Cyclic AMP-dependent phosphodiesterase isozyme-specific potentiation by protein kinase C in hypertrophic cardiomyopathic hamster hearts

Molecular Pharmacology

Volumn 50, Issue 3, 1996, Pages 549-555

  Yu, Hongwei ^a   Cai, John J ^a   Lee, Hon Chi ^a,b  

^a UNIVERSITY OF IOWA   (United States)

^b UNIVERSITY OF IOWA HOSPITALS AND CLINICS   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHODIESTERASE; PROTEIN KINASE C;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; DRUG POTENTIATION; ENZYME ACTIVATION; ENZYME KINETICS; ENZYME SPECIFICITY; HAMSTER; HYPERTROPHIC CARDIOMYOPATHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; QUANTITATIVE DIAGNOSIS;

3',5'-CYCLIC-GMP PHOSPHODIESTERASE; 3',5'-CYCLIC-NUCLEOTIDE PHOSPHODIESTERASE; ANIMALS; BRAIN; CARDIOMYOPATHY, HYPERTROPHIC; CELLS, CULTURED; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; CRICETINAE; HEART VENTRICLES; ISOENZYMES; KINETICS; MESOCRICETUS; MOLECULAR WEIGHT; MYOCARDIUM; PHOSPHORYLATION; PROTEIN KINASE C; RATS; REFERENCE VALUES;

EID: 0029786960     PISSN: 0026895X     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (37)

