Artículos de revistas
Osteoblast Adhesion Dynamics: A Possible Role For Ros And Lmw-ptp
Registro en:
Journal Of Cellular Biochemistry. Wiley-liss Inc., v. 115, n. 6, p. 1063 - 1069, 2014.
7302312
10.1002/jcb.24691
2-s2.0-84907421826
Autor
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.
Institución
Resumen
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. 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