메뉴 건너뛰기




Volumn 95, Issue 6, 2004, Pages 612-618

Vascular reactivity in heart failure: Role of myosin light chain phosphatase

Author keywords

cGMP; Congestive heart failure; Nitric oxide; Vascular function

Indexed keywords

8 BROMO CYCLIC GMP; ISOENZYME; LEUCINE ZIPPER PROTEIN; MYOSIN LIGHT CHAIN KINASE; MYOSIN LIGHT CHAIN PHOSPHATASE; NITRIC OXIDE;

EID: 4644285523     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.0000142736.39359.58     Document Type: Article
Times cited : (42)

References (43)
  • 1
    • 0025038436 scopus 로고
    • Heart Failure: Mechanisms of cardiac and vascular dysfunction and the rationale for pharmacolgic intervention
    • Francis GS, Cohn JN. Heart Failure: Mechanisms of cardiac and vascular dysfunction and the rationale for pharmacolgic intervention. FASEB J. 1990;4:3068-3075.
    • (1990) FASEB J , vol.4 , pp. 3068-3075
    • Francis, G.S.1    Cohn, J.N.2
  • 3
    • 0035070413 scopus 로고    scopus 로고
    • Blunted peripheral vasodilatory response is a hallmark of progressive deterioration in mild to moderate congestive heart failure
    • Nakamura M, Arakawa N, Yoshida H, Saitoh S, Kon H, Hiramori K. Blunted peripheral vasodilatory response is a hallmark of progressive deterioration in mild to moderate congestive heart failure. J Card Fail. 2001;7:38-44.
    • (2001) J Card Fail , vol.7 , pp. 38-44
    • Nakamura, M.1    Arakawa, N.2    Yoshida, H.3    Saitoh, S.4    Kon, H.5    Hiramori, K.6
  • 5
    • 0033862993 scopus 로고    scopus 로고
    • Role of ET(A) receptors in the regulation of vascular reactivity in rats with congestive heart failure
    • Thorin E, Lucas M, Cernacek P, Dupuis J. Role of ET(A) receptors in the regulation of vascular reactivity in rats with congestive heart failure. Am J Physiol. 2000;279:H844-H851.
    • (2000) Am J Physiol , vol.279
    • Thorin, E.1    Lucas, M.2    Cernacek, P.3    Dupuis, J.4
  • 6
    • 0028093149 scopus 로고
    • Effects of L-arginine on impaired acetylcholine-induced and ischemic vasodilation of the forearm in patients with heart failure
    • Hirooka Y, Imaizumi T, Tagawa T, Shiramoto M, Endo T, Ando S, Takeshita A. Effects of L-arginine on impaired acetylcholine-induced and ischemic vasodilation of the forearm in patients with heart failure. Circulation. 1994;90:658-668.
    • (1994) Circulation , vol.90 , pp. 658-668
    • Hirooka, Y.1    Imaizumi, T.2    Tagawa, T.3    Shiramoto, M.4    Endo, T.5    Ando, S.6    Takeshita, A.7
  • 8
    • 0025951502 scopus 로고
    • Endothelium-dependent vasodilation is attenuated in patients with heart failure
    • Kubo SH, Rector TS, Bank AJ, Williams RE, Heifetz SM. Endothelium-dependent vasodilation is attenuated in patients with heart failure. Circulation. 1991;84:1589-1596.
    • (1991) Circulation , vol.84 , pp. 1589-1596
    • Kubo, S.H.1    Rector, T.S.2    Bank, A.J.3    Williams, R.E.4    Heifetz, S.M.5
  • 10
    • 0029739056 scopus 로고    scopus 로고
    • The management of chronic heart failure
    • Cohn JN. The management of chronic heart failure. N Engl J Med. 1996;335:490-498.
    • (1996) N Engl J Med , vol.335 , pp. 490-498
    • Cohn, J.N.1
  • 11
    • 0001068154 scopus 로고
    • Biochemistry of the contractile process in smooth muscle
    • Johnson LR, ed. New York, NY: Raven Press
    • Hartshorne DJ. Biochemistry of the contractile process in smooth muscle. In: Johnson LR, ed, Physiology of the Gastrointestinal Tract. New York, NY: Raven Press; 1987:432-482.
    • (1987) Physiology of the Gastrointestinal Tract , pp. 432-482
    • Hartshorne, D.J.1
  • 12
    • 0026692912 scopus 로고
    • Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle
    • Gong MC, Cohen P, Kitazawa T, Ikebe M, Masuo M, Somlyo AP, Somlyo AV. Myosin light chain phosphatase activities and the effects of phosphatase inhibitors in tonic and phasic smooth muscle. J Biol Chem. 1992;267:14662-14668.
