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Volumn 8, Issue 10, 2010, Pages 2283-2293

Differential phosphorylation of myosin light chain (Thr)18 and (Ser)19 and functional implications in platelets

Author keywords

Cytoskeletal rearrangements; Myosin; Platelets; Protease activated receptors; Secretion; Shape change

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ADENOSINE TRIPHOSPHATE; CALCIUM ION; MYOSIN LIGHT CHAIN; RHO KINASE; SERINE; THREONINE;

EID: 78649337010     PISSN: 15387933     EISSN: 15387836     Source Type: Journal    
DOI: 10.1111/j.1538-7836.2010.04000.x     Document Type: Article
Times cited : (44)

References (50)
  • 1
    • 0028302211 scopus 로고
    • Role of platelets in thrombosis and hemostasis
    • Packham MA. Role of platelets in thrombosis and hemostasis. Can J Physiol Pharmacol 1994; 72: 278-84.
    • (1994) Can J Physiol Pharmacol , vol.72 , pp. 278-284
    • Packham, M.A.1
  • 2
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: the platelet paradigm
    • Shattil SJ, Kashiwagi H, Pampori N. Integrin signaling: the platelet paradigm. Blood 1998; 91: 2645-57.
    • (1998) Blood , vol.91 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 3
    • 0025952271 scopus 로고
    • Pharmacological receptors on blood platelets
    • Hourani SM, Cusack NJ. Pharmacological receptors on blood platelets. Pharmacol Rev 1991; 43: 243-98.
    • (1991) Pharmacol Rev , vol.43 , pp. 243-298
    • Hourani, S.M.1    Cusack, N.J.2
  • 4
    • 0030470605 scopus 로고    scopus 로고
    • ADP receptors on platelets
    • Mills DC. ADP receptors on platelets. Thromb Haemost 1996; 76:835-56.
    • (1996) Thromb Haemost , vol.76 , pp. 835-856
    • Mills, D.C.1
  • 5
    • 0031041906 scopus 로고    scopus 로고
    • Thrombin receptors on human platelets initial localization and subsequent redistribution during platelet activation
    • Molino M, Bainton DF, Hoxie JA, Coughlin SR, Brass LF. Thrombin receptors on human platelets initial localization and subsequent redistribution during platelet activation. J Biol Chem 1997; 272: 6011-7.
    • (1997) J Biol Chem , vol.272 , pp. 6011-6017
    • Molino, M.1    Bainton, D.F.2    Hoxie, J.A.3    Coughlin, S.R.4    Brass, L.F.5
  • 6
    • 0033369594 scopus 로고    scopus 로고
    • More pieces of the platelet activation puzzle slide into place
    • Brass LF. More pieces of the platelet activation puzzle slide into place. J Clin Invest 1999; 104: 1663-5.
    • (1999) J Clin Invest , vol.104 , pp. 1663-1665
    • Brass, L.F.1
  • 7
    • 0033613183 scopus 로고    scopus 로고
    • How the protease thrombin talks to cells
    • Coughlin SR. How the protease thrombin talks to cells. Proc Natl Acad Sci U S A 1999; 96: 11023-7.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 11023-11027
    • Coughlin, S.R.1
  • 8
    • 0034921205 scopus 로고    scopus 로고
    • Protease-activated receptors in vascular biology
    • Coughlin SR. Protease-activated receptors in vascular biology. Thromb Haemost 2001; 86: 298-307.
    • (2001) Thromb Haemost , vol.86 , pp. 298-307
    • Coughlin, S.R.1
  • 9
    • 0021200684 scopus 로고
    • Evidence for a role of myosin phosphorylation in the initiation of the platelet shape change response
    • Daniel JL, Molish IR, Rigmaiden M, Stewart G. Evidence for a role of myosin phosphorylation in the initiation of the platelet shape change response. J Biol Chem 1984; 259: 9826-31.
