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Type: Artigo de periódico
Title: Phosphoproteome Reveals An Atlas Of Protein Signaling Networks During Osteoblast Adhesion.
Author: Milani, Renato
Ferreira, Carmen V
Granjeiro, José M
Paredes-Gamero, Edgar J
Silva, Rodrigo A
Justo, Giselle Z
Nader, Helena B
Galembeck, Eduardo
Peppelenbosch, Maikel P
Aoyama, Hiroshi
Zambuzzi, Willian F
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 GSK3beta 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.
Subject: Actin Depolymerizing Factors
Amino Acid Motifs
Cell Adhesion
Cell Line
Cell Proliferation
Cell Shape
Focal Adhesions
Protein Array Analysis
Reproducibility Of Results
Signal Transduction
Time Factors
Citation: Journal Of Cellular Biochemistry. v. 109, n. 5, p. 957-66, 2010-Apr.
Rights: fechado
Identifier DOI: 10.1002/jcb.22479
Date Issue: 2010
Appears in Collections:Unicamp - Artigos e Outros Documentos

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