    • (1992) J Biol Chem , vol.267 , pp. 14662-14668
    • Gong, M.C.1    Cohen, P.2    Kitazawa, T.3    Ikebe, M.4    Masuo, M.5    Somlyo, A.P.6    Somlyo, A.V.7
  • 13
    • 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
  • 14
    • 0026340753 scopus 로고
    • Molecular characterization of a mammalian smooth muscle myosin light chain kinase
    • Gallagher PJ, Herring BP, Griffin SA, Stull JT. Molecular characterization of a mammalian smooth muscle myosin light chain kinase. J Biol Chem. 1991;266:23936-23944.
    • (1991) J Biol Chem , vol.266 , pp. 23936-23944
    • Gallagher, P.J.1    Herring, B.P.2    Griffin, S.A.3    Stull, J.T.4
  • 15
    • 0141751697 scopus 로고    scopus 로고
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase
    • 2+ sensitivity of smooth muscle and nonmuscle myosin II: Modulated by G proteins, kinases, and myosin phosphatase. Physiol Rev. 2003;83:1325-1358.
    • (2003) Physiol Rev , vol.83 , pp. 1325-1358
    • Somlyo, A.P.1    Somlyo, A.V.2
  • 16
    • 0024599385 scopus 로고
    • Cyclic GMP and mechanisms of vasodilation
    • Lincoln TM. Cyclic GMP and mechanisms of vasodilation. Pharmacol Ther. 1989;41:479-502.
    • (1989) Pharmacol Ther , vol.41 , pp. 479-502
    • Lincoln, T.M.1
  • 17
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne DJ, Ito M, Erdîdi F. Myosin light chain phosphatase: subunit composition, interactions and regulation. J Mus Research Cell Motil. 1998;19:325-341.
    • (1998) J Mus Research Cell Motil , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdîdi, F.3
  • 18
    • 0034111688 scopus 로고    scopus 로고
    • A myosin phosphatase targeting subunit isoform transition defines a smooth muscle developmental phenotypic switch
    • Dirksen WP, Vladic F, Fisher SA. A myosin phosphatase targeting subunit isoform transition defines a smooth muscle developmental phenotypic switch. Am J Physiol. 2000;278:C589-C600.
    • (2000) Am J Physiol , vol.278
    • Dirksen, W.P.1    Vladic, F.2    Fisher, S.A.3
  • 19
    • 0035813193 scopus 로고    scopus 로고
    • Role of myosin phosphatase isoforms in cGMP-mediated smooth muscle relaxation
    • Khatri JJ, Joyce KM, Brozovich FV, Fisher SA. Role of myosin phosphatase isoforms in cGMP-mediated smooth muscle relaxation. J Biol Chem. 2001;276:37250-37257.
    • (2001) J Biol Chem , vol.276 , pp. 37250-37257
    • Khatri, J.J.1    Joyce, K.M.2    Brozovich, F.V.3    Fisher, S.A.4
  • 20
    • 0033635907 scopus 로고    scopus 로고
    • Determinants of the contractile properties in the embryonic chicken gizzard and aorta
    • Ogut O, Brozovich FV. Determinants of the contractile properties in the embryonic chicken gizzard and aorta. Am J Physiol. 2000;279:C1722-C1732.
    • (2000) Am J Physiol , vol.279
    • Ogut, O.1    Brozovich, F.V.2
  • 21
    • 0037040242 scopus 로고    scopus 로고
    • Agonist-induced force enhancement. The role of isoforms and phosphorylation of the mysoin-targeting subunit of mysoin light chain phosphatase
    • Richards CT, Ogut O, Brozovich FV. Agonist-induced force enhancement. The role of isoforms and phosphorylation of the mysoin-targeting subunit of mysoin light chain phosphatase. J Biol Chem. 2002; 277:4422-4427.
    • (2002) J Biol Chem , vol.277 , pp. 4422-4427
    • Richards, C.T.1    Ogut, O.2    Brozovich, F.V.3
  • 22
    • 0032718519 scopus 로고    scopus 로고
    • Endothelium-derived relaxing factor: Discovery, early studies, and identification as nitric oxide
    • Furchgott RF. Endothelium-derived relaxing factor: discovery, early studies, and identification as nitric oxide. Biosci Rep. 1999;19:235-251.
    • (1999) Biosci Rep , vol.19 , pp. 235-251
    • Furchgott, R.F.1
  • 23
    • 0032484126 scopus 로고    scopus 로고
    • The large conductance, voltage-dependent, and calcium-sensitive K+ channel, Hslo, is a target of cGMP-dependent protein kinase phosphorylation in vivo
