Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/198382
Type: Artigo de periódico
Title: On The Road To Understanding Of The Osteoblast Adhesion: Cytoskeleton Organization Is Rearranged By Distinct Signaling Pathways.
Author: Zambuzzi, Willian Fernando
Bruni-Cardoso, Alexandre
Granjeiro, José Mauro
Peppelenbosch, Maikel Petrus
de Carvalho, Hernandes Faustino
Aoyama, Hiroshi
Ferreira, Carmen Veríssima
Abstract: Pre-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.
Subject: Animals
Cell Adhesion
Cell Cycle
Cell Line
Cytoskeleton
Intracellular Signaling Peptides And Proteins
Mice
Models, Biological
Osteoblasts
Protein-serine-threonine Kinases
Signal Transduction
Threonine
Tyrosine
Citation: Journal Of Cellular Biochemistry. v. 108, n. 1, p. 134-44, 2009-Sep.
Rights: fechado
Identifier DOI: 10.1002/jcb.22236
Address: http://www.ncbi.nlm.nih.gov/pubmed/19562668
Date Issue: 2009
Appears in Collections:Unicamp - Artigos e Outros Documentos

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