Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/32276
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dc.contributor.authorPagano, Rosana L.
dc.contributor.authorSampaio, Sandra C.
dc.contributor.authorJuliano, Maria A. [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorGiorgi, Renata
dc.date.accessioned2016-01-24T13:59:20Z-
dc.date.available2016-01-24T13:59:20Z-
dc.date.issued2010-02-25
dc.identifierhttp://dx.doi.org/10.1016/j.ejphar.2009.11.033
dc.identifier.citationEuropean Journal of Pharmacology. Amsterdam: Elsevier B.V., v. 628, n. 1-3, p. 240-246, 2010.
dc.identifier.issn0014-2999
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/32276-
dc.description.abstractProteinase-activated receptors (PAR) are widely recognized for their modulatory properties in inflammatory and immune responses; however, their direct role on phagocyte effector functions remains unknown. S100A9, a protein secreted during inflammatory responses, deactivates activated peritoneal macrophages, and its C-terminal portion inhibits spreading and phagocytosis of adherent peritoneal cells. Herein, the effect of PAR1 and PAR2 agonists was investigated on spreading and phagocytosis by adherent peritoneal cells, as well as the ability of murine C-terminal of S100A9 peptide (mS100A9p) to modulate this effect. Adherent peritoneal cells obtained from mouse abdominal cavity were incubated with PAR1 and PAR2 agonists and spreading and phagocytosis of Candida albicans particles were evaluated. PAR1 agonists increased both the spreading and the phagocytic activity, but PAR2 agonists only increased the spreading index. mS100A9p reverted both the increased spreading and phagocytosis induced by PAR1 agonists, but no interference in the increased spreading induced by PAR2 agonists was noticed. the shorter homologue peptide to the C-terminal of mS100A9p, corresponding to the H(92)-E(97) region, also reverted the increased spreading and phagocytosis induced by PAR1 agonists. These findings show that proteinase-activated receptors have an important role for spreading and phagocytosis of adherent peritoneal cells, and that the pepticle corresponding to the C-terminal of S100A9 protein is a remarkable candidate for use as a novel compound to modulate PAR1 function. (C) 2009 Elsevier B.V. All rights reserved.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipFundacao Butantan
dc.format.extent240-246
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofEuropean Journal of Pharmacology
dc.rightsAcesso restrito
dc.subjectProteinase-activated receptoren
dc.subjectAdherent peritoneal cellen
dc.subjectPhagocytosisen
dc.subjectSpreadingen
dc.subjectS100A9en
dc.subject(Mouse)en
dc.titleInvolvement of proteinase-activated receptors 1 and 2 in spreading and phagocytosis by murine adherent peritoneal cells: Modulation by the C-terminal of S100A9 proteinen
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionButantan Inst
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationButantan Inst, Lab Pathophysiol, BR-05503900 São Paulo, Brazil
dc.description.affiliationUniv São Paulo, Inst Biomed Sci, Dept Physiol & Biophys, BR-05508900 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Inst Pharmacol, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Inst Pharmacol, Dept Biophys, BR-04044020 São Paulo, Brazil
dc.identifier.doi10.1016/j.ejphar.2009.11.033
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000274784500034
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