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(Received for publication, April 17, 1997, and in revised form, May 29, 1997)
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From the The properties of cardiac L-type channels have
been well characterized electrophysiologically, and many such studies
have demonstrated that the channels are regulated by a
cAMP-dependent pathway. However, the subunit composition of
native cardiac L-type calcium channels has not been completely defined.
Furthermore, a very important question exists regarding the status of
the C-terminal domain of the pore-forming Department of Molecular Pharmacology and
Biological Chemistry, Northwestern University Medical School, Chicago,
Illinois 60611 and the Department of
Pharmacology, University of Illinois at Chicago,
Chicago, Illinois 60612
1
subunit, as this domain has the potential to be the target of protein
kinases but may be truncated as a result of post-translational
processing. In the present studies, the 1C and
2 subunits were identified by subunit-specific
antibodies after partial purification from heart membranes, or
immunoprecipitation from cardiac myocytes. Both the 2
and the full-length 1C subunits were found to be
expressed and co-localized in intact cardiac myocytes along T-tubule
membranes. Using a quantitative antibody binding analysis, we
demonstrated that the majority of the 1C subunits in
intact cardiac myocytes appear to be full-length. In addition, we
observed that adenylyl cyclase is localized in a pattern similar to the
channel subunits in cardiac myocytes. Taken together, our results
provide new insights into the structural basis for understanding the
regulation of L-type calcium channels by a cAMP-mediated signaling
pathway.
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