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Am J Physiol Heart Circ Physiol 277: H931-H939, 1999;
0363-6135/99 $5.00
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Vol. 277, Issue 3, H931-H939, September 1999

Phosphorylation events associated with cyclic nucleotidedependent inhibition of smooth muscle contraction

David A. Woodrum1, Colleen M. Brophy1,2,3,5, Christopher J. Wingard4, Arthur Beall3,5, and Howard Rasmussen1,2,3

1 Department of Cell Biology and Anatomy, 2 Department of Surgery, 3 Department of Medicine, Institute of Molecular Medicine and Genetics, and 4 Department of Physiology and Endocrinology, Medical College of Georgia, Augusta 30912; and 5 Augusta Veterans Affairs Medical Center, Augusta, Georgia 30901

Activation of cyclic nucleotide-dependent signaling pathways leads to relaxation of bovine carotid artery smooth muscle contractions and is associated with increased phosphorylation of the small heat shock-related protein (HSP20). Previous reports have shown that human umbilical artery smooth muscle is uniquely resistant to cyclic nucleotide-dependent relaxation, and HSP20 is not phosphorylated. In this investigation, we determined the phosphorylation events associated with cyclic nucleotide-dependent inhibition of smooth muscle contraction. In carotid artery, activation of cyclic nucleotide-dependent signaling pathways inhibited contractile responses to serotonin but did not inhibit myosin light chain phosphorylation or oxygen consumption. The inhibition of contraction was associated with increases in HSP20 phosphorylation. In umbilical artery, activation of cyclic nucleotide-dependent signaling pathways did not inhibit serotonin-induced contraction or myosin light chain phosphorylation. The lack of contractile inhibition in umbilical artery was not associated with significant increases in HSP20 phosphorylation. In conclusion, cyclic nucleotide-dependent contractile inhibition is independent of the inhibition of myosin light chain phosphorylation or oxygen consumption but does correlate with increased HSP20 phosphorylation.

heat shock proteins; myosin light chains; oxygen consumption


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