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Volumn 101, Issue 7, 2007, Pages 712-722

cGMP-dependent relaxation of smooth muscle is coupled with the change in the phosphorylation of myosin phosphatase

Author keywords

cGMP; Myosin light chain phosphatase; Phosphorylation; Smooth muscle; Vasodilation

Indexed keywords

CYCLIC GMP; MYOSIN LIGHT CHAIN KINASE INHIBITOR; MYOSIN LIGHT CHAIN PHOSPHATASE; PHENYLEPHRINE;

EID: 34848854240     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/CIRCRESAHA.107.153981     Document Type: Article
Times cited : (89)

References (28)
  • 1
    • 0019195506 scopus 로고
    • The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine
    • Furchgott RF, Zawadzki JV. The obligatory role of endothelial cells in the relaxation of arterial smooth muscle by acetylcholine. Nature. 1980;288:373-376.
    • (1980) Nature , vol.288 , pp. 373-376
    • Furchgott, R.F.1    Zawadzki, J.V.2
  • 2
    • 0034033975 scopus 로고    scopus 로고
    • Rising behind NO: CGMP-dependent protein kinases
    • Hofmann F, Ammendola A, Schlossmann J. Rising behind NO: cGMP-dependent protein kinases. J Cell Sci. 2000;113:1671-1676.
    • (2000) J Cell Sci , vol.113 , pp. 1671-1676
    • Hofmann, F.1    Ammendola, A.2    Schlossmann, J.3
  • 3
    • 0034862256 scopus 로고    scopus 로고
    • Invited review: CGMP-dependent protein kinase signaling mechanisms in smooth muscle: from the regulation of tone to gene expression
    • Lincoln TM, Dey N, Sellak H. Invited review: cGMP-dependent protein kinase signaling mechanisms in smooth muscle: from the regulation of tone to gene expression. J Appl Physiol. 2001;91:1421-1430.
    • (2001) J Appl Physiol , vol.91 , pp. 1421-1430
    • Lincoln, T.M.1    Dey, N.2    Sellak, H.3
  • 5
    • 0024550123 scopus 로고
    • Regulation of smooth muscle contractile elements by second messengers
    • Kamm KE, Stull JT. Regulation of smooth muscle contractile elements by second messengers. Ann Rev Physiol. 1989;51:299-313.
    • (1989) Ann Rev Physiol , vol.51 , pp. 299-313
    • Kamm, K.E.1    Stull, J.T.2
  • 6
    • 0028043535 scopus 로고
    • Signal transduction and regulation in smooth muscle
    • Somlyo AP, Somlyo AV. Signal transduction and regulation in smooth muscle. Nature. 1994;372:231-236.
    • (1994) Nature , vol.372 , pp. 231-236
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 7
    • 0028114606 scopus 로고
    • Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M
    • Chen YH, Chen MX, Alessi DR, Campbell DG, Shanahan C, Cohen P, Cohen PT. Molecular cloning of cDNA encoding the 110 kDa and 21 kDa regulatory subunits of smooth muscle protein phosphatase 1M. FEBS Lett. 1994;356:51-55.
    • (1994) FEBS Lett , vol.356 , pp. 51-55
    • Chen, Y.H.1    Chen, M.X.2    Alessi, D.R.3    Campbell, D.G.4    Shanahan, C.5    Cohen, P.6    Cohen, P.T.7
  • 9
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi D, MacDougall LK, Sola MM, Ikebe M, Cohen P. The control of protein phosphatase-1 by targetting subunits. The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur J Biochem. 1992;210:1023-1035.
    • (1992) Eur J Biochem , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.M.3    Ikebe, M.4    Cohen, P.5
  • 10
    • 0028152923 scopus 로고
    • Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle
    • Shirazi A, Iizuka K, Fadden P, Mosse C, Somlyo AP, Somlyo AV, Haystead TA. Purification and characterization of the mammalian myosin light chain phosphatase holoenzyme. The differential effects of the holoenzyme and its subunits on smooth muscle. J Biol Chem. 1994;269:31598-31606.
