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Published ahead of print on April 24, 2003, doi:10.1165/rcmb.2002-0157OC

Am. J. Respir. Cell Mol. Biol., Volume 29, Number 4, October 2003, 465-471

A more recent version of this article appeared on October 1, 2003
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Submitted on August 16, 2002
Revised on April 18, 2003

Hypoxia inhibits myosin phosphatase in pulmonary arterial smooth muscle cells: Role of Rho-kinase

Zhiqian Wang1, M. Carita Lanner1*, Najia Jin1, Darl Swartz2, Liang Li1, and Rodney A Rhoades1

1 Department of Cellular and Integrative Physiology, Indiana University School of Medicine, Indianapolis, IN, USA, 2 Department of Anatomy, Indiana University School of Medicine, Indianapolis, IN, USA

* To whom correspondence should be addressed. E-mail: clanner{at}iupui.edu.

Rho-kinase was recently found to phosphorylate the myosin binding subunit (MBS) of MP and to regulate MP activity. Although myosin light chain (MLC) phosphorylation in pulmonary arterial smooth muscle cells (PASMCs) is thought to be the cellular/molecular basis for hypoxia pulmonary vasoconstriction (HPV), very little is known about the role that Rho-kinase/MP plays in HPV. Rat PASMCs were cultured and made hypoxic (PO2=23±2 mmHg). Cells exposed to normoxia (PO2~148 mmHg) served as controls. PASMCs exposed to hypoxia showed a significant increase in MLC and MBS phosphorylation and a significant decease in MP activity. Rho-kinase inhibitors (HA1077 or Y-27632) blocked hypoxia-induced MP inactivation and inhibited the hypoxia-induced MLC phosphorylation. Hypoxia was also found to induce stress fiber formation and actin polymerization in cultured PASMCs. In summary, these data show that MP inhibition in PASMCs is linked to activation of Rho-kinase and that hypoxia inhibits the MP signaling pathway via Rho-kinase.




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