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J Appl Physiol 102: 1595-1603, 2007. First published January 11, 2007; doi:10.1152/japplphysiol.01020.2006 Free Article
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Simulated microgravity effects on the rat carotid and femoral arteries: role of contractile protein expression and mechanical properties of the vessel wall

Sunup Hwang, Stanislav A. Shelkovnikov, and Ralph E. Purdy

Department of Pharmacology, School of Medicine, University of California, Irvine, California

Submitted 12 September 2006 ; accepted in final form 2 January 2007

The goal of this study was to determine the effects of microgravity on myofilament protein expression and both passive and active length-force relationships in carotid and femoral arteries. Microgravity was simulated by 20-day hindlimb unweighting (HU) in Wistar male rats, and carotid and femoral artery segments were isolated from both HU and control (CTL) rats for Western blot and length-force analysis. Western blots revealed that HU significantly decreased myosin light chain-20 (MLC-20) protein levels in both carotid and femoral arteries and decreased myosin heavy chain (MHC) in femoral artery. {alpha}-Actin levels were not altered by HU treatment in either artery. Length-force analysis demonstrated that HU did not change either passive or active length-force relationships in the femoral artery. HU-treated arterial rings developed significantly less force to 100 mM K+ than CTL, but optimal lengths were identical. In the carotid artery, length-active force curves were identical for both CTL and HU; however the length-passive force curve for HU-treated rings exhibited a steeper slope than CTL, suggesting decreased compliance of the artery wall. In conclusion, our data suggest that the HU-induced decreases in both MLC-20 and MHC in femoral artery are responsible for the decreased contraction to 100 mM K+ in HU-treated femoral artery rings. In the carotid artery, the HU-induced decrease in vessel wall compliance may counter any decrease in contractility caused by the decreased MLC-20 levels.

hindlimb unweighting; deoxyribonucleic acid; actin; myosin; length-force relationship



Address for reprint requests and other correspondence: R. E. Purdy, Dept. of Pharmacology, College of Medicine, Univ. of California, Irvine, CA 92697-4625 (e-mail: repurdy{at}uci.edu)




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