© 1999 American Heart Association, Inc.
Cellular Biology |
11,12-Epoxyeicosatrienoic Acid Stimulates Endogenous Mono-ADP-Ribosylation in Bovine Coronary Arterial Smooth Muscle
From the Departments of Pharmacology and Toxicology (P.-L.L., C.-L.C., W.B.C.), Medical College of Wisconsin, Milwaukee, Wis; Department of Medicine (R.B.), University of Massachusetts Medical Center, Worcester, Mass.
Correspondence and reprint requests to Pin-Lan Li, MD, PhD, Department of Pharmacology and Toxicology, Medical College of Wisconsin, 8701 Watertown Plank Rd, Milwaukee, WI 53226. E-mail pli{at}post.its.mcw.edu
Abstract—The role of
endogenous ADP-ribosylation in mediating the activation of
the Ca2+-activated K+ channels was
determined in bovine coronary arteries. Endogenous
ADP-ribosylation was examined by incubating coronary
arterial homogenates or lysates of cultured
coronary arterial smooth muscle cells with
[adenylate-32P]NAD. Four 32P-labeled
proteins were observed at 51, 52, 80, and 124 kDa in the
homogenates and lysates. This reaction was enhanced by the
addition of 11,12-epoxyeicosatrienoic acid (11,12-EET), a cytochrome
P450–derived eicosanoid, and GTP to the incubation. By Western blot
analysis, 42- and 70-kDa proteins were recognized by specific
antibodies against ADP-ribosyltransferase in the coronary
arterial homogenates and smooth muscle cell
lysate but not in the lysate of endothelial cells. The
52-kDa acceptor protein of endogenous ADP-ribosylation
comigrated with a protein ADP-ribosylated by cholera toxin and was
recognized and immunoprecipitated by an anti–GS
antibody. These results suggest that GS is one of
several acceptors of the ADP-ribose moiety. As shown by the patch-clamp
technique, 11,12-EET stimulated the activation of the K+
channels in the smooth muscle cells, and this activation was completely
blocked by novobiocin, vitamin K1, 3-aminobenzamide, and
m-iodobenzylguanidine, inhibitors of
endogenous mono-ADP-ribosyltransferases. We conclude that
endogenous mono-ADP-ribosyltransferases are present in
smooth muscle from bovine coronary arteries. These enzymes
transfer ADP-ribose to the cellular proteins such as GS
and may mediate intracellular signal transduction in coronary
vascular smooth muscle. In the coronary circulation, the
ADP-ribosylation signaling pathway may play an important role in
mediating the activation of the K+ channels induced by
11,12-EET.
Key Words: mono-ADP-ribosyltransferase • K+ channel • coronary artery • eicosanoid • epoxyeicosatrienoic acid
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