메뉴 건너뛰기




Volumn 259, Issue 3, 1999, Pages 892-900

Activation of a cGMP-stimulated cAMP phosphodiesterase by protein kinase C in a liver Golgi-endosomal fraction

Author keywords

3'; 5' cyclic nucleotide phosphodiesterase; Cyclic AMP dependent protein kinases; Endosomes; Golgi apparatus; Phorbol esters; Protein kinase C

Indexed keywords

CYCLIC AMP PHOSPHODIESTERASE; CYCLIC GMP; PROTEIN KINASE C;

EID: 0033083849     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00123.x     Document Type: Article
Times cited : (36)

References (56)
  • 1
    • 0025994414 scopus 로고
    • Hormonal regulation of cyclic nucleotide phosphodiesterases
    • 1. Conti, M., Jin, C., Monaco, L., Repaske, D. & Swinnen, J.V. (1991) Hormonal regulation of cyclic nucleotide phosphodiesterases. Endocr. Rev. 12, 218-234.
    • (1991) Endocr. Rev. , vol.12 , pp. 218-234
    • Conti, M.1    Jin, C.2    Monaco, L.3    Repaske, D.4    Swinnen, J.V.5
  • 2
    • 0028136159 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterases
    • 2. Beavo, J., Conti, M. & Heaslip, R. (1994) Multiple cyclic nucleotide phosphodiesterases. Mol. Pharm. Acol. 46, 399-405.
    • (1994) Mol. Pharm. Acol. , vol.46 , pp. 399-405
    • Beavo, J.1    Conti, M.2    Heaslip, R.3
  • 3
    • 18144445994 scopus 로고
    • The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases
    • 3. Beltman, J., Sonnenburg, W.K. & Beavo, J.A. (1993) The role of protein phosphorylation in the regulation of cyclic nucleotide phosphodiesterases. Mol. Cell. Biochem. 127-128, 239-253.
    • (1993) Mol. Cell. Biochem. , vol.127-128 , pp. 239-253
    • Beltman, J.1    Sonnenburg, W.K.2    Beavo, J.A.3
  • 4
    • 0021944009 scopus 로고
    • Differential regulation of bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase isozymes by cyclic AMP-dependent protein kinase and calmodulin-dependent protein phosphatase
    • 4. Sharma, R.K. & Wang, J.H. (1985) Differential regulation of bovine brain calmodulin-dependent cyclic nucleotide phosphodiesterase isozymes by cyclic AMP-dependent protein kinase and calmodulin-dependent protein phosphatase. Proc. Natl Acad. Sci. USA 82, 2603-2607.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 2603-2607
    • Sharma, R.K.1    Wang, J.H.2
  • 5
    • 0022559490 scopus 로고
    • 2+ dependent phosphorylation and dephosphorylation of the 63 kDa subunit-containing bovine brain calmodulin stimulated cyclic nucleotide phosphodiesterase isozyme
    • 2+ dependent phosphorylation and dephosphorylation of the 63 kDa subunit-containing bovine brain calmodulin stimulated cyclic nucleotide phosphodiesterase isozyme. J. Biol. Chem. 261, 1322-1328.
    • (1986) J. Biol. Chem. , vol.261 , pp. 1322-1328
    • Sharma, R.K.1    Wang, J.H.2
  • 7
    • 0023677847 scopus 로고
    • Activation of the particulate low Km phosphodiesterase of adipocytes by addition of cAMP-dependent protein kinase
    • 7. Gettys, T.W., Vine, A.J., Simmons, M.F. & Corbin, J.D. (1988) Activation of the particulate low Km phosphodiesterase of adipocytes by addition of cAMP-dependent protein kinase. J. Biol. Chem. 263, 10359-10363.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10359-10363
    • Gettys, T.W.1    Vine, A.J.2    Simmons, M.F.3    Corbin, J.D.4
  • 8
    • 0023679813 scopus 로고
    • Phosphorylation results in activation of a cAMP phosphodiesterase in human platelets
    • 8. Macphee, C.H., Reifsnyder, D.H., Moore, T., Lerea, K.M. & Beavo, J. (1988) Phosphorylation results in activation of a cAMP phosphodiesterase in human platelets. J. Biol. Chem. 263, 10353-10358.