    • (1984) J Biol Chem , vol.259 , pp. 9826-9831
    • Daniel, J.L.1    Molish, I.R.2    Rigmaiden, M.3    Stewart, G.4
  • 10
    • 0024532116 scopus 로고
    • Molecular mechanisms of platelet activation
    • Siess W. Molecular mechanisms of platelet activation. Physiol Rev 1989; 69: 58-178.
    • (1989) Physiol Rev , vol.69 , pp. 58-178
    • Siess, W.1
  • 11
    • 0027709195 scopus 로고
    • Regulation of platelet function by the cytoskeleton
    • Fox JE. Regulation of platelet function by the cytoskeleton. Adv Exp Med Biol 1993; 344: 175-85.
    • (1993) Adv Exp Med Biol , vol.344 , pp. 175-185
    • Fox, J.E.1
  • 12
    • 0020465177 scopus 로고
    • Calmodulin and the regulation of the actin-myosin interaction in smooth muscle and nonmuscle cells
    • Adelstein RS. Calmodulin and the regulation of the actin-myosin interaction in smooth muscle and nonmuscle cells. Cell 1982; 30:349-50.
    • (1982) Cell , vol.30 , pp. 349-350
    • Adelstein, R.S.1
  • 13
    • 0023927958 scopus 로고
    • Effects of phosphorylation of light chain residues threonine 18 and serine 19 on the properties and conformation of smooth muscle myosin
    • Ikebe M, Koretz J, Hartshorne DJ. Effects of phosphorylation of light chain residues threonine 18 and serine 19 on the properties and conformation of smooth muscle myosin. J Biol Chem 1988; 263: 6432-7.
    • (1988) J Biol Chem , vol.263 , pp. 6432-6437
    • Ikebe, M.1    Koretz, J.2    Hartshorne, D.J.3
  • 14
    • 0026592482 scopus 로고
    • Diphosphorylation of platelet myosin by myosin light chain kinase
    • Itoh K, Hara T, Shibata N. Diphosphorylation of platelet myosin by myosin light chain kinase. Biochim Biophys Acta 1992; 1133: 286-92.
    • (1992) Biochim Biophys Acta , vol.1133 , pp. 286-292
    • Itoh, K.1    Hara, T.2    Shibata, N.3
  • 15
    • 0024455475 scopus 로고
    • Phosphorylation of a second site for myosin light chain kinase on platelet myosin
    • Ikebe M. Phosphorylation of a second site for myosin light chain kinase on platelet myosin. Biochemistry 1989; 28: 8750-5.
    • (1989) Biochemistry , vol.28 , pp. 8750-8755
    • Ikebe, M.1
  • 16
    • 0033562781 scopus 로고    scopus 로고
    • Agonist-induced regulation of myosin phosphatase activity in human platelets through activation of Rho-kinase
    • Suzuki Y, Yamamoto M, Wada H, Ito M, Nakano T, Sasaki Y, Narumiya S, Shiku H, Nishikawa M. Agonist-induced regulation of myosin phosphatase activity in human platelets through activation of Rho-kinase. Blood 1999; 93: 3408-17.
    • (1999) Blood , vol.93 , pp. 3408-3417
    • Suzuki, Y.1    Yamamoto, M.2    Wada, H.3    Ito, M.4    Nakano, T.5    Sasaki, Y.6    Narumiya, S.7    Shiku, H.8    Nishikawa, M.9
  • 17
    • 0022410257 scopus 로고
    • Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase
    • Ikebe M, Hartshorne DJ. Phosphorylation of smooth muscle myosin at two distinct sites by myosin light chain kinase. J Biol Chem 1985; 260: 10027-31.
    • (1985) J Biol Chem , vol.260 , pp. 10027-10031
    • Ikebe, M.1    Hartshorne, D.J.2
  • 18
    • 0036646489 scopus 로고    scopus 로고
    • Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton
    • Kiss E, Muranyi A, Csortos C, Gergely P, Ito M, Hartshorne DJ, Erdodi F. Integrin-linked kinase phosphorylates the myosin phosphatase target subunit at the inhibitory site in platelet cytoskeleton. Biochem J 2002; 365: 79-87.
