Participation of transmembrane proline 82 in angiotensin II AT(1) receptor signal transduction

Página do item simplificado
dc.contributor.authorReis, Rosana I.
dc.contributor.authorSantos, Edson L.
dc.contributor.authorPesquero, Joao B.
dc.contributor.authorOliveira, Laerte
dc.contributor.authorSchanstra, Joost P.
dc.contributor.authorBascands, Jean-Loup
dc.contributor.authorPecher, Christiane
dc.contributor.authorPaiva, Antonio C. M.
dc.contributor.authorCosta-Neto, Claudio M.
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionINSERM
dc.contributor.institutionUniv Toulouse 3
dc.date.accessioned2016-01-24T13:48:35Z
dc.date.available2016-01-24T13:48:35Z
dc.date.issued2007-04-05
dc.description.abstractMost of the classical physiological effects of the octapeptide angiotensin II (AngII) are produced by activating the AT, receptor which belongs to the G-protein coupled receptor family (GPCR). Peptidic GPCRs may be functionally divided in three regions: (i) extracellular domains involved in ligand binding; (ii) intracellular domains implicated in agonist-induced coupling to G protein and (iii) seven transmembrane domains (TM) involved in signal transduction. the TM regions of such receptors have peculiar characteristics such as the presence of proline residues. in this project we aimed to investigate the participation of two highly conserved proline residues (Pro82 and Pro162), located in TM II and TM IV, respectively, in AT1 receptor signal transduction. Both mutations did not cause major alterations in AngII affinity. Functional assays indicated that the P162A mutant did not influence the signal transduction. On the other hand, a potent deleterious effect of P82A mutation on signal transduction was observed. We believe that the Pro82 residue is crucial to signal transduction, although it is not possible to say yet if this is due to a direct participation or if due to a structural rearrangement of TM II. in this last hypothesis, the removal of proline residue might be correlated to a removal of a kink, which in turn can be involved in the correct positioning of residues involved in signal transduction. (c) 2006 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniv São Paulo, Fac Med Ribeirao Preto, Dept Biochem & Immunol, BR-14049900 Ribeirao Preto, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04023062 São Paulo, Brazil
dc.description.affiliationINSERM, U388, F-31432 Toulouse, France
dc.description.affiliationUniv Toulouse 3, Inst Louis Bugnard, IFR31, F-31432 Toulouse, France
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04023062 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent32-36
dc.identifierhttp://dx.doi.org/10.1016/j.regpep.2006.11.028
dc.identifier.citationRegulatory Peptides. Amsterdam: Elsevier B.V., v. 140, n. 1-2, p. 32-36, 2007.
dc.identifier.doi10.1016/j.regpep.2006.11.028
dc.identifier.issn0167-0115
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/29660
dc.identifier.wosWOS:000245151700006
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofRegulatory Peptides
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectsite-directed mutagenesisen
dc.subjectsignal transductionen
dc.subjectG-protein coupled receptorsen
dc.subjectagonisten
dc.titleParticipation of transmembrane proline 82 in angiotensin II AT(1) receptor signal transductionen
dc.typeinfo:eu-repo/semantics/article
Arquivos
Coleções
Em verificação - Geral