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(Received for publication, March 31, 1997, and in revised form, May 23, 1997)
From the Vascular Biology Center, Department of Pediatrics, and
Department of Pharmacology and Toxicology, Medical College of
Georgia, Augusta, Georgia 30912
Endothelial nitric-oxide synthase (eNOS) and
caveolin-1 are associated within endothelial plasmalemmal caveolae. It
is not known, however, whether eNOS and caveolin-1 interact directly or
indirectly or whether the interaction affects eNOS activity. To answer
these questions, we have cloned the bovine caveolin-1 cDNA and have
investigated the eNOS-caveolin-1 interaction in an in vitro
binding assay system using glutathione S-transferase (GST)-caveolin-1 fusion proteins and baculovirus-expressed bovine eNOS.
We have also mapped the domains involved in the interaction using an
in vivo yeast two-hybrid system. Results obtained using both in vitro and in vivo protein interaction
assays show that both N- and C-terminal cytosolic domains of caveolin-1
interact directly with the eNOS oxygenase domain. Interaction of eNOS
with GST-caveolin-1 fusion proteins significantly inhibits enzyme
catalytic activity. A synthetic peptide corresponding to caveolin-1
residues 82-101 also potently and reversibly inhibits eNOS activity by interfering with the interaction of the enzyme with
Ca2+/calmodulin (CaM). Regulation of eNOS in endothelial
cells, therefore, may involve not only positive allosteric
regulation by Ca2+/CaM, but also negative allosteric
regulation by caveolin-1.
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