Osteoblast Adhesion Dynamics: A Possible Role for ROS and LMW-PTP

dc.contributorUniversidade Estadual Paulista (UNESP)
dc.creatorFernandes, Gustavo V. O.
dc.creatorCavagis, Alexandre D. M.
dc.creatorFerreira, Carmen V.
dc.creatorOlej, Beni
dc.creatorLeao, Mauricio de Souza
dc.creatorYano, Claudia L.
dc.creatorPeppelenbosch, Maikel
dc.creatorGranjeiro, Jose Mauro
dc.creatorZambuzzi, Willian F.
dc.date2014-12-03T13:08:58Z
dc.date2016-10-25T20:09:43Z
dc.date2014-12-03T13:08:58Z
dc.date2016-10-25T20:09:43Z
dc.date2014-06-01
dc.date.accessioned2017-04-06T06:16:19Z
dc.date.available2017-04-06T06:16:19Z
dc.identifierJournal Of Cellular Biochemistry. Hoboken: Wiley-blackwell, v. 115, n. 6, p. 1063-1069, 2014.
dc.identifier0730-2312
dc.identifierhttp://hdl.handle.net/11449/111779
dc.identifierhttp://acervodigital.unesp.br/handle/11449/111779
dc.identifier10.1002/jcb.24691
dc.identifierWOS:000334523300006
dc.identifierhttp://dx.doi.org/10.1002/jcb.24691
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/922552
dc.descriptionReactive 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 (30min and 2h 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 30min 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 (Y-397). Moreover, after 2h there was a decrease in ROS content and FAK phosphorylation. There was no significant change in LMW-PTP expression at 30min or 2h. 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. J. Cell. Biochem. 115: 1063-1069, 2014. (c) 2013 Wiley Periodicals, Inc.
dc.descriptionConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.descriptionFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.languageeng
dc.publisherWiley-Blackwell
dc.relationJournal of Cellular Biochemistry
dc.rightsinfo:eu-repo/semantics/closedAccess
dc.subjectADHESION
dc.subjectFAK
dc.subjectLMW-PTP
dc.subjectOSTEOBLAST
dc.subjectREDOX
dc.subjectROS
dc.titleOsteoblast Adhesion Dynamics: A Possible Role for ROS and LMW-PTP
dc.typeOtro


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