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Circulation Research. 2003
Published online before print February 6, 2003, doi: 10.1161/01.RES.0000059987.90200.44
A more recent version of this article appeared on March 7, 2003
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Submitted on September 13, 2002
Revised on January 6, 2003
Accepted on January 17, 2003

Activation of RhoA and Inhibition of Myosin Phosphatase as Important Components in Hypertension in Vascular Smooth Muscle

Tetsuya Seko ; Masaaki Ito *; Yasuko Kureishi ; Ryuji Okamoto ; Nobuyuki Moriki ; Katsuya Onishi ; Naoki Isaka ; David J. Hartshorne ; and Takeshi Nakano

From the First Department of Internal Medicine (T.S., M.I., Y.K., R.O., N.M., K.O., N.I., T.N.), Mie University School of Medicine, Tsu, Mie, Japan; the Muscle Biology Group (D.J.H.), University of Arizona, Tucson, Ariz.

* To whom correspondence should be addressed. E-mail: m-ito{at}clin.medic.mie-u.ac.jp.

Two mechanisms are proposed to account for the inhibition of myosin phosphatase (MP) involved in Ca2+ sensitization of vascular muscle, ie, phosphorylation of either MYPT1, a target subunit of MP or CPI-17, an inhibitory phosphoprotein. In cultured vascular aorta smooth muscle cells (VSMCs), stimulation with angiotensin II activated RhoA, and this was blocked by pretreatment with 8-bromo-cGMP. VSMCs stimulated by angiotensin II, endothelin-1, or U-46619 significantly increased the phosphorylation levels of both MYPT1 (at Thr696) and CPI-17 (at Thr38). The angiotensin II-induced phosphorylation of MYPT1 was completely blocked by 8-bromo-cGMP or Y-27632 (a Rho-kinase inhibitor), but not by GF109203X (a PKC inhibitor). In contrast, phosphorylation of CPI-17 was inhibited only by GF109203X. Y-27632 dramatically corrected the hypertension in N{omega}-nitro-L-arginine methyl ester (L-NAME)-treated rats, and this hypertension also was sensitive to isosorbide mononitrate. The level of the active form of RhoA was significantly higher in aortas from L-NAME-treated rats. Expression of RhoA, Rho-kinase, MYPT1, CPI-17, and myosin light chain kinase were not significantly different in aortas from L-NAME-treated and control rats. Activation of RhoA without changes in levels of other signaling molecules were observed in three other rat models of hypertension, ie, stroke-prone spontaneously hypertensive rats, renal hypertensive rats, and DOCA-salt rats. These results suggest that independent of the cause of hypertension, a common point in downstream signaling and a critical component of hypertension is activation of RhoA and subsequent activation of Rho-kinase.
Key words: hypertension • RhoA • Rho-kinase • myosin phosphatase • Ca2+ sensitization




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V. Sauzeau, M. Rolli-Derkinderen, S. Lehoux, G. Loirand, and P. Pacaud
Sildenafil Prevents Change in RhoA Expression Induced by Chronic Hypoxia in Rat Pulmonary Artery
Circ. Res., October 3, 2003; 93(7): 630 - 637.
[Abstract] [Full Text] [PDF]

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 Physiol. Rev.Home page
A. P. SOMLYO and A. V. SOMLYO
Ca2+ Sensitivity of Smooth Muscle and Nonmuscle Myosin II: Modulated by G Proteins, Kinases, and Myosin Phosphatase
Physiol Rev, October 1, 2003; 83(4): 1325 - 1358.
[Abstract] [Full Text] [PDF]

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 Circ. Res.Home page
K. Ito, Y. Hirooka, K. Sakai, T. Kishi, K. Kaibuchi, H. Shimokawa, and A. Takeshita
Rho/Rho-Kinase Pathway in Brain Stem Contributes to Blood Pressure Regulation via Sympathetic Nervous System: Possible Involvement in Neural Mechanisms of Hypertension
Circ. Res., June 27, 2003; 92(12): 1337 - 1343.
[Abstract] [Full Text] [PDF]


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