1. Lee, H., J. J. Cai, and H. Yu. Effect of protein kinase C on cyclic 3′,5′-adenosine monophosphate-dependent phosphodiesterase in hypertrophic cardiomyopathic hamster hearts. J. Pharmacol. Exp. Ther. 270:1171-1176 (1994).
2. Lee, H., J. J. Matsuda, S. I. Reynertson, J. B. Martins, and E. F. Shibata. Reversal of lidocaine effects on sodium currents by isoproterenol in rabbit hearts and heart cells. J. Clin. Invest. 91:693-701 (1993).
3. Bode, D. C., J. R. Kaner, and L. L. Brunton. Cellular distribution of phosphodiesterase isoforms in rat cardiac tissue. Circ. Res. 68:1070-1079 (1991).
4. Thompson, W. J., W. L. Terasaki, P. M. Epstein, and S. J. Strada. Assay of cyclic nucleotide phosphodiesterase and resolution of multiple molecular forms of enzyme. Adv. Cyclic Nucl. Res. 10:69-92 (1979).
5. Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254 (1976).
6. Hartzell, H. C. Regulation of cardiac ion channels by catecholamines, acetylcholine and second messenger systems. Prog. Biophys. Mol. Biol. 52:165-247 (1988).
7. Lytton, J., and D. H. MacLennan. Sarcoplasmic reticulum, in The Heart and Cardiovascular System: Scientific Foundation (H. A. Fozzard, E. Haber, R. B. Jennings, A. M. Katz, and H. E. Morgan, eds.). Raven Press, New York, 1203-1222 (1991).
8. Solaro, R. J. Protein phosphorylation and the cardiac myofilaments, in Protein Phosphorylation in Heart Muscle (R. J. Solaro, ed.). CRC Press, Boca Raton, 129-156 (1986).
9. Lindemann, J. P., and A. M. Watanabe. Mechanisms of adrenergic and cholinergic regulation of myocardial contractility, in Physiology and Pathophysiology of the Heart (N. Sperelakis, ed.). Kluver Academic Publishers, Boston, 423-452 (1989).
10. Beavo, J. A. Multiple isozymes of cyclic nucleotide phosphodiesterase. Adv. Second Messenger Phosphoprot. Res. 22:1-38 (1988).
11. Thompson, W. J. Cyclic nucleotide phosphodiesterases: pharmacology, biochemistry and function. Pharmacol. Ther. 51:13-33 (1991).
12. Beavo, J. A., M. Conti, and R. J. Heaslip. Multiple cyclic nucleotide phosphodiesterases. Mol. Pharmacol. 46:399-405 (1994).
13. M) cyclic adenosine monophosphate phosphodiesterase. Am. J. Cardiol. 63: 2A-8A (1989).
14. Wu, Z., R. K. Sharma, and J. H. Wang. Catalytic and regulatory properties of calmodulin-stimulated phosphodiesterase isozymes. Adv. Second Messenger Phosphoprot. Res. 25:29-43 (1992).
15. Sharma, R. K. Phosphorylation and characterization of bovine heart calmodulin-dependent phosphodiesterase. Biochemistry 30:5963-5968 (1991).
16. Beltman, J., W. K. Sonnenburg, and J. A. Beavo. The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases. Mol. Cell. Biochem. 127/128:239-253 (1993).
17. Zhang, G. Y., J. H. Wang, and R. K. Sharma. Purification and characterization of bovine brain calmodulin-dependent protein kinase II: the significance of autophosphorylation in the regulation of 63 kDa calmodulin-dependent cyclic nucleotide phosphodiesterase isozyme. Mol. Cell. Biochem. 122:159-169 (1993).
18. ++-dependent phosphorylation and dephosphorylation of 63-kDa subunit-containing bovine brain calmodulin-stimulated cyclic nucleotide phosphodiesterase isozyme. J. Biol. Chem. 264:1322-1328 (1986).
19. Charbonneau, H., N. Beier, K. A. Walsh, and J. A. Beavo. Identification of a conserved domain among cyclic nucleotide phosphodiesterases from diverse species. Proc. Natl. Acad. Sci. USA 83:9308-9312 (1986).
20. Bentley, J. K., A. Kadlecek, C. H. Sherbert, D. Seger, W. K. Sonnenburg, H. Charbonneau, J. P. Novack, and J. A. Beavo. Molecular cloning of cDNA encoding a "63"-kDa calmodulin-stimulated phosphodiesterase from bovine brain. J. Biol. Chem. 267:18676-18682 (1992).
21. Repaske, D. R. J. V. Swinnen, S.-L. C. Jin, J. J. Van Wyk, and M. Conti. A polymerase chain reaction strategy to identify and clone cyclic nucleotide phosphodiesterase cDNAs. J. Biol. Chem. 267:18683-18688 (1992).
22. Sonnenburg, W. K., D. Seger, and J. A. Beavo. Molecular cloning of a cDNA encoding the "61-kDa" calmodulin-stimulated cyclic nucleotide phosphodiesterase. J. Biol. Chem. 268:645-652 (1993).
23. Charbonneau, H., S. Kumar, J. P. Novack, D. K. Blumenthal, P. R. Griffin, J. Shabanowitz, D. F. Hunt, J. A. Beavo, and K. A. Walsh. Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain. Biochemistry 30:7931-7940 (1991).
24. Polli, J. W., and R. L. Kincaid. Molecular cloning of DNA encoding a calmodulin-dependent phosphodiesterase enriched in striatum. Proc. Natl. Acad. Sci. USA 89:11079-11083 (1992).
25. Kemp, B. E., and R. B. Pearson. Protein kinase recognition sequence motifs. Trends Biochem. Sci. 15:342-346 (1990).
26. Yasuda, I., A. Kishimoto, S. Tanaka, M. Tominaga, A. Sakuri, and Y. Nishizuka. A synthetic peptide substrate for selective assay of protein kinase C. Biochem. Biophys. Res. Commun. 166:1220-1227 (1990).
27. Trong, H. L., M. Beier, W. K. Sonnenburg, S. D. Stroop, K. A. Walsh, J. A. Beavo, and H. Charbonneau, Amino acid sequence of the cyclic GMP stimulated cyclic nucleotide phosphodiesterase from bovine heart. Biochemistry 29:10280-10288 (1990).
28. Bethke, T. W. Meyer, W. Schmitz, H. Scholz, B. Stein, K. Thomas, and H. Wenzlaff. Phosphodiesterase inhibition in ventricular cardiomyocytes from guinea-pig hearts. Br. J. Pharmacol. 107:127-133 (1992).
29. Sen, L., M. O'Neill, J. D. Marsh, and T. W. Smith. Myocyte structure, function, and calcium kinetics in the cardiomyopathic hamster heart. Am. J. Physiol. 259:H1533-H1543 (1990).
30. Sugioka, M., M. Ito, H. Masuoka, K. Ichikawa, T. Konishi, T. Tanka, and T. Nakano, Identification and characterization of isoenzymes of cyclic nucleotide phosphodiesterase in human kidney and heart, and the effects of new cardiotonic agents on these isoenzymes. Naunyn-Schmiedeberg's Arch. Pharmacol 350:284-293 (1994).
31. Xiong, Y., E. W. Westhead, and L. L. Slakey. Role of phosphodiesterase isoenzymes in regulating intracellular cyclic AMP in adenosine-stimulated smooth muscle cells. Biochem. J. 305:627-633 (1995).
32. Houslay, M. D., S. L. Griffiths, Y. M. Horton, C. Livingstone, M. Lobban, F. MacDonald, N. Morris, J. Pryde, G. Scotland, Y. Shakur, G. Sweeney, and E. K. Y. Tang. Regulation of intracellular cyclic AMP concentrations in hepatocytes involves the integrated activation and desensitization of adenylyl cyclase coupled with the action and activation of specific isoforms of cyclic AMP phosphodiesterase. Biochem. Soc. Trans. 20:140-146 (1992).
33. Mano, T., K. Iwase, Y. Sawai, N. Oda, Y. Nishida, T. Mokuno, Y. Itoh, M. Kotake, R. Masunaga, A. Nakai, T. Tujimura, A. Nagaska, and H. Hidaka. Changes of calmodulin concentration and cyclic 3′,5′-nucleotide phosphodiesterase activities in cardiac muscle of hyper- and hypothyroid rats. J. Endocrinol. 143:515-620 (1994).
34. Mishra, S. K., K. K. Menon, D. Roman, and S. Kumar. Calcium, calmodulin and 3′,5′-cyclic nucleotide phosphodiesterase activity in human muscular disorders. J. Neurol. Sci. 109:215-218 (1992).
35. Stabel, S., and P. J. Parker. Protein kinase C. Pharmacol. Ther. 51:71-95 (1991).
36. Cai, J. J., and H. Lee. Protein kinase C isozyme-specific modulation of cyclic AMP-dependent phosphodiesterase in hypertrophic cardiomyopathic hamster hearts. Mol. Pharmacol. 49:81-88 (1996).
37. Rouleau, J. L., L. H. S. Chuck, G. Hollosi, P. Kidd, R. E. Sievers, J. Wikman-Coffelt, and W. W. Parmley. Verapamil preserves myocardial contractility in the hereditary cardiomyopathy of the Syrian hamster. Circ. Res. 50:405-412 (1982).