메뉴 건너뛰기




Volumn 274, Issue 2 43-2, 1998, Pages

ANF elicits phosphorylation of the cGMP phosphodiesterase in vascular smooth muscle cells

Author keywords

Cyclic nucleotides; Protein kinases; Protein phosphorylation; Smooth muscle relaxation

Indexed keywords

8 BROMO CYCLIC GMP; ADENOSINE TRIPHOSPHATE; ATRIAL NATRIURETIC FACTOR; CYCLIC AMP; CYCLIC GMP; CYCLIC GMP DEPENDENT PROTEIN KINASE; CYCLIC GMP PHOSPHODIESTERASE; PHOSPHORUS 32;

EID: 0031938315     PISSN: 03636135     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpheart.1998.274.2.h448     Document Type: Article
Times cited : (109)

References (38)
  • 1
    • 0019452847 scopus 로고
    • A specific substrate from rabbit cerebellum for guanosine 3′:5′-monophosphate-dependent protein kinase. I. Purification and characterization
    • Aswad, A. W., and P. Greengard. A specific substrate from rabbit cerebellum for guanosine 3′:5′-monophosphate-dependent protein kinase. I. Purification and characterization. J. Biol. Chem. 256: 3487-3493, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 3487-3493
    • Aswad, A.W.1    Greengard, P.2
  • 2
    • 0028136159 scopus 로고
    • Multiple cyclic nucleotide phosphodiesterases
    • Beavo, J. A., M. Conti, and R. J. Heaslip. Multiple cyclic nucleotide phosphodiesterases. Mol. Pharmacol. 46: 399-405, 1994.
    • (1994) Mol. Pharmacol. , vol.46 , pp. 399-405
    • Beavo, J.A.1    Conti, M.2    Heaslip, R.J.3
  • 3
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254, 1976.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 4
    • 0027099769 scopus 로고
    • Interaction of the catalytic subunit of protein kinase A with the lung type V cyclic GMP phosphodiesterase: Modulation of non-catalytic binding sites
    • Burns, F. M., and N. J. Pyne. Interaction of the catalytic subunit of protein kinase A with the lung type V cyclic GMP phosphodiesterase: modulation of non-catalytic binding sites. Biochem. Biophys. Res. Commun. 189: 1389-1396, 1992.
    • (1992) Biochem. Biophys. Res. Commun. , vol.189 , pp. 1389-1396
    • Burns, F.M.1    Pyne, N.J.2
  • 5
    • 0026661981 scopus 로고
    • Aphenylalanine in peptide substrates provides for selectivity between cGMP- and cAMP-dependent protein kinases
    • Colbran, J. L., S. H. Francis, A. B. Leach, M. K. Thomas, H. Jiang, L. M. McAllister, and J. D. Corbin. Aphenylalanine in peptide substrates provides for selectivity between cGMP- and cAMP-dependent protein kinases. J. Biol. Chem. 267: 9589-9594, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 9589-9594
    • Colbran, J.L.1    Francis, S.H.2    Leach, A.B.3    Thomas, M.K.4    Jiang, H.5    McAllister, L.M.6    Corbin, J.D.7
  • 6
    • 0022372522 scopus 로고
    • cAMP-dependent protein kinase activation lowers hepatocyte cAMP
    • Corbin, J. D., S. J. Beebe, and P. F. Blackmore. cAMP-dependent protein kinase activation lowers hepatocyte cAMP. J. Biol. Chem. 260: 8731-8735, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 8731-8735
    • Corbin, J.D.1    Beebe, S.J.2    Blackmore, P.F.3
  • 8
    • 0024476861 scopus 로고
    • 2+ levels in cultured vascular smooth muscle cells
    • 2+ levels in cultured vascular smooth muscle cells. J. Biol. Chem. 264: 1146-1155, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 1146-1155
    • Cornwell, T.L.1    Lincoln, T.M.2
  • 9
    • 0026319608 scopus 로고
    • Regulation of sarcoplasmic reticulum protein phosphorylation by localized cyclic GMP-dependent protein kinase in vascular smooth muscle cells
    • Cornwell, T. L., K. B. Pryzwansky, T. A. Wyatt, and T. M. Lincoln. Regulation of sarcoplasmic reticulum protein phosphorylation by localized cyclic GMP-dependent protein kinase in vascular smooth muscle cells. Mol. Pharmacol. 40: 923-931, 1991.
