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DC Field | Value | Language |
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dc.contributor.author | Oliani, S. M. | - |
dc.contributor.author | Paul-Clark, M. J. | - |
dc.contributor.author | Christian, H. C. | - |
dc.contributor.author | Flower, R. J. | - |
dc.contributor.author | Perretti, M. | - |
dc.date.accessioned | 2014-05-20T15:22:16Z | - |
dc.date.accessioned | 2016-10-25T17:55:54Z | - |
dc.date.available | 2014-05-20T15:22:16Z | - |
dc.date.available | 2016-10-25T17:55:54Z | - |
dc.date.issued | 2001-02-01 | - |
dc.identifier | http://dx.doi.org/10.1016/S0002-9440(10)64002-3 | - |
dc.identifier.citation | American Journal of Pathology. Bethesda: Amer Soc Investigative Pathology, Inc., v. 158, n. 2, p. 603-615, 2001. | - |
dc.identifier.issn | 0002-9440 | - |
dc.identifier.uri | http://hdl.handle.net/11449/33278 | - |
dc.identifier.uri | http://acervodigital.unesp.br/handle/11449/33278 | - |
dc.description.abstract | Annexin 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.extent | 603-615 | - |
dc.language.iso | eng | - |
dc.publisher | Amer Soc Investigative Pathology, Inc | - |
dc.source | Web of Science | - |
dc.title | Neutrophil interaction with inflamed postcapillary venule endothelium alters annexin 1 expression | en |
dc.type | outro | - |
dc.contributor.institution | St Bartholomews & Royal London Sch Med & Dent | - |
dc.contributor.institution | Universidade Estadual Paulista (UNESP) | - |
dc.contributor.institution | Univ Oxford | - |
dc.description.affiliation | St Bartholomews & Royal London Sch Med & Dent, Div Pharmacol, William Harvey Res Inst, London EC1M 6BQ, England | - |
dc.description.affiliation | Univ Estadual Paulista, Inst Biociencias Letras & Ciências Exatas, São Paulo, Brazil | - |
dc.description.affiliation | Univ Estadual Paulista, Dept Biol, São Paulo, Brazil | - |
dc.description.affiliation | Univ Oxford, Dept Human Anat & Genet, Oxford, England | - |
dc.description.affiliationUnesp | Univ Estadual Paulista, Inst Biociencias Letras & Ciências Exatas, São Paulo, Brazil | - |
dc.description.affiliationUnesp | Univ Estadual Paulista, Dept Biol, São Paulo, Brazil | - |
dc.identifier.doi | 10.1016/S0002-9440(10)64002-3 | - |
dc.identifier.wos | WOS:000166925900029 | - |
dc.rights.accessRights | Acesso restrito | - |
dc.relation.ispartof | American Journal of Pathology | - |
Appears in Collections: | Artigos, TCCs, Teses e Dissertações da Unesp |
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