    • (1988) J. Biol. Chem. , vol.263 , pp. 10353-10358
    • Macphee, C.H.1    Reifsnyder, D.H.2    Moore, T.3    Lerea, K.M.4    Beavo, J.5
  • 9
    • 0024323112 scopus 로고
    • Activation and phosphorylation of the 'dense vesicle' high affinity cyclic AMP phosphodiesterase by cAMP-dependent protein kinase
    • 9. Kilgour, E., Anderson, N.G. & Houslay, M.D. (1989) Activation and phosphorylation of the 'dense vesicle' high affinity cyclic AMP phosphodiesterase by cAMP-dependent protein kinase. Biochem. J. 269, 27-36.
    • (1989) Biochem. J. , vol.269 , pp. 27-36
    • Kilgour, E.1    Anderson, N.G.2    Houslay, M.D.3
  • 10
    • 0025278787 scopus 로고
    • Stimulation of the insulin-sensitive cAMP phosphodiesterase by an ATP-dependent soluble factor from insulin-treated rat adipocytes
    • 10. Shibata, H. & Kono, T. (1990) Stimulation of the insulin-sensitive cAMP phosphodiesterase by an ATP-dependent soluble factor from insulin-treated rat adipocytes. Biochem. Biophys. Res. Commun. 167, 614-620.
    • (1990) Biochem. Biophys. Res. Commun. , vol.167 , pp. 614-620
    • Shibata, H.1    Kono, T.2
  • 11
    • 0027326931 scopus 로고
    • Stimulation by insulin of a serine kinase in human platelets that phosphorylates and activates the cGMP-inhibited cAMP phosphodiesterase
    • 11. Lopez-Aparacio, P., Belfrage, P., Manganiello, V., Kono, T. & Degerman, E. (1993) Stimulation by insulin of a serine kinase in human platelets that phosphorylates and activates the cGMP-inhibited cAMP phosphodiesterase. Biochem. Biophys. Res. Commun. 193, 1137-1144.
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 1137-1144
    • Lopez-Aparacio, P.1    Belfrage, P.2    Manganiello, V.3    Kono, T.4    Degerman, E.5
  • 12
    • 0019230601 scopus 로고
    • Insulin triggers cyclic AMP-dependent activation and phosphorylation of a plasma membrane cyclic AMP phosphodiesterase
    • 12. Marchmont, R.J. & Houslay, M.D. (1980) Insulin triggers cyclic AMP-dependent activation and phosphorylation of a plasma membrane cyclic AMP phosphodiesterase. Nature 286, 904-906.
    • (1980) Nature , vol.286 , pp. 904-906
    • Marchmont, R.J.1    Houslay, M.D.2
  • 13
    • 0028243837 scopus 로고
    • The short-term activation of a rolipram-sensitive cAMP-specific phosphodiesterase by thyroid-stimulating hormone in thyroid FRTL-5 cells mediated by a cAMP-dependent phosphorylation
    • 13. Sette, C., Iona, S. & Conti, M. (1994) The short-term activation of a rolipram-sensitive cAMP-specific phosphodiesterase by thyroid-stimulating hormone in thyroid FRTL-5 cells mediated by a cAMP-dependent phosphorylation. J. Biol. Chem. 269, 9245-9252.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9245-9252
    • Sette, C.1    Iona, S.2    Conti, M.3
  • 14
    • 0028360098 scopus 로고
    • The rat PDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase
    • 14. Sette, Vicini, E. & Conti, M. (1994) The rat PDE3/IVd phosphodiesterase gene codes for multiple proteins differentially activated by cAMP-dependent protein kinase. J. Biol. Chem. 269, 18271-18274.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18271-18274
    • Sette, V.E.1    Conti, M.2
  • 15
    • 0026566697 scopus 로고
    • The catalytic subunit of protein kinase a triggers activation of the type V cyclic GMP-specific phosphodiesterase from guinea-pig lung
    • 15. Burns, F., Rodger, I.W. & Pyne, N. (1992) The catalytic subunit of protein kinase A triggers activation of the type V cyclic GMP-specific phosphodiesterase from guinea-pig lung. Biochem. J. 283, 487-491.