    • (1991) Mol. Pharmacol. , vol.40 , pp. 923-931
    • Cornwell, T.L.1    Pryzwansky, K.B.2    Wyatt, T.A.3    Lincoln, T.M.4
  • 10
    • 0027946487 scopus 로고
    • Regulation of the expression of cyclic GMP-dependent protein kinase by cell density in vascular smooth muscle cells
    • Cornwell, T. L., G. A. Soff, A. E. Traynor, and T. M. Lincoln. Regulation of the expression of cyclic GMP-dependent protein kinase by cell density in vascular smooth muscle cells. J. Vasc. Res. 31: 330-337, 1994.
    • (1994) J. Vasc. Res. , vol.31 , pp. 330-337
    • Cornwell, T.L.1    Soff, G.A.2    Traynor, A.E.3    Lincoln, T.M.4
  • 11
    • 0022261486 scopus 로고
    • Atriopeptin II elevates cyclic GMP, activates cyclic GMP-dependent protein kinase and causes relaxation in rat thoracic aorta
    • Fiscus, R. R., R. M. Rapoport, S. A. Waldman, and F. Murad. Atriopeptin II elevates cyclic GMP, activates cyclic GMP-dependent protein kinase and causes relaxation in rat thoracic aorta. Biochim. Biophys. Acta 846: 179-184, 1985.
    • (1985) Biochim. Biophys. Acta , vol.846 , pp. 179-184
    • Fiscus, R.R.1    Rapoport, R.M.2    Waldman, S.A.3    Murad, F.4
  • 12
    • 0023723086 scopus 로고
    • Purification of cGMP-binding protein phosphodiesterase from rat lung
    • Francis, S. H., and J. D. Corbin. Purification of cGMP-binding protein phosphodiesterase from rat lung. Methods Enzymol. 159: 722-729, 1988.
    • (1988) Methods Enzymol. , vol.159 , pp. 722-729
    • Francis, S.H.1    Corbin, J.D.2
  • 13
    • 0028186819 scopus 로고
    • Progress in understanding the mechanism and function of cyclic GMP-dependent protein kinase
    • edited by F. Murad. New York: Academic
    • Francis, S. H., and J. D. Corbin. Progress in understanding the mechanism and function of cyclic GMP-dependent protein kinase. In: Advances in Pharmacology. Cyclic GMP: Synthesis, Metabolism and Function, edited by F. Murad. New York: Academic, 1994, vol. 26, p. 115-170.
    • (1994) Advances in Pharmacology. Cyclic GMP: Synthesis, Metabolism and Function , vol.26 , pp. 115-170
    • Francis, S.H.1    Corbin, J.D.2
  • 14
    • 0018871466 scopus 로고
    • Characterization of a novel cGMP binding protein from rat lung
    • Francis, S. H., T. M. Lincoln, and J. D. Corbin. Characterization of a novel cGMP binding protein from rat lung. J. Biol. Chem. 255: 620-626, 1980.
    • (1980) J. Biol. Chem. , vol.255 , pp. 620-626
    • Francis, S.H.1    Lincoln, T.M.2    Corbin, J.D.3
  • 15
    • 0023803473 scopus 로고
    • Relaxation of vascular and tracheal smooth muscle by cyclic nucleotide analogs that preferentially activate purified cGMP-dependent protein kinase
    • Francis, S. H., B. D. Noblett, B. W. Todd, J. N. Wells, and J. D. Corbin. Relaxation of vascular and tracheal smooth muscle by cyclic nucleotide analogs that preferentially activate purified cGMP-dependent protein kinase. Mol. Pharmacol. 34: 506-517, 1988.
    • (1988) Mol. Pharmacol. , vol.34 , pp. 506-517
    • Francis, S.H.1    Noblett, B.D.2    Todd, B.W.3    Wells, J.N.4    Corbin, J.D.5
  • 17
    • 0025250142 scopus 로고
    • Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators
    • Halbrugge, M., L. Friedrich, M. Eigenthaler, P. Schanzenbecher, and U. Walter. Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators. J. Biol. Chem. 265: 3088-3093, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3088-3093
    • Halbrugge, M.1    Friedrich, L.2    Eigenthaler, M.3    Schanzenbecher, P.4    Walter, U.5
  • 18
    • 0020314909 scopus 로고
