Structural analysis of three peptides related to the transmambranic helix VI of AT1 receptor

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dc.contributor.authorRibeiro de Noronha, Samuel Marcos [UNIFESP]
dc.contributor.authorCorrêa, Silvana Aparecida Alves [UNIFESP]
dc.contributor.authorPoletti, Erick Fernando
dc.contributor.authorLopes, Douglas Duarte
dc.contributor.authorSilva, Caroline Correa da
dc.contributor.authorSforca, Mauricio Luis
dc.contributor.authorShimuta, Suma Imura
dc.contributor.authorTonin Zanchin, Nilson Ivo
dc.contributor.authorNakaie, Clovis Ryuichi
dc.contributor.authorCotrim Guerreiro da Silva, Ismael Dale
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionDept Biofis
dc.contributor.institutionLab Nacl Luz Sincroton
dc.date.accessioned2016-01-24T13:59:31Z
dc.date.available2016-01-24T13:59:31Z
dc.date.issued2010-04-01
dc.description.abstractIntroduction: Angiotensin II (AII) is the main active product of the renin angiotensin system. Better known effects of All are via AT1 receptor (AT1R). Expression of AT1R mutants (L265D and L262D) in CHO cells increased cAMP formation when compared to CHO cells expressing the wild type (WT) AT1R. Morphological transformation of CHO cells transfected with mutants correlated with their increased cAMP formation. DNA synthesis was inhibited in these cells too, indicating that cAMP promotes inhibitory effects on transfected CHO cells growth and causes their morphological change from a tumorigenic phenotype to a non-tumorigenic one.Objectives: To assess the importance of leucine 262 and 265 in determining AT1R structure by means of a comparative structural analysis of two mutant peptides and of a wild-type fragment.Methodology: Three peptides had their conformation compared by circular dichroism (CD): L262D(259-272). L265D(259-272) (mutants) and WT(260-277).Results: Secondary structures were: beta-turn for WT and L262D and random coil for L265D.Conclusions: Strong correlation was found in the results of biochemical, cellular and structural approaches used to compare WT AT1R to mutant types. Random coil structure of the L265D mutant may be a key point to explain those changes observed in biochemical (binding and signal transduction) and proliferation assays (Correa et al., 2005). beta-Turn formation is an important step during early protein folding and this secondary simple structure is present in L262D and WT, but not in L265D. Therefore, leucine 265 seems to play a crucial role in determining an entirely functional AT1R. (C) 2009 Elsevier B.V. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Mol Gynecol Lab, Dept Gynecol, BR-04039032 São Paulo, Brazil
dc.description.affiliationDept Biofis, São Paulo, Brazil
dc.description.affiliationLab Nacl Luz Sincroton, Campinas, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Mol Gynecol Lab, Dept Gynecol, BR-04039032 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent115-118
dc.identifierhttp://dx.doi.org/10.1016/j.npep.2009.11.006
dc.identifier.citationNeuropeptides. Edinburgh: Churchill Livingstone, v. 44, n. 2, p. 115-118, 2010.
dc.identifier.doi10.1016/j.npep.2009.11.006
dc.identifier.issn0143-4179
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/32425
dc.identifier.wosWOS:000276001700008
dc.language.isoeng
dc.publisherChurchill Livingstone
dc.relation.ispartofNeuropeptides
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectAngiotensin II type 1 receptoren
dc.subjectAngiotensin IIen
dc.subjectRenin angiotensin systemen
dc.subjectCircular dichroism spectroscopyen
dc.subjectMutationen
dc.titleStructural analysis of three peptides related to the transmambranic helix VI of AT1 receptoren
dc.typeinfo:eu-repo/semantics/article
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