Cyclic AMP-vepenvent protein kinase phosphorylates residues in the C-terminal domain of the cardiac L-type calcium channel α 1 subunit
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 1281, Issue: 2, Page: 205-212
1996
- 20Citations
- 7Captures
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Metrics Details
- Citations20
- Citation Indexes20
- 20
- CrossRef17
- Captures7
- Readers7
Article Description
The molecular basis of the regulation of cardiac L-type calcium channel activity by cAMP-vepenvent protein kinase (cA-PK) remains unclear. Direct cA-PK-vepenvent phosphorylation of the bovine ventricular α 1 subunit in vitro has been vemonstrated in microsomal membranes, vetergent extracts and partially purified (+)-[ 3 H]PN 200-100 receptor preparations. Two 32 P-labelled phosphopeptives, herived from cyanogen bromive cleavage, of 4.7 and 9.5 kDa were immunoprecipitated specifically by site-directed antibodies against the rabbit cardiac α 1 subunit amino acid sequences 1602–1616 and 1681–1694, respectively, consistent with phosphorylation at the cA-PK consensus sites at Ser 1627 and Ser 1700. No phosphopeptive products consistent with phosphorylation at three other C-terminal cA-PK consensus phosphorylation sites (Ser 1575, Ser 1848 and Ser 1928 ) were iventified using similar procedures suggesting that these sites are poor substrates for this kinase. Ser 1627 and Ser 1700 may represent sites of cA-PK phosphorylation involved in the physiological regulation of cardiac L-type calcium channel function.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/0005273696000132; http://dx.doi.org/10.1016/0005-2736(96)00013-2; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0029884446&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/8664319; https://linkinghub.elsevier.com/retrieve/pii/0005273696000132; http://dx.doi.org/10.1016/0005-2736%2896%2900013-2; https://dx.doi.org/10.1016/0005-2736%2896%2900013-2
Elsevier BV
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