Phosphoproteome reveals an atlas of protein signaling networks during osteoblast adhesion

Renato Milani, Carmen V. Ferreira, José M. Granjeiro, Edgar J. Paredes-Gamero, Rodrigo A. Silva, Giselle Z. Justo, Helena B. Nader, Eduardo Galembeck, Maikel P. Peppelenbosch, Hiroshi Aoyama, Willian F. Zambuzzi

Research output: Contribution to journalArticleAcademicpeer-review

37 Citations (Scopus)

Abstract

Cell adhesion on surfaces is a fundamental process in the emerging biomaterials field and developmental events as well. However, the mechanisms regulating this biological process in osteoblasts are not fully understood. Reversible phosphorylation catalyzed by kinases is probably the most important regulatory mechanism in eukaryotes. Therefore, the goal of this study is to assess osteoblast adhesion through a molecular prism under a peptide array technology, revealing essential signaling proteins governing adhesion-related events. First, we showed that there are main morphological changes on osteoblast shape during adhesion up to 3 h. Second, besides classical proteins activated upon integrin activation, our results showed a novel network involving signaling proteins such as Rap1A, PKA, PKC, and GSK3β during osteoblast adhesion on polystyrene. Third, these proteins were grouped in different signaling cascades including focal adhesion establishment, cytoskeleton rearrangement, and cell-cycle arrest. We have thus provided evidence that a global phosphorylation screening is able to yield a systems-oriented look at osteoblast adhesion, providing new insights for understanding of bone formation and improvement of cell-substratum interactions. Altogether, these statements are necessary means for further intervention and development of new approaches for the progress of tissue engineering.

Original languageEnglish
Pages (from-to)957-966
Number of pages10
JournalJournal of Cellular Biochemistry
Volume109
Issue number5
DOIs
Publication statusPublished - 1 Apr 2010
Externally publishedYes

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