Abstract
The entry of Ca into many excitable cells occurs through voltage-dependent Ca channels that are activated in response to depolarization. An interesting aspect of some Ca channels is that in addition to their voltage dependence, they can be regulated by neurotransmitters. This has been most thoroughly characterized in electrophysiological studies of cardiac cells (Reuter, 1983; Tsienet al., 1986). The probability of opening of the predominant type of cardiac Ca channel, that which is sensitive to dihydropyridines (Niliuset al., 1985), is increased by norepinephrine and decreased by acetylcholine (Reuter, 1983; Heschleret al., 1986; Tsienet al., 1986). This regulation is believed to be mediated by cyclic AMP (cAMP) and to involve a cAMP-dependent phosphorylation of the channel itself or an associated regulatory protein (Reuter, 1983). A similar type of regulation by cAMP has also been observed with Ca channels in skeletal muscle and some neuronal preparations (Schmidet al., 1985; Chad and Eckert, 1986). The regulation of Ca channels by mechanisms implicating protein kinases other than cAMP-dependent protein kinase also has been reported (Di Virgilioet al., 1986; Paupardin-Tritschet al., 1986; Rane and Dunlap, 1986; Galizziet al., 1987; Stronget al., 1987). A goal of our laboratory is to elucidate the biochemical events involved in the regulation of Ca channels by phosphorylation-dependent processes. To this end we initiated studies with dihydropyridine-sensitive Ca channels from cardiac and skeletal muscle to determine if any of the peptide components of these channels serve as a substrate for cAMP-dependent, as well as Ca-dependent, protein kinases.
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References
Borsotto, M., Barhanin, J., Norman, R. I., and Lazdunski, M., 1984, Purification of the dihydropyridine receptor of the voltage-sensitive calcium channel from skeletal muscle transverse tubules using ( + )[3H]PN 200–110, Biochem. Biophys. Res. Commun. 122:1357–1366.
Borsotto, M., Barhanin, J., Fosset, M., and Lazdunski, M., 1985, The 1,4-dihydropyridine receptor associated with skeletal muscle voltage-dependent Ca channels, J. Biol. Chem. 260:14255–14263.
Chad, J. E., and Eckert, R., 1986, An enzymatic mechanism for calcium current inactivation in dialysed Helix neurones, J. Physiol. 378:31–51.
Cooper, C. L., Vandaele, S., Barhanin, J., Fosset, M., Lazdunski, M., and Hosey, M. M., 1987, Purification and characterization of the dihydropyridine-sensitive voltage-dependent calcium channel from cardiac tissue, J. Biol. Chem. 262:509–512.
Curtis, B. M., and Catterall, W. A., 1984, Purification of the calcium antagonist receptor of voltagesensitive calcium channels from skeletal muscle transverse tubules, Biochemistry 23:2113–2118.
Di Virgilio, F., Pozzan, T., Wolheim, C. B., Vicentini, L. M., and Meldolesi, J., 1986, Tumor promoter phorbol myristate acetate inhibits Ca2+ influx through voltage-gated Ca2+ channels in two secretory cell lines, PC12 and RINm5F, J. Biol. Chem. 2611:32–35.
Galizzi, J.-P., Qar, J., and Fosset, M., VanRenterghem, C., and Lazdunski, M., 1987, Regulation of calcium channels in aortic smooth muscle cells by protein kinase C activators (diacylglycerol and phorbol esters) and by peptides (vasopressin and bombesin) that stimulate phosphoinositide break down, J. Biol. Chem. 262:6947–6950.
Heschler, J., Kameyama, M., and Trautwein, W., 1986, On the mechanism of muscarinic inhibition of the cardiac Ca current, Pflugers Arch. 407:182–189.
Hosey, M. M., Borsotto, M., and Lazdunski, M., 1986, Phosphorylation and dephosphorylation of the dihydropyridine-sensitive voltage-dependent Ca channel in skeletal muscle membranes by cAMP and Ca-dependent processes, Proc. Natl. Acad. Sci. USA 83:3733–3737.
Hunter, T., and Sefton, B. M., 1980, Transforming gene product of Rous sarcoma virus phosphorylates tyrosine, Proc. Natl. Acad. Sci. USA 77:1311–1315.
Laemmli, U. K., 1970, Cleavage of structural proteins during the assembly of the head of the bacteriophage T4, Nature 227:680–685.
McGuiness, T. L., Lai, Y., Greengard, P., Woodgett, J. R., and Cohen, P., 1983, A multifunctional calmodulin-dependent protein kinase, FEBS Lett. 163:329–334.
Nilius, B., Hess, P., Lansman, J. B., and Tsien, R. W., 1985, A novel type of cardiac calcium channel in ventricular cells, Nature 316:443–446.
Paupardin-Tritsch, D., Hammond, C., Gerschenfeld, H. M., Nairn, A. C., and Greengard, P., 1986, cGMP-dependent protein kinase enhances Ca current and potentiates the serotonin-induced Ca current increase in snail neurones, Nature 323:812–814.
Rane, S. G., and Dunlap, K., 1986, Kinase C activator 1,2-oleoylacetylglycerol attenuates voltagedependent calcium current in sensory neurons, Proc. Natl. Acad. Sci. USA 83:184–188.
Reuter, H., 1983, Calcium channel modulation by neurotransmitters, enzymes and drugs, Nature 301: 569–574.
Schmid, A., Renaud, J.-F., and Lazdunski, M., 1985, Short term and long term effects of ß-adrenergic effectors and cyclic AMP on nitrendipine-sensitive voltage-dependent Ca2+ channels of skeletal muscle, J. Biol. Chem. 260:13041–13046.
Schmid, A., Barhanin, J., Coppola, T., Borsotto, M., and Lazdunski, M., 1986, Immunochemical analysis of subunit structures of 1,4-dihydropyridine receptors associated with voltage-dependent Ca2+ channels in skeletal, cardiac, and smooth muscle, Biochemistry 25:3492–3495.
Streissnig, J., Knaus, H.-G., Grabner, M., Moosburger, K., Seitz, W., Leitz, H., and Glossman, H., 1987, Photoaffinity labeling of the phenylalkylamine receptor of the skeletal muscle transverse tubule calcium channel, FEBS Lett. 212:247–253.
Strong, J. A., Fox, A. P., Tsien, R. W., and Kaczmarek, L. K., 1987, Stimulation of protein kinase C recruits covert calcium channels in Aplysia bag cell neurons, Nature 325:714–717.
Sugden, P. H., Holladay, L. A., Reimann, E. M., and Corbin, J. D., 1976, Purification and charac terization of the catalytic subunit of adenosine, 3′:5′-cyclic monophosphate-dependent protein kinase from bovine liver, Biochem. J. 159:409–422.
Tsien, R. W., Bean, B. P., Hess, P., Lansman, J. B., Nilius, B., and Nowycky, M. C., 1986, Mechanisms of calcium channel modulation by beta-adrenergic agents and dihydropyridine calcium agonists, J. Mol. Cell. Cardiol. 18:691–710.
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© 1989 Plenum Press, New York
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Cooper, C.L., O’Callahan, C.M., Hosey, M.M. (1989). Phosphorylation of Dihydropyridine-Sensitive Calcium Channels from Cardiac and Skeletal Muscle. In: Fiskum, G. (eds) Cell Calcium Metabolism. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5598-4_8
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DOI: https://doi.org/10.1007/978-1-4684-5598-4_8
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