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Volume 17, Number 4,
Issue of February 15, 1997
pp. 1243-1255
Copyright ©1997 Society for Neuroscience
Modulation of the Cloned Skeletal Muscle L-Type Ca2+
Channel by Anchored cAMP-Dependent Protein Kinase
Received Sept. 20, 1996; revised Nov. 25, 1996; accepted Nov. 26, 1996.
Barry D. Johnson,
Jeffrey P. Brousal,
Blaise Z. Peterson,
Peter A. Gallombardo,
Gregory H. Hockerman,
Yvonne Lai,
Todd Scheuer, and
William A. Catterall
Department of Pharmacology, University of Washington, Seattle,
Washington 98195-7280
Ca2+ influx through skeletal muscle Ca2+
channels and the force of contraction are increased in response to
 -adrenergic stimulation and high-frequency electrical stimulation.
These effects are thought to be mediated by cAMP-dependent
phosphorylation of the skeletal muscle Ca2+ channel.
Modulation of the cloned skeletal muscle Ca2+ channel by
cAMP-dependent phosphorylation and by depolarizing prepulses was
reconstituted by transient expression in tsA-201 cells and compared to
modulation of the native skeletal muscle Ca2+ channel as
expressed in mouse 129CB3 skeletal muscle cells. The heterologously
expressed Ca2+ channel consisting of  1,
2 , and subunits gave currents that were similar
in time course, current density, and dihydropyridine sensitivity to the
native Ca2+ channel. cAMP-dependent protein kinase (PKA)
stimulation by Sp-5,6-DCl-cBIMPS (cBIMPS) increased currents through
both native and expressed channels two- to fourfold. Tail currents
after depolarizations to potentials between  20 and +80 mV increased
in amplitude and decayed more slowly as either the duration or
potential of the depolarization was increased. The time- and
voltage-dependent slowing of channel deactivation required the activity
of PKA, because it was enhanced by cBIMPS and reduced or eliminated by the peptide PKA inhibitor PKI (5-24) amide. This voltage-dependent modulation of the cloned skeletal muscle Ca2+ channel by
PKA also required anchoring of PKA by A-Kinase Anchoring Proteins
because it was blocked by peptide Ht 31, which disrupts such anchoring.
The results show that the skeletal muscle Ca2+ channel
expressed in heterologous cells is modulated by PKA at rest and during
depolarization and that this modulation requires anchored protein
kinase, as it does in native skeletal muscle cells.
Key words:
L-type Ca2+ channel;
cAMP-dependent protein
kinase;
skeletal muscle;
heterologous expression
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