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Physiol. Genomics (February 3, 2004). doi:10.1152/physiolgenomics.00207.2003
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Submitted on December 11, 2003
Accepted on January 27, 2004

Molecular Heterogeneity of Calcium Channel {beta} Subunits in Canine and Human Heart: Evidence for Differential Subcellular Localization

Jason D Foell1, Ravi C Balijepalli1, Brian P Delisle1, Anne Marie R Yunker2, Seth L Robia3, Jeffrey W Walker3, Maureen W McEnery2, Craig T January4, and Timothy J Kamp4*

1 Medicine, University of Wisconsin, Madison, WI, USA
2 General Medical Sciences, Case Western Reserve University, Cleveland, OH, USA
3 Physiology, University of Wisconsin, Madison, WI, USA
4 Medicine, University of Wisconsin, Madison, WI, USA; Physiology, University of Wisconsin, Madison, WI, USA

* To whom correspondence should be addressed. E-mail: tjk{at}medicine.wisc.edu.

Multiple Ca2+ channel {beta} (Cav{beta}) subunit 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 Cav{beta} 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 Cav{beta} genes, we designed a systematic RT-PCR strategy to screen human and canine left ventricular myocardial samples for all known Cav{beta} isoforms. A total of 18 different Cav{beta} isoforms were detected in both canine and human ventricles including splice variants from all four Cav{beta} genes. Six of these isoforms have not previously been described. Western blots of ventricular membrane fractions and immunocytochemistry demonstrated that all four Cav{beta} subunit genes are expressed at the protein level, and the Cav{beta} subunits show differential subcellular localization with Cav{beta}1b, Cav{beta}2, Cav{beta}3 predominantly localized to the T-tubule sarcolemma, whereas, Cav{beta}1a and Cav{beta}4 are more prevalent in the surface sarcolemma. Co-expression of the novel Cav{beta}2c subunits (Cav{beta}2cN1, Cav{beta}2cN2, and Cav{beta}2cN4) 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 Cav{beta}2c isoform-specific modulation of voltage-dependent activation. These results demonstrate a previously unappreciated heterogeneity of Cav{beta} subunit isoforms in ventricular myocytes and suggest the presence of different subcellular populations of Ca2+ channels with distinct functional properties.




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