    • (1992) Biochem. J. , vol.283 , pp. 487-491
    • Burns, F.1    Rodger, I.W.2    Pyne, N.3
  • 16
    • 0026046502 scopus 로고
    • A new cGMP phosphodiesterase isolated from bovine platelets is substrate for cAMP and cGMP-dependent protein kinases: Evidence for a key role in the process of platelet activation
    • 16. Robichon, A. (1991) A new cGMP phosphodiesterase isolated from bovine platelets is substrate for cAMP and cGMP-dependent protein kinases: evidence for a key role in the process of platelet activation. J. Cell. Biochem. 47, 147-157.
    • (1991) J. Cell. Biochem. , vol.47 , pp. 147-157
    • Robichon, A.1
  • 17
    • 0025143899 scopus 로고
    • Substrate- and kinase-directed regulation of phosphorylation of a cGMP binding phosphodiesterase by cGMP
    • 17. Thomas, M.K., Francis, S.H. & Corbin, J.D. (1990) Substrate-and kinase-directed regulation of phosphorylation of a cGMP binding phosphodiesterase by cGMP. J. Biol. Chem. 265, 14971-14978.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14971-14978
    • Thomas, M.K.1    Francis, S.H.2    Corbin, J.D.3
  • 18
    • 0025778534 scopus 로고
    • Phosphatidylinositol-stimulated phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in vertebrate rod photoreceptors
    • 18. Hayashi, F., Lin, G.Y., Matsumoto, H. & Yamazaki, A. (1991) Phosphatidylinositol-stimulated phosphorylation of an inhibitory subunit of cGMP phosphodiesterase in vertebrate rod photoreceptors. Proc. Natl Acad. Sci. USA 88, 4333-4337.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 4333-4337
    • Hayashi, F.1    Lin, G.Y.2    Matsumoto, H.3    Yamazaki, A.4
  • 19
    • 0013596145 scopus 로고
    • The role of protein kinase C in transmembrane signalling
    • 19. Kikkawa, U. & Nishizuka, Y. (1986) The role of protein kinase C in transmembrane signalling. Annu. Rev. Cell. Biol. 58, 31-44.
    • (1986) Annu. Rev. Cell. Biol. , vol.58 , pp. 31-44
    • Kikkawa, U.1    Nishizuka, Y.2
  • 20
    • 0023035691 scopus 로고
    • The phorbol ester TPA inhibits cyclic AMP phosphodiesterase activity in intact hepatocytes
    • 20. Irvine, F., Pyne, N.J. & Houslay, M.D. (1986) The phorbol ester TPA inhibits cyclic AMP phosphodiesterase activity in intact hepatocytes. FEBS Lett. 208, 455-459.
    • (1986) FEBS Lett. , vol.208 , pp. 455-459
    • Irvine, F.1    Pyne, N.J.2    Houslay, M.D.3
  • 21
    • 0023156708 scopus 로고
    • Phorbol 12-myristate 13-acetate and vasopressin potentiate the effect of corticotropin-releasing factor on cyclic AMP production in rat anterior pituitary cells
    • 21. Abou-Samra, A.B., Harwood, J.P., Manganiello, V.C., Catt, K.J. & Aguilera, J. (1987) Phorbol 12-myristate 13-acetate and vasopressin potentiate the effect of corticotropin-releasing factor on cyclic AMP production in rat anterior pituitary cells. J. Biol. Chem. 262, 1129-1136.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1129-1136
    • Abou-Samra, A.B.1    Harwood, J.P.2    Manganiello, V.C.3    Catt, K.J.4    Aguilera, J.5
  • 22
    • 0025943154 scopus 로고
    • Protein kinase C modulates cAMP content in proximal tubular cells: Role of phosphodiesterase inhibition
    • 22. Le Goas, F., Amiel, C. & Friedlander, G. (1991) Protein kinase C modulates cAMP content in proximal tubular cells: role of phosphodiesterase inhibition. Am. J. Physiol. 261, F587-F592.
