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(Received for publication, July 10, 1997, and in revised form, September 11, 1997)
From the Vascular Biology Center, the Department of Pediatrics, and
the Department of Pharmacology and Toxicology, Medical College of
Georgia, Augusta, Georgia 30912
Neuronal nitric-oxide synthase (nNOS) has been
shown previously to interact with 
1-syntrophin in
the dystrophin complex of skeletal muscle. In the present study, we
have examined whether nNOS also interacts with caveolin-3 in skeletal
muscle. nNOS and caveolin-3 are coimmunoprecipitated from rat skeletal
muscle homogenates by antibodies directed against either of the two
proteins. Synthetic peptides corresponding to the membrane-proximal
caveolin-3 residues 65-84 and 109-130 and homologous caveolin-1
residues 82-101 and 135-156 potently inhibit the catalytic activity
of purified, recombinant nNOS. Purified nNOS also binds to a
glutathione S-transferase-caveolin-1 fusion protein in
in vitro binding assays. In vitro binding is completely abolished by preincubation of nNOS with either of the two
caveolin-3 inhibitory peptides. Interactions between nNOS and
caveolin-3, therefore, appear to be direct and to involve two distinct
caveolin scaffolding/inhibitory domains. Other caveolin-interacting enzymes, including endothelial nitric-oxide synthase and the c-Src tyrosine kinase, are also potently inhibited by each of the four caveolin peptides. Inhibitory interactions mediated by two different caveolin domains may thus be a general feature of enzyme docking to
caveolin proteins in plasmalemmal caveolae.
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A. Papapetropoulos, R. D. Rudic, and W. C Sessa Molecular control of nitric oxide synthases in the cardiovascular system Cardiovasc Res, August 15, 1999; 43(3): 509 - 520. [Abstract] [Full Text] [PDF]
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A. Schlegel, R. B. Schwab, P. E. Scherer, and M. P. Lisanti A Role for the Caveolin Scaffolding Domain in Mediating the Membrane Attachment of Caveolin-1. THE CAVEOLIN SCAFFOLDING DOMAIN IS BOTH NECESSARY AND SUFFICIENT FOR MEMBRANE BINDING IN VITRO J. Biol. Chem., August 6, 1999; 274(32): 22660 - 22667. [Abstract] [Full Text] [PDF]
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