    • Alioua A, Tanaka Y, Wallner M, Hofmann F, Ruth P, Meera P, Toro L. The large conductance, voltage-dependent, and calcium-sensitive K+ channel, Hslo, is a target of cGMP-dependent protein kinase phosphorylation in vivo. J Biol Chem. 1998;273:32950-32956.
    • (1998) J Biol Chem , vol.273 , pp. 32950-32956
    • Alioua, A.1    Tanaka, Y.2    Wallner, M.3    Hofmann, F.4    Ruth, P.5    Meera, P.6    Toro, L.7
  • 24
    • 0027284439 scopus 로고
    • The nitric oxide and cGMP signal transduction system: Regulation and mechanism of action
    • Schmidt HH, Lohmann SM, Walter U. The nitric oxide and cGMP signal transduction system: Regulation and mechanism of action. Biochim Biophys Acta. 1993;1178:153-175.
    • (1993) Biochim Biophys Acta , vol.1178 , pp. 153-175
    • Schmidt, H.H.1    Lohmann, S.M.2    Walter, U.3
  • 25
    • 0033574411 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinase activates cloned BKCa channels expressed in mammalian cells by direct phosphorylation at serine 1072
    • Fukao M, Mason HS, Britton FC, Kenyon JL, Horowitz B, Keef KD. Cyclic GMP-dependent protein kinase activates cloned BKCa channels expressed in mammalian cells by direct phosphorylation at serine 1072. J Biol Chem. 1999;274:10927-10935.
    • (1999) J Biol Chem , vol.274 , pp. 10927-10935
    • Fukao, M.1    Mason, H.S.2    Britton, F.C.3    Kenyon, J.L.4    Horowitz, B.5    Keef, K.D.6
  • 27
    • 0346422448 scopus 로고    scopus 로고
    • Unzipping the role of myosin light chain phosphatase in smooth muscle cell relaxation
    • Huang QQ, Fisher SA, Brozovich FV. Unzipping the role of myosin light chain phosphatase in smooth muscle cell relaxation. J Biol Chem. 2004; 279:597-603.
    • (2004) J Biol Chem , vol.279 , pp. 597-603
    • Huang, Q.Q.1    Fisher, S.A.2    Brozovich, F.V.3
  • 28
    • 0024565176 scopus 로고
    • Regional variation in rat cardiac myosin isoenzymes and ATPase activity after infarction
    • Geenen DL, Malhotra A, Scheuer J. Regional variation in rat cardiac myosin isoenzymes and ATPase activity after infarction. Am J Physiol. 1989;256:H745-H750.
    • (1989) Am J Physiol , vol.256
    • Geenen, D.L.1    Malhotra, A.2    Scheuer, J.3
  • 29
    • 85047679815 scopus 로고
    • Ventricular function and contractile proteins in the infarcted overloaded rat heart
    • Geenen DL, Malhotra A, Liang D, Scheuer J. Ventricular function and contractile proteins in the infarcted overloaded rat heart. Cardiovasc Res. 1991;25:330-336.
    • (1991) Cardiovasc Res , vol.25 , pp. 330-336
    • Geenen, D.L.1    Malhotra, A.2    Liang, D.3    Scheuer, J.4
  • 30
    • 0030771274 scopus 로고    scopus 로고
    • Changes in skeletal muscle biochemistry and histology relative to fiber type in rats with heart failure
    • Delp MD, Duan C, Mattson JP, Musch TI. Changes in skeletal muscle biochemistry and histology relative to fiber type in rats with heart failure. J Appl Physiol. 1997;83:1291-1299.
    • (1997) J Appl Physiol , vol.83 , pp. 1291-1299
    • Delp, M.D.1    Duan, C.2    Mattson, J.P.3    Musch, T.I.4
  • 31
    • 0032819320 scopus 로고    scopus 로고
    • Interactions between angiotensin II and nitric oxide during exercise in normal and heart failure rats
    • Symons JD, Stebbins CL, Musch TI. Interactions between angiotensin II and nitric oxide during exercise in normal and heart failure rats. J Appl Physiol. 1999;87:574-581.
    • (1999) J Appl Physiol , vol.87 , pp. 574-581
    • Symons, J.D.1    Stebbins, C.L.2    Musch, T.I.3
  • 32
    • 0033385458 scopus 로고    scopus 로고
    • Noninvasive evaluation of cardiac dysfunction by echocardiography in streptozotocin-induced diabetic rats
    • Hoit BD, Castro C, Bultron G, Knight S, Matlib MA. Noninvasive evaluation of cardiac dysfunction by echocardiography in streptozotocin-induced diabetic rats. J Card Fail. 1999;5:324-333.
    • (1999) J Card Fail , vol.5 , pp. 324-333