    • (2002) Biochem J , vol.365 , pp. 79-87
    • Kiss, E.1    Muranyi, A.2    Csortos, C.3    Gergely, P.4    Ito, M.5    Hartshorne, D.J.6    Erdodi, F.7
  • 19
    • 0033214045 scopus 로고    scopus 로고
    • Platelet shape change is mediated by both calcium-dependent and -independent signaling pathways Role of p160 Rho-associated coiled-coil-containing protein kinase in platelet shape change
    • Paul BZ, Daniel JL, Kunapuli SP. Platelet shape change is mediated by both calcium-dependent and -independent signaling pathways Role of p160 Rho-associated coiled-coil-containing protein kinase in platelet shape change. J Biol Chem 1999; 274: 28293-300.
    • (1999) J Biol Chem , vol.274 , pp. 28293-28300
    • Paul, B.Z.1    Daniel, J.L.2    Kunapuli, S.P.3
  • 22
    • 31544455817 scopus 로고    scopus 로고
    • Relative contribution of G-protein-coupled pathways to protease-activated receptor-mediated Akt phosphorylation in platelets
    • Kim S, Jin J, Kunapuli SP. Relative contribution of G-protein-coupled pathways to protease-activated receptor-mediated Akt phosphorylation in platelets. Blood 2006; 107: 947-54.
    • (2006) Blood , vol.107 , pp. 947-954
    • Kim, S.1    Jin, J.2    Kunapuli, S.P.3
  • 25
    • 59749100019 scopus 로고    scopus 로고
    • RhoA downstream of G(q) and G(12/13) pathways regulates protease-activated receptor-mediated dense granule release in platelets
    • Jin J, Mao Y, Thomas D, Kim S, Daniel JL, Kunapuli SP. RhoA downstream of G(q) and G(12/13) pathways regulates protease-activated receptor-mediated dense granule release in platelets. Biochem Pharmacol 2009; 77: 835-44.
    • (2009) Biochem Pharmacol , vol.77 , pp. 835-844
    • Jin, J.1    Mao, Y.2    Thomas, D.3    Kim, S.4    Daniel, J.L.5    Kunapuli, S.P.6
  • 26
    • 0030953664 scopus 로고    scopus 로고
    • Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor
    • Polgar J, Clemetson JM, Kehrel BE, Wiedemann M, Magnenat EM, Wells TN, Clemetson KJ. Platelet activation and signal transduction by convulxin, a C-type lectin from Crotalus durissus terrificus (tropical rattlesnake) venom via the p62/GPVI collagen receptor. J Biol Chem 1997; 272: 13576-83.
    • (1997) J Biol Chem , vol.272 , pp. 13576-13583
    • Polgar, J.1    Clemetson, J.M.2    Kehrel, B.E.3    Wiedemann, M.4    Magnenat, E.M.5    Wells, T.N.6    Clemetson, K.J.7
  • 27
    • 0028212628 scopus 로고
    • Collagen induces normal signal transduction in platelets deficient in CD36 (platelet glycoprotein IV)
    • Daniel JL, Dangelmaier C, Strouse R, Smith JB. Collagen induces normal signal transduction in platelets deficient in CD36 (platelet glycoprotein IV). Thromb Haemost 1994; 71: 353-6.
    • (1994) Thromb Haemost , vol.71 , pp. 353-356
    • Daniel, J.L.1    Dangelmaier, C.2    Strouse, R.3    Smith, J.B.4
  • 28
    • 0029935373 scopus 로고    scopus 로고
    • Changes in cytosolic calcium concentrations and cell morphology in single platelets adhered to fibrinogen-coated surface under flow
    • Jen CJ, Chen HI, Lai KC, Usami S. Changes in cytosolic calcium concentrations and cell morphology in single platelets adhered to fibrinogen-coated surface under flow. Blood 1996; 87: 3775-82.
