Phosphorylation of the L-type calcium channel beta subunit is involved in beta-adrenergic signal transduction in canine myocardium.

Abstract:

:Cyclic AMP-mediated phosphorylation of calcium channel subunits was studied in vitro and in vivo in preparations from dog heart. Calcium channels in native cardiac membranes were phosphorylated by cAMP-dependent protein kinase (PKA) solubilized with digitonin and subsequently immunoprecipitated using a polyclonal antibody generated against the deduced carboxy-terminal sequence of the cardiac beta subunit. A 62 kDa protein was identified as the major PKA-substrate in the immunoprecipitates. In the intact myocardium, this putative beta subunit was found to be phosphorylated in response to cAMP elevating agents. In contrast, no phosphorylation of a protein with an electrophoretic mobility similar to the alpha 1 subunit was detected, although 1,4-dihydropyridine receptor sites were recovered in the immunoprecipitates. Thus, we suggest that PKA-mediated phosphorylation of the beta subunit is the major mechanism for beta-adrenergic regulation of cardiac L-type calcium channel activity.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Haase H,Karczewski P,Beckert R,Krause EG

doi

10.1016/0014-5793(93)80733-b

subject

Has Abstract

pub_date

1993-12-06 00:00:00

pages

217-22

issue

2

eissn

0014-5793

issn

1873-3468

pii

0014-5793(93)80733-B

journal_volume

335

pub_type

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