Nitric oxide has a role in regulating VLA-4-integrin expression on the human neutrophil cell surface

dc.creatorConran, N
dc.creatorGambero, A
dc.creatorFerreira, HHA
dc.creatorAntunes, E
dc.creatorde Nucci, G
dc.date2003
dc.date37073
dc.date2014-11-15T01:02:55Z
dc.date2015-11-26T17:18:04Z
dc.date2014-11-15T01:02:55Z
dc.date2015-11-26T17:18:04Z
dc.date.accessioned2018-03-29T00:05:54Z
dc.date.available2018-03-29T00:05:54Z
dc.identifierBiochemical Pharmacology. Pergamon-elsevier Science Ltd, v. 66, n. 1, n. 43, n. 50, 2003.
dc.identifier0006-2952
dc.identifierWOS:000183820100005
dc.identifier10.1016/S0006-2952(03)00243-0
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/81993
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/81993
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/81993
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1282597
dc.descriptionRecent research demonstrates that the beta1 integrins may be involved in neutrophil migration. Here, we investigate the role of nitric oxide in the expression and function of the very late antigen-4 (VLA-4) and Mac-1 integrins on human neutrophils. Human blood neutrophils were treated with N-nitro-L-arginine methyl ester (L-NAME) and their adhesion to fibronectin (FN) and serum observed. Adhesion of neutrophils to FN and serum increased significantly following incubation with 0.1 mM L-NAME by 65.5 and 44.6%, respectively. Increased adhesions to FN and serum were abolished by a VLA-4-specific monoclonal antibody, HP2/1, and a Mac-1-specific monoclonal antibody, ICRF 44, respectively. The microfilament- and microtubule-depolymerizing agents, dihydrochalasin B and nocodazole, were also able to reverse L-NAME-induced adhesion to both IN and serum. L-NAME induced a discrete increase in the expression of CD49d (VLA-4, 25.3 +/- 4.8%), but not CD11b, on the neutrophil cell surface, as detected by flow cytometry. Results indicate that NO has a role in regulating VLA-4 and Mac-1 function on the human neutrophil cell surface and that this modulation in integrin function is accompanied by cytoskeletal rearrangements and changes in the ability of the neutrophil to adhere to the extracellular matrix. (C) 2003 Elsevier Science Inc. All fights reserved.
dc.description66
dc.description1
dc.description43
dc.description50
dc.languageen
dc.publisherPergamon-elsevier Science Ltd
dc.publisherOxford
dc.publisherInglaterra
dc.relationBiochemical Pharmacology
dc.relationBiochem. Pharmacol.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectadhesion molecules
dc.subjectcytoskeleton
dc.subjectMac-1
dc.subjectneutrophil
dc.subjectnitric oxide synthase inhibitors
dc.subjectVLA-4
dc.subjectLate Activation Antigen-4
dc.subjectIn-vitro
dc.subjectLeukocyte Adhesion
dc.subjectEndothelial-cells
dc.subjectCyclic-gmp
dc.subjectPolymorphonuclear Leukocytes
dc.subjectFibroblast Barriers
dc.subjectSrc Kinase
dc.subjectP-selectin
dc.subjectIntegrin
dc.titleNitric oxide has a role in regulating VLA-4-integrin expression on the human neutrophil cell surface
dc.typeArtículos de revistas


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