Cardiac Sarcolemmal Substrate of the cGMP-Dependent Protein Kinase

References

• Sperelakis N. Regulation of calcium slow channels in myocardial cells by cyclic nucleotides and phosphorylation. Protein Phosphorylation in Heart Muscle, R. J. Solaro. CRC Press, Boca Raton, FL 1986; 55–83
   Google Scholar
• Kohlhardt M, Haap K. 8-Bromo-guanosine-3′,5′-monophosphate mimics the effect of acetylcholine on slow response action potential and contractile force in mammalian atrial myocardium. J. Mol. Cell. Cardiol. 1978; 10: 573–586
   PubMedGoogle Scholar
• Wahler G. M., Sperelakis N. Intracellular injection of cyclic GMP depresses cardiac slow action potentials. J. Cyclic Nucl. Prot. Phosph. Res. 1985; 10: 83–95
   PubMedGoogle Scholar
• Bkaily G, Sperelakis N. Injection of Guanosine-3,5 cyclic monophosphate into heart cells blocks calcium slow channels. Am. J. Physiol. 1985; 248: H745–H749
   Google Scholar
• Hartzell H. C., Fischmeister R. Opposite effects of cyclic GMP and cyclic AMP on Ca2+ current in single heart cells. Nature 1986; 323: 273–275
   PubMed Web of Science ®Google Scholar
• MacLeod K. M., Diamond J. Effects of the cyclic GMP lowering agent LY83583 in the interaction of carbachol with forskolin in rabbit isolated cardiac preparations. J. Pharmacol. Exp. Therap. 1986; 238: 313–318
   PubMedGoogle Scholar
• Mehegan J. P., Muir W. W., Unverferth D. V., Fertel R. H., McGuick S. M. Electrophysiological effects of cGMP on canine cardiac Purkinje fibers. J. Cardiovasc. Pharmacol. 1985; 7: 30–35
   PubMedGoogle Scholar
• Wahler G. M., Rusch N. J., Sperelakis N. Inhibition of whole-cell calcium channel current by 8-bromo-cGMP in voltage clamped embryonic chick heart myocytes. Physiologist 1987; 30: 178, (abstract 45.4).
   Google Scholar
• Sperelakis N, Wahler G. M., Bkaily G. Properties of myocardial calcium slow channels and mechanisms of action of calcium antagonistic drugs. Current Topics in Membranes and Transport, A. Shamoo. Academic, Orlando, FL, 25: 43–76
   Google Scholar
• Jones L. R., Besch H. R., Jr., Fleming J. W., McConnaughy M. M., Watanabe A. M. Separation of vesicles of cardiac sarcolemma from vesicle of cardiac sarcoplasmic reticulum. J. Biol. Chem. 1979; 254: 530–539
   PubMed Web of Science ®Google Scholar
• Lowry O. H., Rosebrough N. J., Fair A. L., Randall R. J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 1970; 227: 680–685
   PubMed Web of Science ®Google Scholar
• Gill G. N., Holdy K. E., Walton G. M., Kanstein C. B. Purification and characterization of 3′,5′-cGMP dependent protein kinase. Proc. Natl. Acad. Sci. USA 1976; 73: 3918–3922
   PubMed Web of Science ®Google Scholar
• Lincoln T. M., Corbin J. D. Characterization and biological role of the cGMP-dependent protein kinase. Advances in Cyclic Nucleotide Research, P. Greengard, G. A. Robinson. Raven Press, New York 1983; 15: 139–192
   Google Scholar
• Walter U. Cyclic-GMP-regulated enzymes and their possible physiological functions. Advances in Cyclic Nucleotide and Protein Phosphorylation Research, P. Greengard, et al. Raven Press, New York 1984; 249–258
   Google Scholar
• Wrenn R. W., Kou J. F. cGMP-dependent phosphorylation of an endogenous protein from rat heart. Biochem. Biophys. Res. Commun. 1981; 101: 1274–1280
   PubMedGoogle Scholar
• Hamet D, Coquil J. F. cGMP binding and cGMP phosphodiesterase in rat platelets. J. Cyclic Nucl. Res. 1978; 4: 281–290
   PubMedGoogle Scholar
• Geahlen R. L., Krebs E. G. Regulatory subunit of the Type I cAMP-dependent protein kinase as an inhibitor and substrate of the cGMP-dependent protein kinase. J. Biol. Chem. 1980; 255: 1164–1169
   PubMed Web of Science ®Google Scholar
• Geahlen R. L., Krebs E. G. Studies of the phosphorylation of the type I cAMP-dependent protein kinase. J. Biol. Chem. 1980; 255: 9375–9379
   PubMed Web of Science ®Google Scholar
• Rao M. C., Toskulkao C. Characterization of a 50 kD flounder intestinal phosphoprotein. FASEB J. 1988; 2: A1725, (abstract 8302).
   Google Scholar