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(Received for publication, May 5, 1995) From the Intracellular application of proteases increases cardiac calcium
current to a level similar to
Volume 270,
Number 29,
Issue of July 21, pp. 17306-17310, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
Subunit in
Voltage-dependent Inactivation of Cardiac Calcium Channels
-adrenergic stimulation. Using
transiently transfected HEK 293 cells, we studied the molecular
mechanism underlying calcium channel stimulation by proteolytic
treatment. Perfusion of HEK cells, coexpressing the human cardiac (hHT)
, and 
subunits,
with 1 mg/ml of trypsin or carboxypeptidase A, increased the peak
amplitude of the calcium channel current 3-4-fold without
affecting the voltage dependence. Similar results were obtained in HEK
cells cotransfected with hHT 
and or
with alone, suggesting that modification of the
subunit itself is responsible for the current
enhancement by proteolysis. To further characterize the modification of
the subunit by trypsin, we expressed a deletion
mutant in which part of the carboxyl-terminal tail up to amino acid
1673 was removed. The expressed calcium channel currents no longer
responded to intracellular application of the proteases; however, a
3-fold higher current density as well as faster inactivation compared
with the wild type was observed. The results provide evidence that a
specific region of the carboxyl-terminal tail of the cardiac
subunit is an important regulatory segment that may
serve as a critical component of the gating machinery that influences
both inactivation properties as well as channel availability.
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