    • Endothelium-induced relaxation by acetylcholine associated with larger rises in cyclic GMP in coronary arterial strips
    • Holzmann, S. Endothelium-induced relaxation by acetylcholine associated with larger rises in cyclic GMP in coronary arterial strips. J. Cyclic Nucleotide Res. 8: 409-419, 1982.
    • (1982) J. Cyclic Nucleotide Res. , vol.8 , pp. 409-419
    • Holzmann, S.1
  • 19
    • 0029814390 scopus 로고    scopus 로고
    • Phosphorylation of the inositol 1,4,5-triphosphate receptor. Cyclic GMP-dependent protein kinase mediates cAMP and cGMP dependent phosphorylation in the intact rat aorta
    • Komalavilas, P., and T. M. Lincoln. Phosphorylation of the inositol 1,4,5-triphosphate receptor. Cyclic GMP-dependent protein kinase mediates cAMP and cGMP dependent phosphorylation in the intact rat aorta. J. Biol. Chem. 271: 21933-21938, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21933-21938
    • Komalavilas, P.1    Lincoln, T.M.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 277: 680-685, 1970.
    • (1970) Nature , vol.277 , pp. 680-685
    • Laemmli, U.K.1
  • 21
    • 0024599385 scopus 로고
    • Cyclic GMP and mechanisms of vasodilation
    • Lincoln, T. M. Cyclic GMP and mechanisms of vasodilation. Pharmacol. Ther. 41: 470-502, 1989.
    • (1989) Pharmacol. Ther. , vol.41 , pp. 470-502
    • Lincoln, T.M.1
  • 24
    • 0018078448 scopus 로고
    • Studies on the structure and mechanism of activation of the guanosine 3′,5′-monophosphate-dependent protein kinase
    • Lincoln, T. M., D. A. Flockhart, and J. D. Corbin. Studies on the structure and mechanism of activation of the guanosine 3′,5′-monophosphate-dependent protein kinase. J. Cell Biol. 253: 6002-6009, 1978.
    • (1978) J. Cell Biol. , vol.253 , pp. 6002-6009
    • Lincoln, T.M.1    Flockhart, D.A.2    Corbin, J.D.3
  • 25
  • 26
    • 0021305911 scopus 로고
    • Possible role of cyclic-GMP-dependent protein kinase in vascular smooth muscle function
    • Lincoln, T. M., and R. M. Johnson. Possible role of cyclic-GMP-dependent protein kinase in vascular smooth muscle function. Adv. Cyclic Nucleotide Res. 17: 285-296, 1984.
    • (1984) Adv. Cyclic Nucleotide Res. , vol.17 , pp. 285-296
    • Lincoln, T.M.1    Johnson, R.M.2
  • 27
    • 0022548645 scopus 로고
    • Selective inhibition of cyclic nucleotide phosphodiesterases of human, bovine, and rat aorta
    • Lugnier, C., P. Schoeffter, A. L. Bec, E. Strouthou, and J. C. Stoclet. Selective inhibition of cyclic nucleotide phosphodiesterases of human, bovine, and rat aorta. Biochem. Pharmacol. 35: 1743-1751, 1986.
    • (1986) Biochem. Pharmacol. , vol.35 , pp. 1743-1751
    • Lugnier, C.1    Schoeffter, P.2    Bec, A.L.3    Strouthou, E.4    Stoclet, J.C.5
  • 29
    • 0022481682 scopus 로고
    • Cyclic guanosine monophosphate as a mediator of vasodilation
    • Murad, F. Cyclic guanosine monophosphate as a mediator of vasodilation. J. Clin. Invest. 78: 1-5, 1986.
    • (1986) J. Clin. Invest. , vol.78 , pp. 1-5
    • Murad, F.1
  • 30
    • 0020643222 scopus 로고
    • Regulatory subunits of bovine heart and rabbit skeletal muscle cAMP-dependent protein kinase isozymes
    • Rannels, S. R., A. Beasley, and J. D. Corbin. Regulatory subunits of bovine heart and rabbit skeletal muscle cAMP-dependent protein kinase isozymes. Methods Enzymol. 99: 55-62, 1983.
    • (1983) Methods Enzymol. , vol.99 , pp. 55-62
    • Rannels, S.R.1    Beasley, A.2    Corbin, J.D.3
  • 31
    • 0020972355 scopus 로고
    • Assays of protein kinase
    • Roskoski, R. Assays of protein kinase. Methods Enzymol. 99: 3-6, 1983.
    • (1983) Methods Enzymol. , vol.99 , pp. 3-6
    • Roskoski, R.1
  • 32
    • 0027050098 scopus 로고
