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dc.contributor.authorOliani, S. M.-
dc.contributor.authorPaul-Clark, M. J.-
dc.contributor.authorChristian, H. C.-
dc.contributor.authorFlower, R. J.-
dc.contributor.authorPerretti, M.-
dc.date.accessioned2014-05-20T15:22:16Z-
dc.date.accessioned2016-10-25T17:55:54Z-
dc.date.available2014-05-20T15:22:16Z-
dc.date.available2016-10-25T17:55:54Z-
dc.date.issued2001-02-01-
dc.identifierhttp://dx.doi.org/10.1016/S0002-9440(10)64002-3-
dc.identifier.citationAmerican Journal of Pathology. Bethesda: Amer Soc Investigative Pathology, Inc., v. 158, n. 2, p. 603-615, 2001.-
dc.identifier.issn0002-9440-
dc.identifier.urihttp://hdl.handle.net/11449/33278-
dc.identifier.urihttp://acervodigital.unesp.br/handle/11449/33278-
dc.description.abstractAnnexin 1 (ANX-A1) exerts antimigratory actions in several models of acute and chronic inflammation, This is related to its ability to mimic the effect of endogenous ANX-A1 that is externalized on neutrophil adhesion to the postcapillary endothelium. In the present study we monitored ANX-A1 expression and localization in intravascular and emigrated neutrophils, using a classical model of rat peritonitis, For this purpose, a pair of antibodies raised against the ANX-A1 N-terminus tie, able to recognize intact ANX-A1) or the whole protein tie, able to interact with all ANX-A1 isoforms) was used by immunofluorescence and immunocytochemistry analyses. The majority (similar to 50%) of ANX-A1 on the plasma membrane of intravascular neutrophils was intact. Extravasation into the subendothelial matrix caused loss of this pool of intact protein (to similar to6%), concomitant with an increase in total amount of the protein; only similar to 25% of the total protein was now recognized by the antibody raised against the N-terminus tie, it was intact). In the cytoplasm of these cells, ANX-A1 was predominantly associated with large vacuoles, possibly endosomes, In situ hybridization confirmed de novo synthesis of ANX-A1 in the extravasated cells. In conclusion, biochemical pathways leading to the externalization, proteolysis, and synthesis of ANX-A1 are activated during the process of neutrophil extravasation.en
dc.format.extent603-615-
dc.language.isoeng-
dc.publisherAmer Soc Investigative Pathology, Inc-
dc.sourceWeb of Science-
dc.titleNeutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expressionen
dc.typeoutro-
dc.contributor.institutionSt Bartholomews & Royal London Sch Med & Dent-
dc.contributor.institutionUniversidade Estadual Paulista (UNESP)-
dc.contributor.institutionUniv Oxford-
dc.description.affiliationSt Bartholomews & Royal London Sch Med & Dent, Div Pharmacol, William Harvey Res Inst, London EC1M 6BQ, England-
dc.description.affiliationUniv Estadual Paulista, Inst Biociencias Letras & Ciências Exatas, São Paulo, Brazil-
dc.description.affiliationUniv Estadual Paulista, Dept Biol, São Paulo, Brazil-
dc.description.affiliationUniv Oxford, Dept Human Anat & Genet, Oxford, England-
dc.description.affiliationUnespUniv Estadual Paulista, Inst Biociencias Letras & Ciências Exatas, São Paulo, Brazil-
dc.description.affiliationUnespUniv Estadual Paulista, Dept Biol, São Paulo, Brazil-
dc.identifier.doi10.1016/S0002-9440(10)64002-3-
dc.identifier.wosWOS:000166925900029-
dc.rights.accessRightsAcesso restrito-
dc.relation.ispartofAmerican Journal of Pathology-
Appears in Collections:Artigos, TCCs, Teses e Dissertações da Unesp

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