| First Author | Hao Q | Year | 2006 |
| Journal | Free Radic Biol Med | Volume | 41 |
| Issue | 2 | Pages | 302-10 |
| PubMed ID | 16814111 | Mgi Jnum | J:110419 |
| Mgi Id | MGI:3640213 | Doi | 10.1016/j.freeradbiomed.2006.04.011 |
| Citation | Hao Q, et al. (2006) Selective regulation of hydrogen peroxide signaling by receptor tyrosine phosphatase-alpha. Free Radic Biol Med 41(2):302-10 |
| abstractText | Reactive oxygen species (ROS) are constantly produced in the human body and are involved in the pathogenesis of aging, cardiovascular diseases, and cancer. Emerging evidence indicates that oxidation and inhibition of protein tyrosine phosphatases (PTPs) are critical for ROS signal transduction. However, the role of individual PTPs in ROS signaling remains unclear. Here, we demonstrated that the receptor-like PTPalpha (RPTPalpha) was an effector of H(2)O(2), the most stable form of ROS. H(2)O(2) at nontoxic concentration rapidly induced the association of RPTPalpha with Src family kinases, platelet-derived growth factor receptor-beta, and protein kinase D in various cultured cells, although it markedly suppressed RPTPalpha phosphorylation on Tyr-789. We further identified that RPTPalpha selectively regulated the signal transduction pathways induced by H(2)O(2). Particularly, RPTPalpha was required for the activation of protein kinase D and for the modulation of p130Cas tyrosine phosphorylation in response to H(2)O(2.) In contrast, the H(2)O(2)-induced inactivation of Src family kinases and suppression of paxillin phosphorylation on Tyr-118 were both largely independent of RPTPalpha. Our findings indicate that H(2)O(2) signaling pathways are selectively regulated by RPTPalpha in cells, which may provide new insights into the functional regulation of ROS signal transduction by PTPs. |
