Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/88170
Type: Artigo de periódico
Title: Osteoblast Adhesion Dynamics: A Possible Role For Ros And Lmw-ptp
Author: Fernandes G.V.O.
Cavagis A.D.M.
Ferreira C.V.
Olej B.
De Souza Leao M.
Yano C.L.
Peppelenbosch M.
Granjeiro J.M.
Zambuzzi W.F.
Abstract: Reactive oxygen species (ROS) modulate a variety of intracellular events, but their role in osteoblast adhesion and spreading remains unclear. ROS is a very-known physiological modulators of Protein Tyrosine Phosphatases activities, mainly to low molecular weight protein tyrosine phosphatase (LMW-PTP) activity. As this biological mechanism is not clear in osteoblast adhesion, we decided to investigate ROS levels and phosphorylations of FAK and Src, identifying these proteins as potential substrates to LMW-PTP activity. Our results showed that during osteoblast adhesion/spreading (30 min and 2 h of seeding) the intracellular ROS content (hydrogen peroxide) is finely regulated by an effective anti-oxidant system [catalase and Superoxide Dismutase (SOD) activities were evaluated]. During the first 30 min of adhesion, there was an increase in ROS production and a concomitant increase in focal adhesion kinase (FAK) activity after its phosphorylation at Tyrosine 397 (Y397). Moreover, after 2 h there was a decrease in ROS content and FAK phosphorylation. There was no significant change in LMW-PTP expression at 30 min or 2 h. In order to validate our hypothesis that LMW-PTP is able to control FAK activity by modulating its phosphorylation status, we decided to overexpress and silence LMW-PTP in this context. Our results showed that FAK phosphorylation at Y 397 was increased and decreased in osteoblasts with silenced or overexpressed LMW-PTP, respectively. Together, these data show that ROS modulate FAK phosphorylation by an indirect way, suggesting that a LMW-PTP/FAK supra-molecular complex is involved in transient responses during osteoblast adhesion and spreading. © 2013 Wiley Periodicals, Inc.
Editor: Wiley-Liss Inc.
Rights: fechado
Identifier DOI: 10.1002/jcb.24691
Address: http://www.scopus.com/inward/record.url?eid=2-s2.0-84907421826&partnerID=40&md5=a74ee490794ba6436e5c6116b3c7dc72
Date Issue: 2014
Appears in Collections:Unicamp - Artigos e Outros Documentos

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