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dc.contributor.CRUESPUNIVERSIDADE DE ESTADUAL DE CAMPINASpt_BR
dc.typeArtigo de periódicopt_BR
dc.titleOn The Road To Understanding Of The Osteoblast Adhesion: Cytoskeleton Organization Is Rearranged By Distinct Signaling Pathways.pt_BR
dc.contributor.authorZambuzzi, Willian Fernandopt_BR
dc.contributor.authorBruni-Cardoso, Alexandrept_BR
dc.contributor.authorGranjeiro, José Mauropt_BR
dc.contributor.authorPeppelenbosch, Maikel Petruspt_BR
dc.contributor.authorde Carvalho, Hernandes Faustinopt_BR
dc.contributor.authorAoyama, Hiroshipt_BR
dc.contributor.authorFerreira, Carmen Veríssimapt_BR
unicamp.authorWillian Fernando Zambuzzi, Department of Biochemistry, Biology Institute, University of Campinas, Campinas, São Paulo, Brazil. wzamba@unicamp.brpt_BR
unicamp.author.externalAlexandre Bruni-Cardoso,pt
unicamp.author.externalJosé Mauro Granjeiro,pt
unicamp.author.externalMaikel Petrus Peppelenbosch,pt
unicamp.author.externalHernandes Faustino de Carvalho,pt
unicamp.author.externalHiroshi Aoyama,pt
unicamp.author.externalCarmen Veríssima Ferreira,pt
dc.subjectAnimalspt_BR
dc.subjectCell Adhesionpt_BR
dc.subjectCell Cyclept_BR
dc.subjectCell Linept_BR
dc.subjectCytoskeletonpt_BR
dc.subjectIntracellular Signaling Peptides And Proteinspt_BR
dc.subjectMicept_BR
dc.subjectModels, Biologicalpt_BR
dc.subjectOsteoblastspt_BR
dc.subjectProtein-serine-threonine Kinasespt_BR
dc.subjectSignal Transductionpt_BR
dc.subjectThreoninept_BR
dc.subjectTyrosinept_BR
dc.description.abstractPre-osteoblast adhesion attracts increasing interest in both medicine and dentistry. However, how this physiological event alters osteoblast phenotype is poorly understood. We therefore attempted to address this question by investigating key biochemical mechanism that governs pre-osteoblast adhesion on polystyrene surface. Importantly, we found that cofilin activity was strongly modulated by PP2A (Ser/Thr phosphatase), while cell-cycle was arrested. Accordingly, we observed that the profile of cofilin phosphorylation (at Ser03) was similar to phospho-PP2A (at Tyr307). Also, it is plausible to suggest during pre-osteoblast adhesion that PP2A phosphorylation at Y307 was executed by phospho-Src (Y416). In addition, it was observed that MAPKp38, but not MAPK-erk, played a key role on pre-osteoblast adhesion by phosphorylating MAPKAPK-2 and ATF-2 (also called CRE-BP1). Also, the up-modulation of RhoA reported here suggests its involvement at the beginning of osteoblast attachment, while Akt remained active during all periods. Altogether, our results clearly showed that osteoblast adhesion is under an intricate network of signaling molecules, which are responsible to guide their interaction with substrate mainly via cytoskeleton rearrangement.en
dc.relation.ispartofJournal Of Cellular Biochemistrypt_BR
dc.relation.ispartofabbreviationJ. Cell. Biochem.pt_BR
dc.date.issued2009-Seppt_BR
dc.identifier.citationJournal Of Cellular Biochemistry. v. 108, n. 1, p. 134-44, 2009-Sep.pt_BR
dc.language.isoengpt_BR
dc.description.volume108pt_BR
dc.description.firstpage134-44pt_BR
dc.rightsfechadopt_BR
dc.rights.holder(c) 2009 Wiley-Liss, Inc.pt_BR
dc.sourcePubMedpt_BR
dc.identifier.issn1097-4644pt_BR
dc.identifier.doi10.1002/jcb.22236pt_BR
dc.identifier.urlhttp://www.ncbi.nlm.nih.gov/pubmed/19562668pt_BR
dc.date.available2015-11-27T13:15:21Z-
dc.date.accessioned2015-11-27T13:15:21Z-
dc.description.provenanceMade available in DSpace on 2015-11-27T13:15:21Z (GMT). No. of bitstreams: 1 pmed_19562668.pdf: 485654 bytes, checksum: 5c7a0e7550bcf10118bba8ae5d1138e3 (MD5) Previous issue date: 2009en
dc.identifier.urihttp://repositorio.unicamp.br/jspui/handle/REPOSIP/198382-
dc.identifier.idPubmed19562668pt_BR
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