    • Hoit, B.D.1    Castro, C.2    Bultron, G.3    Knight, S.4    Matlib, M.A.5
  • 33
    • 0033857582 scopus 로고    scopus 로고
    • The smooth muscle cross-bridge cycle studied using sinusoidal length perturbations
    • Rhee AY, Brozovich FV. The smooth muscle cross-bridge cycle studied using sinusoidal length perturbations. Biophys J. 2000;79:1511-1523.
    • (2000) Biophys J , vol.79 , pp. 1511-1523
    • Rhee, A.Y.1    Brozovich, F.V.2
  • 34
    • 0037335687 scopus 로고    scopus 로고
    • The smooth muscle myosin seven amino acid heavy chain insert's kinetic role in the crossbridge cycle for mouse bladder
    • Karagiannis P, Babu GJ, Periasamy M, Brozovich FV. The smooth muscle myosin seven amino acid heavy chain insert's kinetic role in the crossbridge cycle for mouse bladder. J Physiol. 2003;547:463-473.
    • (2003) J Physiol , vol.547 , pp. 463-473
    • Karagiannis, P.1    Babu, G.J.2    Periasamy, M.3    Brozovich, F.V.4
  • 35
    • 0030980825 scopus 로고    scopus 로고
    • Endothelin-1 alters the contractile phenotype of cultured embryonic smooth muscle cells
    • Fisher SA, Ikebe M, Brozovich F. Endothelin-1 alters the contractile phenotype of cultured embryonic smooth muscle cells. Circ Res. 1997; 80:885-893.
    • (1997) Circ Res , vol.80 , pp. 885-893
    • Fisher, S.A.1    Ikebe, M.2    Brozovich, F.3
  • 36
    • 0033521035 scopus 로고    scopus 로고
    • Forced expression of essential myosin light chain isoforms demonstrates their role in smooth muscle force production
    • Huang QQ, Fisher SA, Brozovich FV. Forced expression of essential myosin light chain isoforms demonstrates their role in smooth muscle force production. J Biol Chem. 1999;274:35095-35098.
    • (1999) J Biol Chem , vol.274 , pp. 35095-35098
    • Huang, Q.Q.1    Fisher, S.A.2    Brozovich, F.V.3
  • 37
    • 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
  • 38
    • 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
  • 39
    • 0026438790 scopus 로고
    • Heterogeneous distribution of endothelium-dependent relaxations resistant to NG-nitro-L-arginine in rats
    • Nagao T, Illiano S, Vanhoutte PM. Heterogeneous distribution of endothelium-dependent relaxations resistant to NG-nitro-L-arginine in rats. Am J Physiol. 1992;263:H1090-H1094.
    • (1992) Am J Physiol , vol.263
    • Nagao, T.1    Illiano, S.2    Vanhoutte, P.M.3
  • 40
    • 0022553832 scopus 로고
    • Cyclic GMP-dependent protein kinase relaxes skinned fibers from guinea pig taenia coli but not from chicken gizzard
    • Pfitzer G, Merkel L, Ruegg JC, Hofmann F. Cyclic GMP-dependent protein kinase relaxes skinned fibers from guinea pig taenia coli but not from chicken gizzard. Pflugers Arch. 1986;407:87-91.
    • (1986) Pflugers Arch , vol.407 , pp. 87-91
    • Pfitzer, G.1    Merkel, L.2    Ruegg, J.C.3    Hofmann, F.4
  • 41
    • 0038447042 scopus 로고    scopus 로고
    • Dimerization of cGMP-dependent protein kinase 1α and the myosin-binding subunit of myosin phosphatase: Role of leucine zipper domains
    • Surks HK, Mendelsohn ME. Dimerization of cGMP-dependent protein kinase 1α and the myosin-binding subunit of myosin phosphatase: role of leucine zipper domains. Cell Signal. 2003;15:937-944.
    • (2003) Cell Signal , vol.15 , pp. 937-944
    • Surks, H.K.1    Mendelsohn, M.E.2
  • 43
    • 0035823538 scopus 로고    scopus 로고
    • Recombinant small subunit of smooth muscle myosin light chain phosphatase. Molecular properties and interactions with the targeting subunit
    • Langsetmo K, Stafford WF III, Mabuchi K, Tao T. Recombinant small subunit of smooth muscle myosin light chain phosphatase. Molecular properties and interactions with the targeting subunit. J Biol Chem. 2001;276:34318-34322.
    • (2001) J Biol Chem , vol.276 , pp. 34318-34322
    • Langsetmo, K.1    Stafford III, W.F.2    Mabuchi, K.3    Tao, T.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.