    • (1994) J Biol Chem , vol.269 , pp. 31598-31606
    • Shirazi, A.1    Iizuka, K.2    Fadden, P.3    Mosse, C.4    Somlyo, A.P.5    Somlyo, A.V.6    Haystead, T.A.7
  • 14
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase
    • Feng J, Ito M, Ichikawa K, Isaka N, Nishikawa M, Hartshorne DJ, Nakano T. Inhibitory phosphorylation site for Rho-associated kinase on smooth muscle myosin phosphatase. J Biol Chem. 1999;274:37385-37390.
    • (1999) J Biol Chem , vol.274 , pp. 37385-37390
    • Feng, J.1    Ito, M.2    Ichikawa, K.3    Isaka, N.4    Nishikawa, M.5    Hartshorne, D.J.6    Nakano, T.7
  • 15
    • 0030795828 scopus 로고    scopus 로고
    • Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: Its specific localization in smooth muscle
    • Eto M, Senba S, Morita F, Yazawa M. Molecular cloning of a novel phosphorylation-dependent inhibitory protein of protein phosphatase-1 (CPI17) in smooth muscle: its specific localization in smooth muscle. FEBS Lett. 1997;410:356-360.
    • (1997) FEBS Lett , vol.410 , pp. 356-360
    • Eto, M.1    Senba, S.2    Morita, F.3    Yazawa, M.4
  • 16
    • 0029583638 scopus 로고
    • A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization
    • Eto M, Ohmori T, Suzuki M, Furuya K, Morita F. A novel protein phosphatase-1 inhibitory protein potentiated by protein kinase C. Isolation from porcine aorta media and characterization. J Biochem. 1995;118:1104-1107.
    • (1995) J Biochem , vol.118 , pp. 1104-1107
    • Eto, M.1    Ohmori, T.2    Suzuki, M.3    Furuya, K.4    Morita, F.5
  • 17
    • 0034705765 scopus 로고    scopus 로고
    • Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase
    • Koyama M, Ito M, Feng J, Seko T, Shiraki K, Takase K, Hartshorne DJ, Nakano T. Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase. FEBS Lett. 2000;475:197-200.
    • (2000) FEBS Lett , vol.475 , pp. 197-200
    • Koyama, M.1    Ito, M.2    Feng, J.3    Seko, T.4    Shiraki, K.5    Takase, K.6    Hartshorne, D.J.7    Nakano, T.8
  • 18
    • 0021259446 scopus 로고
    • cGMP and cAMP inhibit tension development in skinned coronary arteries
    • Pfitzer G, Hofmann F, DiSalvo J, Ruegg JC. cGMP and cAMP inhibit tension development in skinned coronary arteries. Pflugers Arch. 1984;401:277-280.
    • (1984) Pflugers Arch , vol.401 , pp. 277-280
    • Pfitzer, G.1    Hofmann, F.2    DiSalvo, J.3    Ruegg, J.C.4
  • 19
    • 0029892621 scopus 로고    scopus 로고
    • Cyclic GMP-dependent stimulation reverses G-protein-coupled inhibition of smooth muscle myosin light chain phosphate
    • Wu X, Somlyo AV, Somlyo AP. Cyclic GMP-dependent stimulation reverses G-protein-coupled inhibition of smooth muscle myosin light chain phosphate. Biochem Boiphys Res Comm. 1996;220:658-663.
    • (1996) Biochem Boiphys Res Comm , vol.220 , pp. 658-663
    • Wu, X.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 20
    • 4544321243 scopus 로고    scopus 로고
    • Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides
    • Wooldridge AA, MacDonald JA, Erdodi F, Ma C, Borman MA, Hartshorne DJ, Haystead TA. Smooth muscle phosphatase is regulated in vivo by exclusion of phosphorylation of threonine 696 of MYPT1 by phosphorylation of Serine 695 in response to cyclic nucleotides. J Biol Chem. 2004;279:34496-34504.
    • (2004) J Biol Chem , vol.279 , pp. 34496-34504
    • Wooldridge, A.A.1    MacDonald, J.A.2    Erdodi, F.3    Ma, C.4    Borman, M.A.5    Hartshorne, D.J.6    Haystead, T.A.7
