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Circulation Research. 2001;89:1030-1037
Published online before print October 25, 2001, doi: 10.1161/hh2301.100817
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(Circulation Research. 2001;89:1030.)
© 2001 American Heart Association, Inc.


Cellular Biology

Molecular Composition of 4-Aminopyridine-Sensitive Voltage-Gated K+ Channels of Vascular Smooth Muscle

Kevin S. Thorneloe, Tim T. Chen, Paul M. Kerr, Elizabeth F. Grier, Burton Horowitz, William C. Cole, Michael P. Walsh

From the Smooth Muscle Research Group and Canadian Institutes of Health Research (CIHR) Group in Regulation of Vascular Contractility (K.S.T., T.T.C., P.M.K., E.F.G., W.C.C., M.P.W.), University of Calgary, Alberta, Canada, and the Department of Physiology, University of Nevada School of Medicine (B.H.), Reno, Nev.

Correspondence to Dr William C. Cole, Smooth Muscle Research Group, University of Calgary, 3330 Hospital Dr NW, Calgary, Alberta T2N 4N1, Canada. E-mail wcole{at}ucalgary.ca

Voltage-gated K+ channels (Kv) play a critical role in regulating arterial tone by modulating the membrane potential of vascular smooth muscle cells. Our previous work demonstrated that the dominant 4-aminopyridine (4-AP)-sensitive, delayed rectifier Kv current of rabbit portal vein (RPV) myocytes demonstrates similar 4-AP sensitivity and biophysical properties to Kv1{alpha}-containing channels. To identify the molecular constituents underlying the 4-AP-sensitive Kv current of vascular myocytes, we characterized the expression pattern of Kv1{alpha} subunits and their modulatory Kvß subunits in RPV. The mRNAs encoding pore-forming subunits Kv1.2, Kv1.4, and Kv1.5 were detected by reverse transcriptase-polymerase chain reaction (RT-PCR), whereas Kv1.1, Kv1.3, and Kv1.6 transcripts were undetectable. Kvß1.1, ß1.2, ß1.3, ß2.1, and ß2.2 messages were expressed, whereas Kvß3.1 and ß4 mRNAs were undetected by RT-PCR. Kv1.2, Kv1.4, Kv1.5, Kvß1.2, ß1.3, and ß2.1 proteins were detected in RPV by Western blotting and/or immunocytochemistry of freshly isolated myocytes. We provide the first evidence, from coimmunoprecipitation studies, for the formation of heteromultimeric Kv channel complexes composed of Kv1.2, Kv1.5, and Kvß1.2 subunits in vascular smooth muscle.


Key Words: vascular smooth muscle • Kv1.5 • Kv1.2 • Kvß subunits • voltage-gated K+ channel




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