    • (1996) Blood , vol.87 , pp. 3775-3782
    • Jen, C.J.1    Chen, H.I.2    Lai, K.C.3    Usami, S.4
  • 29
    • 0035930528 scopus 로고    scopus 로고
    • Differential regulation of Rho and Rac through heterotrimeric G-proteins and cyclic nucleotides
    • Gratacap MP, Payrastre B, Nieswandt B, Offermanns S. Differential regulation of Rho and Rac through heterotrimeric G-proteins and cyclic nucleotides. J Biol Chem 2001; 276: 47906-13.
    • (2001) J Biol Chem , vol.276 , pp. 47906-47913
    • Gratacap, M.P.1    Payrastre, B.2    Nieswandt, B.3    Offermanns, S.4
  • 30
    • 8544239414 scopus 로고    scopus 로고
    • Unresponsiveness of platelets lacking both Galpha(q) and Galpha(13). Implications for collagen-induced platelet activation
    • Moers A, Wettschureck N, Gruner S, Nieswandt B, Offermanns S. Unresponsiveness of platelets lacking both Galpha(q) and Galpha(13). Implications for collagen-induced platelet activation. J Biol Chem 2004; 279: 45354-9.
    • (2004) J Biol Chem , vol.279 , pp. 45354-45359
    • Moers, A.1    Wettschureck, N.2    Gruner, S.3    Nieswandt, B.4    Offermanns, S.5
  • 32
    • 0033199252 scopus 로고    scopus 로고
    • Dichotomous regulation of myosin phosphorylation and shape change by Rho-kinase and calcium in intact human platelets
    • Bauer M, Retzer M, Wilde JI, Maschberger P, Essler M, Aepfelbacher M, Watson SP, Siess W. Dichotomous regulation of myosin phosphorylation and shape change by Rho-kinase and calcium in intact human platelets. Blood 1999; 94: 1665-72.
    • (1999) Blood , vol.94 , pp. 1665-1672
    • Bauer, M.1    Retzer, M.2    Wilde, J.I.3    Maschberger, P.4    Essler, M.5    Aepfelbacher, M.6    Watson, S.P.7    Siess, W.8
  • 33
    • 0037032558 scopus 로고    scopus 로고
    • Coordinated signaling through both G12/13 and G(i) pathways is sufficient to activate GPIIb/IIIa in human platelets
    • Dorsam RT, Kim S, Jin J, Kunapuli SP. Coordinated signaling through both G12/13 and G(i) pathways is sufficient to activate GPIIb/IIIa in human platelets. J Biol Chem 2002; 277: 47588-95.
    • (2002) J Biol Chem , vol.277 , pp. 47588-47595
    • Dorsam, R.T.1    Kim, S.2    Jin, J.3    Kunapuli, S.P.4
  • 34
    • 0017759643 scopus 로고
    • Thrombin-stimulated myosin phosphorylation in intact platelets and its possible involvement secretion
    • Daniel JL, Holmsen H, Adelstein RS. Thrombin-stimulated myosin phosphorylation in intact platelets and its possible involvement secretion. Thromb Haemost 1977; 38: 984-9.
    • (1977) Thromb Haemost , vol.38 , pp. 984-989
    • Daniel, J.L.1    Holmsen, H.2    Adelstein, R.S.3
  • 35
    • 0017393127 scopus 로고
    • Relationship between phosphorylation of blood platelet proteins and secretion of platelet granule constituents. I. Effects of different aggregating agents
    • Haslam RJ, Lynham JA. Relationship between phosphorylation of blood platelet proteins and secretion of platelet granule constituents. I. Effects of different aggregating agents. Biochem Biophys Res Commun 1977; 77: 714-22.