    • (1991) Am. J. Physiol. , vol.261
    • Le Goas, F.1    Amiel, C.2    Friedlander, G.3
  • 23
    • 0022777745 scopus 로고
    • Activation of cyclic amp phosphodiesterase by phorbol and protein kinase C pathway
    • 23. Solomon, S.S. & Palazzolo, M. (1986) Activation of cyclic AMP phosphodiesterase by phorbol and protein kinase C pathway. Am. J. Med. Sci. 292, 182-184.
    • (1986) Am. J. Med. Sci. , vol.292 , pp. 182-184
    • Solomon, S.S.1    Palazzolo, M.2
  • 24
    • 0028062140 scopus 로고
    • Effect of protein kinase C on 3′, 5′-adenosine monophosphate-dependent phosphodiesterase in hypertrophic cardiomyopathic hamster hearts
    • 24. Lee, H.C., Cai, J.J. & Yu, H. (1994) Effect of protein kinase C on 3′, 5′-adenosine monophosphate-dependent phosphodiesterase in hypertrophic cardiomyopathic hamster hearts. J. Pharmacol. Exp. Ther. 270, 1171-1176.
    • (1994) J. Pharmacol. Exp. Ther. , vol.270 , pp. 1171-1176
    • Lee, H.C.1    Cai, J.J.2    Yu, H.3
  • 25
    • 0028308363 scopus 로고
    • Functional effect of phosphorylation of the photoreceptor phosphodiesterase inhibitory subunit by protein kinase C
    • 25. Udovichenko, I.P., Cunnick, J., Gonzalez, K. & Takemoto, D. (1994) Functional effect of phosphorylation of the photoreceptor phosphodiesterase inhibitory subunit by protein kinase C. J. Biol. Chem. 269, 9850-9856.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9850-9856
    • Udovichenko, I.P.1    Cunnick, J.2    Gonzalez, K.3    Takemoto, D.4
  • 26
    • 0022894984 scopus 로고
    • Acute in vivo stimulation of low Km cyclic AMP phosphodiesterase activity by insulin in rat liver Golgi fractions
    • 26. Benelli, C., Desbuquois, B. & De Gallé, B. (1986) Acute in vivo stimulation of low Km cyclic AMP phosphodiesterase activity by insulin in rat liver Golgi fractions. Eur. J. Biochem. 156, 211-220.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 211-220
    • Benelli, C.1    Desbuquois, B.2    De Gallé, B.3
  • 27
    • 0025804585 scopus 로고
    • Characterization of a liver high substrate concentration phosphodiesterase activity sensitive to thyroid status
    • 27. Benelli, C., Geoffroy, V., Fouque, F., Lopez, S. & Desbuquois, B. (1991) Characterization of a liver high substrate concentration phosphodiesterase activity sensitive to thyroid status. Endocrinology 128, 2376-2386.
    • (1991) Endocrinology , vol.128 , pp. 2376-2386
    • Benelli, C.1    Geoffroy, V.2    Fouque, F.3    Lopez, S.4    Desbuquois, B.5
  • 28
    • 0027436284 scopus 로고
    • Evidence that growth hormone stimulates protein kinase C activity in isolated rat hepatocytes
    • 28. Nivet, V., Clot, J.P., Do, X.T., Barrault, V., Prélot, M. & Durand, D. (1993) Evidence that growth hormone stimulates protein kinase C activity in isolated rat hepatocytes. Metabolism 42, 1291-1295.
    • (1993) Metabolism , vol.42 , pp. 1291-1295
    • Nivet, V.1    Clot, J.P.2    Do, X.T.3    Barrault, V.4    Prélot, M.5    Durand, D.6
  • 29
    • 0025139101 scopus 로고
    • (3H) PDBu binding using a 96 well microtiter plate and a cell harvester
    • (3H) PDBu binding using a 96 well microtiter plate and a cell harvester. Analyt. Biochem. 184, 283-290.
