5 x 10(-8) M) and leukotriene B-4 (LTB4, 10(-8) M). L-NAME (but not D-NAME) significantly inhibited the eosinophil migration induced by both fMLP (54% reduction for 1.0 mM; P < 0.05) and LTB4 (61% reduction for 1.0 mM; P < 0.05). In addition, the type II NOS inhibitor 2-amino-5,6-dihydro-6-methyl-4H-1,3-thiazine and the type I/II NOS inhibitor 1-(2-trifluoromethylphenyl) imidazole also markedly (P < 0.05) attenuated fMLP- (52% and 38% reduction for 1.0 mM, respectively) and LTB4- (52% and 51% reduction for 1.0 mM, respectively) induced migration. The inhibition of eosinophil migration by L-NAME was mimicked by the soluble guanylate cyclase inhibitor 1H-[1,2,4] oxadiazolo [4,3,-a] quinoxalin-1-one (0.01 and 0.1 mM) and reversed by either sodium nitroprusside (0.1 mM) or dibutyryl cyclic GMP (1 mM). We conclude that eosinophils do express NO synthase(s) and that nitric oxide plays an essential role in eosinophil locomotion by acting through a cyclic GMP transduction mechanism
Subject: GMP cíclico
Inibidores enzimaticos
Country: Estados Unidos
Editor: National Academy of Sciences
Citation: Proceedings Of The National Academy Of Sciences Of The United States Of America. Natl Acad Sciences, v. 94, n. 25, n. 14111, n. 14114, 1997.
Rights: fechado
Identifier DOI: 10.1073/pnas.94.25.14111
Date Issue: 1997
Appears in Collections:FCM - Artigos e Outros Documentos

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