    • (1977) Biochem Biophys Res Commun , vol.77 , pp. 714-722
    • Haslam, R.J.1    Lynham, J.A.2
  • 36
    • 0018629545 scopus 로고
    • A study of protein phosphorylation in shape change and Ca++-dependent serotonin release by blood platelets
    • Bennett WF, Belville JS, Lynch G. A study of protein phosphorylation in shape change and Ca++-dependent serotonin release by blood platelets. Cell 1979; 18: 1015-23.
    • (1979) Cell , vol.18 , pp. 1015-1023
    • Bennett, W.F.1    Belville, J.S.2    Lynch, G.3
  • 37
    • 0014829125 scopus 로고
    • An electrophoretic study of the low-molecular-weight components of myosin
    • Perrie WT, Perry SV. An electrophoretic study of the low-molecular-weight components of myosin. Biochem J 1970; 119: 31-8.
    • (1970) Biochem J , vol.119 , pp. 31-38
    • Perrie, W.T.1    Perry, S.V.2
  • 38
    • 0032828089 scopus 로고    scopus 로고
    • Molecular mechanism of thromboxane A(2)-induced platelet aggregation. Essential role for p2t(ac) and alpha(2a) receptors
    • Paul BZ, Jin J, Kunapuli SP. Molecular mechanism of thromboxane A(2)-induced platelet aggregation. Essential role for p2t(ac) and alpha(2a) receptors. J Biol Chem 1999; 274: 29108-14.
    • (1999) J Biol Chem , vol.274 , pp. 29108-29114
    • Paul, B.Z.1    Jin, J.2    Kunapuli, S.P.3
  • 39
    • 0037092952 scopus 로고    scopus 로고
    • Protease-activated receptors 1 and 4 do not stimulate G(i) signaling pathways in the absence of secreted ADP and cause human platelet aggregation independently of G(i) signaling
    • Kim S, Foster C, Lecchi A, Quinton TM, Prosser DM, Jin J, Cattaneo M, Kunapuli SP. Protease-activated receptors 1 and 4 do not stimulate G(i) signaling pathways in the absence of secreted ADP and cause human platelet aggregation independently of G(i) signaling. Blood 2002; 99: 3629-36.
    • (2002) Blood , vol.99 , pp. 3629-3636
    • Kim, S.1    Foster, C.2    Lecchi, A.3    Quinton, T.M.4    Prosser, D.M.5    Jin, J.6    Cattaneo, M.7    Kunapuli, S.P.8
  • 40
    • 0022650773 scopus 로고
    • Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,000-dalton light chain of smooth muscle myosin
    • Ikebe M, Hartshorne DJ, Elzinga M. Identification, phosphorylation, and dephosphorylation of a second site for myosin light chain kinase on the 20,000-dalton light chain of smooth muscle myosin. J Biol Chem 1986; 261: 36-9.
    • (1986) J Biol Chem , vol.261 , pp. 36-39
    • Ikebe, M.1    Hartshorne, D.J.2    Elzinga, M.3
  • 41
    • 0032493295 scopus 로고    scopus 로고
    • Coactivation of two different G protein-coupled receptors is essential for ADP-induced platelet aggregation
    • Jin J, Kunapuli SP. Coactivation of two different G protein-coupled receptors is essential for ADP-induced platelet aggregation. Proc Natl Acad Sci U S A 1998; 95: 8070-4.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8070-8074
    • Jin, J.1    Kunapuli, S.P.2
  • 42
    • 0030756508 scopus 로고    scopus 로고
    • Defective platelet activation in G alpha(q)-deficient mice
    • Offermanns S, Toombs CF, Hu YH, Simon MI. Defective platelet activation in G alpha(q)-deficient mice. Nature 1997; 389: 183-6.