    • (1990) Analyt. Biochem. , vol.184 , pp. 283-290
    • Parant, M.R.1    Vial, H.J.2
  • 30
    • 0023161296 scopus 로고
    • Hormone-and tumor promoter-induced activation or membrane association of protein kinase C in intact cells
    • 30. Thomas, T.P., Gopalakrishna, R. & Anderson, W.B. (1987) Hormone-and tumor promoter-induced activation or membrane association of protein kinase C in intact cells. Enzymology 141, 339-435.
    • (1987) Enzymology , vol.141 , pp. 339-435
    • Thomas, T.P.1    Gopalakrishna, R.2    Anderson, W.B.3
  • 31
    • 0015231739 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterase activities from rat brain
    • 31. Thompson, W.J. & Appleman, M.M. (1971) Multiple cyclic nucleotide phosphodiesterase activities from rat brain. Biochemistry 10, 10311-10316.
    • (1971) Biochemistry , vol.10 , pp. 10311-10316
    • Thompson, W.J.1    Appleman, M.M.2
  • 32
    • 0019987237 scopus 로고
    • Insulin-dependent and insulin-independent high substrate concentration phosphodisterase from rat adipose tissue
    • 32. Weber, H.W. & Appleman, M.M. (1981) Insulin-dependent and insulin-independent high substrate concentration phosphodisterase from rat adipose tissue. J. Biol. Chem. 257, 5339-5341.
    • (1981) J. Biol. Chem. , vol.257 , pp. 5339-5341
    • Weber, H.W.1    Appleman, M.M.2
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein binding
    • 35. Bradford, M.M. (1976) A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein binding. Analyt. Biochem. 72, 248-254.
    • (1976) Analyt. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 36
    • 0023643421 scopus 로고
    • Calcium-activated, phospholipid-dependent protein kinases C from rat liver. Subcellular distribution, purification and characterization of multiple forms
    • 36. Azhar, S., Butte, J. & Reaven, C. (1987) Calcium-activated, phospholipid-dependent protein kinases C from rat liver. Subcellular distribution, purification and characterization of multiple forms. Biochemistry 26, 7047-7057.
    • (1987) Biochemistry , vol.26 , pp. 7047-7057
    • Azhar, S.1    Butte, J.2    Reaven, C.3
  • 37
    • 0026068576 scopus 로고
    • 'Crosstalk': A pivotal role for protein kinase C in modulating relationship between signal transduction pathway
    • 37. Houslay, M.D. (1991) 'Crosstalk': a pivotal role for protein kinase C in modulating relationship between signal transduction pathway. Eur. J. Biochem. 195, 9-27.
    • (1991) Eur. J. Biochem. , vol.195 , pp. 9-27
    • Houslay, M.D.1
  • 38
    • 0027418233 scopus 로고
    • Stimulation of specific types of Gs-stimulated adenylyl cyclases by phorbol ester treatment
    • 38. Jacobowitz, O., Chen, J., Premout, R.T. & Yyengar, R. (1993) Stimulation of specific types of Gs-stimulated adenylyl cyclases by phorbol ester treatment. J. Biol. Chem. 268, 3829-3832.
    • (1993) J. Biol. Chem. , vol.268 , pp. 3829-3832
    • Jacobowitz, O.1    Chen, J.2    Premout, R.T.3    Yyengar, R.4
  • 39
    • 0027528490 scopus 로고
    • Phorbol ester stimulation of the type I and type III adenylyl cyclases in whole cells
    • 39. Choi, E.J., Wong, S.T., Dittman, A.H. & Storm, D.R. (1993) Phorbol ester stimulation of the type I and type III adenylyl cyclases in whole cells. Biochemistry 32, 1891-1894.
