On the Road to Understanding of the Osteoblast Adhesion: Cytoskeleton Organization Is Rearranged by Distinct Signaling Pathways

Willian Fernando Zambuzzi*, Alexandre Bruni-Cardoso, Jose Mauro Granjeiro, Maikel Petrus Peppelenbosch, Hernandes Faustino de Carvalho, Hiroshi Aoyama, Carmen Verissima Ferreira

*Bijbehorende auteur voor dit werk

    Onderzoeksoutput: ArticleAcademicpeer review

    36 Citaten (Scopus)


    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. J. Cell. Biochem. 108: 134-144, 2009. (C) 2009 Wiley-Liss, Inc.

    Originele taal-2English
    Pagina's (van-tot)134-144
    Aantal pagina's11
    TijdschriftJournal of Cellular Biochemistry
    Nummer van het tijdschrift1
    StatusPublished - 1-sep.-2009

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