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1 Boston Biomedical Research Institute, Watertown, MA, USA
2 Boston Biomedical Research Institute, Watertown, MA, USA; Department of Physiology, Tufts University Graduate School of Biomedical Sciences, Boston, MA, USA
3 Boston Biomedical Research Institute, Watertown, MA, USA; Department of Medicine, Harvard Medical School, Boston, MA, USA
* To whom correspondence should be addressed. E-mail: morgan{at}bbri.org.
Caveolin is a principal component of caveolar membranes. In the present study we utilized a decoy peptide approach to define the degree of involvement of caveolin in PKC-dependent regulation of contractility of differentiated vascular smooth muscle. The primary isoform of caveolin in ferret aorta vascular smooth muscle is caveolin-1. Chemical loading of contractile vascular smooth muscle tissue with a synthetic caveolin-1 scaffolding domain peptide inhibited PKC-dependent- increases in contractility induced by a phorbol ester or an alpha agonist. Peptide loading also resulted in a significant inhibition of phorbol ester-induced adducin Ser-662 phosphorylation, an intracellular monitor of PKC kinase activity, ERK-1/2 activation, and Ser 789 phosphorylation of the actin binding protein caldesmon. Alpha agonist-induced ERK1-1/2 activation was also inhibited by the caveolin-1 peptide. Scrambled peptide-loaded tissues or sham loaded tissues were unaffected with respect to both contractility and signaling. Depolarization-induced activation of contraction was not affected by caveolin peptide loading. Similar results with respect to contractility and ERK-1/2 activation during exposure to the phorbol ester or the alpha agonist were obtained with the cholesterol-depleting agent methyl-beta- cyclodextrin. These results are consistent with a role for caveolin-1 in the coordination of signaling leading to the regulation of contractility of smooth muscle.
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