    • (1993) Biochemistry , vol.32 , pp. 1891-1894
    • Choi, E.J.1    Wong, S.T.2    Dittman, A.H.3    Storm, D.R.4
  • 41
    • 0029074582 scopus 로고
    • Erythro-9 (2-hydroxy-3-nonyl) adenine inhibits cyclic GMP-stimulated phosphodiesterase in isolated cardiac myocytes
    • 41. Mery, P.F., Pavoine, C., Pecker, F. & Fischmeister, R. (1995) Erythro-9 (2-hydroxy-3-nonyl) adenine inhibits cyclic GMP-stimulated phosphodiesterase in isolated cardiac myocytes. Mol. Pharmacol. 48, 121-130.
    • (1995) Mol. Pharmacol. , vol.48 , pp. 121-130
    • Mery, P.F.1    Pavoine, C.2    Pecker, F.3    Fischmeister, R.4
  • 42
    • 0029962380 scopus 로고    scopus 로고
    • Rapid regulation of PDE-2 and PDE-4 cyclic AMP phosphodiesterase activity following ligation of the T cell antigen receptor on thymocytes: Analysis using the selective inhibitors erythro-9-(2-hydroxy-3-nonyl)-adenine (EHNA) and rolipram
    • 42. Michie, A.M., Lobban, M., Müller, T., Harnett, M.M. & Houslay, M.D. (1996) Rapid regulation of PDE-2 and PDE-4 cyclic AMP phosphodiesterase activity following ligation of the T cell antigen receptor on thymocytes: analysis using the selective inhibitors erythro-9-(2-hydroxy-3-nonyl)-adenine (EHNA) and rolipram. Cell. Signal. 8, 97-110.
    • (1996) Cell. Signal. , vol.8 , pp. 97-110
    • Michie, A.M.1    Lobban, M.2    Müller, T.3    Harnett, M.M.4    Houslay, M.D.5
  • 43
    • 0029737541 scopus 로고    scopus 로고
    • Characterization of two recombinant PDE3 (cGMP-inhibited cyclic nucleotide phosphodiesterase) isoforms, RcGIP1 and HcGIP2, expressed in NIH 3006 murine fibroblasts and Sf9 insect cells
    • 43. Leroy, M.J., Degerman, E., Taira, M., Murata, T., Wang, L.H., Movsesian, M.A., Meacci, E. & Manganiello, V.C. (1996) Characterization of two recombinant PDE3 (cGMP-inhibited cyclic nucleotide phosphodiesterase) isoforms, RcGIP1 and HcGIP2, expressed in NIH 3006 murine fibroblasts and Sf9 insect cells. Biochemistry 35, 10194-10202.
    • (1996) Biochemistry , vol.35 , pp. 10194-10202
    • Leroy, M.J.1    Degerman, E.2    Taira, M.3    Murata, T.4    Wang, L.H.5    Movsesian, M.A.6    Meacci, E.7    Manganiello, V.C.8
  • 44
    • 0022537772 scopus 로고
    • Phorbol esters, but not epidermal growth factor or insulin rapidly decrease soluble protein kinase C activity in rat hepatocytes
    • 44. Vaarjes, W.J., De Haas, C.G.M. & Van Den Bergh, S.G. (1986) Phorbol esters, but not epidermal growth factor or insulin rapidly decrease soluble protein kinase C activity in rat hepatocytes. Biochem. Biophys. Res. Commun. 138, 1328-1333.
    • (1986) Biochem. Biophys. Res. Commun. , vol.138 , pp. 1328-1333
    • Vaarjes, W.J.1    De Haas, C.G.M.2    Van Den Bergh, S.G.3
  • 45
    • 0025769221 scopus 로고
    • Differences in phorbol ester-induced decrease of the activity of protein kinase C isozymes in rat hepatocytes
    • 45. Robles-Flores, M., Alcantara-Hernandez, R. & Garcia-Sainz, J.A. (1991) Differences in phorbol ester-induced decrease of the activity of protein kinase C isozymes in rat hepatocytes. Biochim. Biophys. Acta 1094, 77-84.
