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 Lettjournal_title
FEBS lettersauthors
Haase H,Karczewski P,Beckert R,Krause EGdoi
10.1016/0014-5793(93)80733-bsubject
Has Abstractpub_date
1993-12-06 00:00:00pages
217-22issue
2eissn
0014-5793issn
1873-3468pii
0014-5793(93)80733-Bjournal_volume
335pub_type
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