Please use this identifier to cite or link to this item: http://repositorio.unifesp.br/handle/11600/29660
Title: Participation of transmembrane proline 82 in angiotensin II AT(1) receptor signal transduction
Authors: Reis, Rosana I.
Santos, Edson L.
Pesquero, Joao B.
Oliveira, Laerte
Schanstra, Joost P.
Bascands, Jean-Loup
Pecher, Christiane
Paiva, Antonio C. M.
Costa-Neto, Claudio M.
Universidade de São Paulo (USP)
Universidade Federal de São Paulo (UNIFESP)
INSERM
Univ Toulouse 3
Keywords: site-directed mutagenesis
signal transduction
G-protein coupled receptors
agonist
Issue Date: 5-Apr-2007
Publisher: Elsevier B.V.
Citation: Regulatory Peptides. Amsterdam: Elsevier B.V., v. 140, n. 1-2, p. 32-36, 2007.
Abstract: Most 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.
URI: http://repositorio.unifesp.br/handle/11600/29660
ISSN: 0167-0115
Other Identifiers: http://dx.doi.org/10.1016/j.regpep.2006.11.028
Appears in Collections:Em verificação - Geral

Files in This Item:
There are no files associated with this item.


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.