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Tang, K.M. et al.

Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure.

Nitric oxide (NO) inhibits vascular contraction by activating cGMP-dependent protein kinase I-alpha (PKGI-alpha), which causes dephosphorylation of myosin light chain (MLC) and vascular smooth muscle relaxation. Here we show that PKGI-alpha attenuates signaling by the thrombin receptor protease- activated receptor-1 ( PAR-1) through direct activation of regulator of G-protein signaling-2 ( RGS-2). NO donors and cGMP cause cGMP-mediated inhibition of PAR-1 and membrane localization of RGS-2. PKGI-alpha binds directly to and phosphorylates RGS-2, which significantly increases GTPase activity of G(q), terminating PAR-1 signaling. Disruption of the RGS-2-PKGI-alpha interaction reverses inhibition of PAR-1 signaling by nitrovasodilators and cGMP. Rgs2-/- mice develop marked hypertension, and their blood vessels show enhanced contraction and decreased cGMP-mediated relaxation. Thus, PKGI-alpha binds to, phosphorylates and activates RGS-2, attenuating receptor-mediated vascular contraction. Our study shows that RGS-2 is required for normal vascular function and blood pressure and is a new drug development target for hypertension.[1]

References

Regulator of G-protein signaling-2 mediates vascular smooth muscle relaxation and blood pressure. Tang, K.M., Wang, G.R., Lu, P., Karas, R.H., Aronovitz, M., Heximer, S.P., Kaltenbronn, K.M., Blumer, K.J., Siderovski, D.P., Zhu, Y., Mendelsohn, M.E., Tang, M., Wang, G. Nat. Med. (2003) [Pubmed]

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