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Titel:

Unchanged beta-adrenergic stimulation of cardiac L-type calcium channels in Ca v 1.2 phosphorylation site S1928A mutant mice.

Dokumenttyp:
Journal Article; Research Support, Non-U.S. Gov't; Article
Autor(en):
Lemke, T; Welling, A; Christel, CJ; Blaich, A; Bernhard, D; Lenhardt, P; Hofmann, F; Moosmang, S
Abstract:
Phosphorylation of serine 1928 (Ser(1928)) of the cardiac Ca(v)1.2 subunit of L-type Ca(2+) channels has been proposed as the mechanism for regulation of L-type Ca(2+) channels by protein kinase A (PKA). To test this directly in vivo, we generated a knock-in mouse with targeted mutation of Ser(1928) to alanine. This mutation did not affect basal L-type current characteristics or regulation of the L-type current by PKA and the beta-adrenergic receptor, whereas the mutation abolished phosphorylati...     »
Zeitschriftentitel:
J Biol Chem
Jahr:
2008
Band / Volume:
283
Heft / Issue:
50
Seitenangaben Beitrag:
34738-44
Sprache:
eng
Volltext / DOI:
doi:10.1074/jbc.M804981200
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/18829456
Print-ISSN:
0021-9258
TUM Einrichtung:
Institut für Pharmakologie und Toxikologie
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