Osteoblast adhesion dynamics: a possible role for ROS and LMW-PTP.

Reactive oxygen species modulate a variety of intracellular events, but their role in osteoblast adhesion and spreading remains unclear. 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 duanyu1670 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 duanyu1670 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 duanyu1670 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 duanyu1670 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 Y397 was increased and decreased in osteoblasts with silenced or overexpressed LMW-PTP, respectively. Together, these data show that duanyu1670 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.

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