    • (1997) Nature , vol.389 , pp. 183-186
    • Offermanns, S.1    Toombs, C.F.2    Hu, Y.H.3    Simon, M.I.4
  • 43
    • 0031916728 scopus 로고    scopus 로고
    • Molecular basis for ADP-induced platelet activation. II. The P2Y1 receptor mediates ADP-induced intracellular calcium mobilization and shape change in platelets
    • Jin J, Daniel JL, Kunapuli SP. Molecular basis for ADP-induced platelet activation. II. The P2Y1 receptor mediates ADP-induced intracellular calcium mobilization and shape change in platelets. J Biol Chem 1998; 273: 2030-4.
    • (1998) J Biol Chem , vol.273 , pp. 2030-2034
    • Jin, J.1    Daniel, J.L.2    Kunapuli, S.P.3
  • 44
    • 0032826036 scopus 로고    scopus 로고
    • Decreased platelet aggregation, increased bleeding time and resistance to thromboembolism in P2Y1-deficient mice
    • Fabre JE, Nguyen M, Latour A, Keifer JA, Audoly LP, Coffman TM, Koller BH. Decreased platelet aggregation, increased bleeding time and resistance to thromboembolism in P2Y1-deficient mice. Nat Med 1999; 5: 1199-202.
    • (1999) Nat Med , vol.5 , pp. 1199-1202
    • Fabre, J.E.1    Nguyen, M.2    Latour, A.3    Keifer, J.A.4    Audoly, L.P.5    Coffman, T.M.6    Koller, B.H.7
  • 46
    • 0001093453 scopus 로고
    • Secretion from rat basophilic RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C
    • Choi OH, Adelstein RS, Beaven MA. Secretion from rat basophilic RBL-2H3 cells is associated with diphosphorylation of myosin light chains by myosin light chain kinase as well as phosphorylation by protein kinase C. J Biol Chem 1994; 269: 536-41.
    • (1994) J Biol Chem , vol.269 , pp. 536-541
    • Choi, O.H.1    Adelstein, R.S.2    Beaven, M.A.3
  • 47
    • 0029029077 scopus 로고
    • Desensitization and resensitization of human platelets to 5-hydroxytryptamine at the level of signal transduction
    • Roevens P, de Chaffoy de Courcelles D. Desensitization and resensitization of human platelets to 5-hydroxytryptamine at the level of signal transduction. Biochem J 1995; 307 (Pt 3): 775-82.
    • (1995) Biochem J , vol.307 , Issue.PT 3 , pp. 775-782
    • Roevens, P.1    de Chaffoy de Courcelles, D.2
  • 48
    • 0033835125 scopus 로고    scopus 로고
    • ADP-induced platelet shape change: an investigation of the signalling pathways involved and their dependence on the method of platelet preparation
    • Wilde JI, Retzer M, Siess W, Watson SP. ADP-induced platelet shape change: an investigation of the signalling pathways involved and their dependence on the method of platelet preparation. Platelets 2000; 11: 286-95.
    • (2000) Platelets , vol.11 , pp. 286-295
    • Wilde, J.I.1    Retzer, M.2    Siess, W.3    Watson, S.P.4
  • 49
    • 0035080479 scopus 로고    scopus 로고
    • Rhokinase is involved in the sustained phosphorylation of myosin and the irreversible platelet aggregation induced by PAR1 activating peptide
    • Missy K, Plantavid M, Pacaud P, Viala C, Chap H, Payrastre B. Rhokinase is involved in the sustained phosphorylation of myosin and the irreversible platelet aggregation induced by PAR1 activating peptide. Thromb Haemost 2001; 85: 514-20.
    • (2001) Thromb Haemost , vol.85 , pp. 514-520
    • Missy, K.1    Plantavid, M.2    Pacaud, P.3    Viala, C.4    Chap, H.5    Payrastre, B.6
  • 50
    • 0021255957 scopus 로고
    • Morphometry of platelet internal contraction
    • White JG, Burris SM. Morphometry of platelet internal contraction. Am J Pathol 1984; 115: 412-7.
    • (1984) Am J Pathol , vol.115 , pp. 412-417
    • White, J.G.1    Burris, S.M.2


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