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Physiol. Genomics 17: 183-200, 2004. First published February 3, 2004; doi:10.1152/physiolgenomics.00207.2003
1094-8341/04 $5.00
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Received 11 December 2003; accepted in final form 27 January 2004.
Physiological Genomics 17:183-200 (2004)
1094-8341/04 $5.00 © 2004 American Physiological Society

Molecular heterogeneity of calcium channel ß-subunits in canine and human heart: evidence for differential subcellular localization

Jason D. Foell 1, Ravi C. Balijepalli 1, Brian P. Delisle 1, Anne Marie R. Yunker 3, Seth L. Robia 2, Jeffrey W. Walker 2, Maureen W. McEnery 3, Craig T. January 1,2 and Timothy J. Kamp 1,2

1 Department of Medicine, University of Wisconsin, Madison 53792
2 Department of Physiology, University of Wisconsin, Madison, Wisconsin 53706
3 Division of General Medical Sciences, Case Western Reserve University, Cleveland, Ohio 44106

Multiple Ca2+ channel ß-subunit (Cavß) isoforms are known to differentially regulate the functional properties and membrane trafficking of high-voltage-activated Ca2+ channels, but the precise isoform expression pattern of Cavß subunits in ventricular muscle has not been fully characterized. Using sequence data from the Human Genome Project to define the intron/exon structure of the four known Cavß genes, we designed a systematic RT-PCR strategy to screen human and canine left ventricular myocardial samples for all known Cavß isoforms. A total of 18 different Cavß isoforms were detected in both canine and human ventricles including splice variants from all four Cavß genes. Six of these isoforms have not previously been described. Western blots of ventricular membrane fractions and immunocytochemistry demonstrated that all four Cavß subunit genes are expressed at the protein level, and the Cavß subunits show differential subcellular localization with Cavß1b, Cavß2, and Cavß3 predominantly localized to the T-tubule sarcolemma, whereas Cavß1a and Cavß4 are more prevalent in the surface sarcolemma. Coexpression of the novel Cavß2c subunits (Cavß2cN1, Cavß2cN2, Cavß2cN4) with the pore-forming {alpha}1C (Cav1.2) and Cav{alpha}2{delta} subunits in HEK 293 cells resulted in a marked increase in ionic current and Cavß2c isoform-specific modulation of voltage-dependent activation. These results demonstrate a previously unappreciated heterogeneity of Cavß subunit isoforms in ventricular myocytes and suggest the presence of different subcellular populations of Ca2+ channels with distinct functional properties.

L-type calcium channel; splice variants




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