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 77-84
    • Robles-Flores, M.1    Alcantara-Hernandez, R.2    Garcia-Sainz, J.A.3
  • 46
    • 0024583044 scopus 로고
    • Isozymics forms of protein kinase C in regenerating rat liver
    • 46. Houwelling, M., Vaartjes, W.J. & Van Golde, L.M.G. (1989) Isozymics forms of protein kinase C in regenerating rat liver. FEBS Lett. 247, 487-491.
    • (1989) FEBS Lett. , vol.247 , pp. 487-491
    • Houwelling, M.1    Vaartjes, W.J.2    Van Golde, L.M.G.3
  • 47
    • 0026545286 scopus 로고
    • Glucagon, vasopressin and angiotensin all elicit a rapid, transient increase in hepatocyte protein kinase C activity
    • 47. Tang, E.K.Y. & Houslay, M.D. (1992) Glucagon, vasopressin and angiotensin all elicit a rapid, transient increase in hepatocyte protein kinase C activity. Biochem. J. 283, 341-346.
    • (1992) Biochem. J. , vol.283 , pp. 341-346
    • Tang, E.K.Y.1    Houslay, M.D.2
  • 49
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • 49. Hug, H. & Sarre, T.F. (1993) Protein kinase C isoenzymes: divergence in signal transduction? Biochem. J. 291, 329-343.
    • (1993) Biochem. J. , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 52
    • 0027207807 scopus 로고
    • Diabetes induces selective alterations in the expression of protein kinase C isoforms in hepatocytes
    • 52. Tang, E.Y., Parker, P.J., Beattie, J. & Houslay, M.D. (1993) Diabetes induces selective alterations in the expression of protein kinase C isoforms in hepatocytes. FEBS. Lett. 326, 117-123.
    • (1993) FEBS. Lett. , vol.326 , pp. 117-123
    • Tang, E.Y.1    Parker, P.J.2    Beattie, J.3    Houslay, M.D.4
  • 53
    • 0028314237 scopus 로고
    • Partial purification of protein kinase isoenzymes from rat liver
    • 53. Perletti, G.P. (1994) Partial purification of protein kinase isoenzymes from rat liver. J. Biochem. Biophys. Methods 28, 195-204.
    • (1994) J. Biochem. Biophys. Methods , vol.28 , pp. 195-204
    • Perletti, G.P.1
  • 54
    • 0026316323 scopus 로고
    • Structure and function studies of the cGMP-stimulated phosphodiesterase
    • 54. Stroop, S.D. & Beavo, J.A. (1991) Structure and function studies of the cGMP-stimulated phosphodiesterase. J. Biol. Chem. 266, 23802-23809.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23802-23809
    • Stroop, S.D.1    Beavo, J.A.2
  • 55
    • 0023809303 scopus 로고
    • Purification and partial characterization of membrane-associated type II (cGMP-activable) cyclic nucleotide phosphodiesterase from rabbit brain
    • 55. Whalin, M.E., Strada, S.J. & Thompson, W.J. (1988) Purification and partial characterization of membrane-associated type II (cGMP-activable) cyclic nucleotide phosphodiesterase from rabbit brain. Biochim. Biophys. Acta 972, 79-94.
    • (1988) Biochim. Biophys. Acta , vol.972 , pp. 79-94
    • Whalin, M.E.1    Strada, S.J.2    Thompson, W.J.3
  • 56
    • 0022454622 scopus 로고
    • Isolation and characterization of bovine cardiac muscle cGMP-inhibited phosphodiesterase: A receptor for new cardiotonic drugs
    • 56. Harrison, S.A., Reifsnyder, D.H., Gallis, B., Cadd, G.G. & Beavo, J.A. (1986) Isolation and characterization of bovine cardiac muscle cGMP-inhibited phosphodiesterase: a receptor for new cardiotonic drugs. Mol. Pharmacol. 29, 506-514.
    • (1986) Mol. Pharmacol. , vol.29 , pp. 506-514
    • Harrison, S.A.1    Reifsnyder, D.H.2    Gallis, B.3    Cadd, G.G.4    Beavo, J.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.