  • 21
    • 0037270157 scopus 로고    scopus 로고
    • Agonist-induced changes in the phosphorylation of the myosin- binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle
    • Niiro N, Koga Y, Ikebe M. Agonist-induced changes in the phosphorylation of the myosin- binding subunit of myosin light chain phosphatase and CPI17, two regulatory factors of myosin light chain phosphatase, in smooth muscle. Biochem J. 2003;369:117-128.
    • (2003) Biochem J , vol.369 , pp. 117-128
    • Niiro, N.1    Koga, Y.2    Ikebe, M.3
  • 23
    • 0031057516 scopus 로고    scopus 로고
    • Cyclic GMP causes Ca2+ desensitization in vascular smooth muscle by activating the myosin light chain phosphatase
    • Lee MR, Li L, Kitazawa T. Cyclic GMP causes Ca2+ desensitization in vascular smooth muscle by activating the myosin light chain phosphatase. J Biol Chem. 1997;272:5063-5068.
    • (1997) J Biol Chem , vol.272 , pp. 5063-5068
    • Lee, M.R.1    Li, L.2    Kitazawa, T.3
  • 24
    • 0036606183 scopus 로고    scopus 로고
    • Membrane depolarization-induced contraction of rat caudal arterial smooth muscle involves Rho-associated kinase
    • Mita M, Yanagihara H, Hishinuma S, Saito M, Walsh MP. Membrane depolarization-induced contraction of rat caudal arterial smooth muscle involves Rho-associated kinase. Biochem J. 2002;364:431-440.
    • (2002) Biochem J , vol.364 , pp. 431-440
    • Mita, M.1    Yanagihara, H.2    Hishinuma, S.3    Saito, M.4    Walsh, M.P.5
  • 25
    • 0141794500 scopus 로고    scopus 로고
    • Ca2+-dependent activation of Rho and Rho kinase in membrane depolarization- induced and receptor stimulation-induced vascular smooth muscle contraction
    • Sakurada S, Takuwa N, Sugimoto N, Wang Y, Seto M, Sasaki Y, Takuwa Y. Ca2+-dependent activation of Rho and Rho kinase in membrane depolarization- induced and receptor stimulation-induced vascular smooth muscle contraction. Circ Res. 2003;93:548-556.
    • (2003) Circ Res , vol.93 , pp. 548-556
    • Sakurada, S.1    Takuwa, N.2    Sugimoto, N.3    Wang, Y.4    Seto, M.5    Sasaki, Y.6    Takuwa, Y.7
  • 26
    • 0037322778 scopus 로고    scopus 로고
    • Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle
    • Kitazawa T, Eto M, Woodsome TP, Khalequzzaman M. Phosphorylation of the myosin phosphatase targeting subunit and CPI-17 during Ca2+ sensitization in rabbit smooth muscle. J Physiol. 2003;546:879-889.
    • (2003) J Physiol , vol.546 , pp. 879-889
    • Kitazawa, T.1    Eto, M.2    Woodsome, T.P.3    Khalequzzaman, M.4
  • 27
    • 3142675244 scopus 로고    scopus 로고
    • Actions downstream of cyclic GMP/protein kinase G can reverse protein kinase C-mediated phosphorylation of CPI-17 and Ca(2+) sensitization in smooth muscle
    • Bonnevier J, Arner A. Actions downstream of cyclic GMP/protein kinase G can reverse protein kinase C-mediated phosphorylation of CPI-17 and Ca(2+) sensitization in smooth muscle. J Biol Chem. 2004;279:28998-29003.
    • (2004) J Biol Chem , vol.279 , pp. 28998-29003
    • Bonnevier, J.1    Arner, A.2
  • 28
    • 0037063362 scopus 로고    scopus 로고
    • Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin
    • Velasco G, Armstrong C, Morrice N, Frame S, Cohen P. Phosphorylation of the regulatory subunit of smooth muscle protein phosphatase 1M at Thr850 induces its dissociation from myosin. FEBS Lett. 2002;527:101-104.
    • (2002) FEBS Lett , vol.527 , pp. 101-104
    • Velasco, G.1    Armstrong, C.2    Morrice, N.3    Frame, S.4    Cohen, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.