    • Relaxation of pig coronary arteries by new and potent cGMP analogs that selectively activate type Iα, compared with type Iβ, cGMP-dependent protein kinase
    • Sekhar, K. R., R. J. Hatchett, J. B. Shabb, L. Wolfe, S. H. Francis, J. N. Wells, B. Jastorff, E. Butt, M. M. Chakinala, and J. D, Corbin. Relaxation of pig coronary arteries by new and potent cGMP analogs that selectively activate type Iα, compared with type Iβ, cGMP-dependent protein kinase. Mol. Pharmacol. 42: 103-108, 1992.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 103-108
    • Sekhar, K.R.1    Hatchett, R.J.2    Shabb, J.B.3    Wolfe, L.4    Francis, S.H.5    Wells, J.N.6    Jastorff, B.7    Butt, E.8    Chakinala, M.M.9    Corbin, J.D.10
  • 33
    • 0028243837 scopus 로고
    • The short-term activation of a rolipram-sensitive, cAMP-specific phosphodiesterase by thyroid-stimulating hormone in thyroid FRTL-5 cells is mediated by a cAMP-dependent phosphorylation
    • Sette, C., S. Iona, and M. Conti. The short-term activation of a rolipram-sensitive, cAMP-specific phosphodiesterase by thyroid-stimulating hormone in thyroid FRTL-5 cells is mediated by a cAMP-dependent phosphorylation. J. Biol. Chem. 269: 9245-9252, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 9245-9252
    • Sette, C.1    Iona, S.2    Conti, M.3
  • 34
    • 0022881517 scopus 로고
    • A monoclonal antibody against alpha-smooth muscle actin: A new probe for smooth muscle differentiation
    • Skalli, O., P. Ropraz, A. Trzeciak, G. Benzonana, D. Gillessen, and G. Gabbiani. A monoclonal antibody against alpha-smooth muscle actin: a new probe for smooth muscle differentiation. J. Cell Biol. 103: 2787-2796, 1986.
    • (1986) J. Cell Biol. , vol.103 , pp. 2787-2796
    • Skalli, O.1    Ropraz, P.2    Trzeciak, A.3    Benzonana, G.4    Gillessen, D.5    Gabbiani, G.6
  • 35
    • 0020656983 scopus 로고
    • Analysis of angiotensin-stimulated sodium transport in cultured smooth muscle cells from rat aorta
    • Smith, J. B., and T. A. Brock. Analysis of angiotensin-stimulated sodium transport in cultured smooth muscle cells from rat aorta. J. Cell. Physiol. 114: 284-290, 1983.
    • (1983) J. Cell. Physiol. , vol.114 , pp. 284-290
    • Smith, J.B.1    Brock, T.A.2
  • 36
    • 0025041146 scopus 로고
    • Characterization of a purified bovine lung cGMP-binding cGMP phosphodiesterase
    • Thomas, M. K., S. H. Francis, and J. D. Corbin. Characterization of a purified bovine lung cGMP-binding cGMP phosphodiesterase. J. Biol. Chem. 265: 14964-14970, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14964-14970
    • Thomas, M.K.1    Francis, S.H.2    Corbin, J.D.3
  • 37
    • 0025143899 scopus 로고
    • Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP
    • Thomas, M. K., S. H. Francis, and J. D. Corbin. Substrate- and kinase-directed regulation of phosphorylation of a cGMP-binding phosphodiesterase by cGMP. J. Biol. Chem. 265: 14971-14978, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 14971-14978
    • Thomas, M.K.1    Francis, S.H.2    Corbin, J.D.3
  • 38
    • 0025833747 scopus 로고
    • Vimentin is transiently co-localized with and phosphorylated by cyclic GMP-dependent protein kinase in formyl-peptide stimulated neutrophils
    • Wyatt, T. A., T. M. Lincoln, and K. B. Pryzwansky. Vimentin is transiently co-localized with and phosphorylated by cyclic GMP-dependent protein kinase in formyl-peptide stimulated neutrophils. J. Biol. Chem. 266: 21274-21280, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21274-21280
    • Wyatt, T.A.1    Lincoln, T.M.2    Pryzwansky, K.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.