메뉴 건너뛰기




Volumn 35, Issue 4, 2003, Pages 347-355

Regulation of force in vascular smooth muscle

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; CALPONIN; CARDIAC MYOSIN; COMPLEMENTARY DNA; MYOSIN HEAVY CHAIN; MYOSIN LIGHT CHAIN; MYOSIN LIGHT CHAIN KINASE; PHOSPHOPROTEIN PHOSPHATASE 1; PROTEIN SUBUNIT;

EID: 0037384395     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2828(03)00045-2     Document Type: Review
Times cited : (74)

References (95)
  • 1
    • 0014237122 scopus 로고
    • Electromechanical and pharmacomechanical coupling in vascular smooth muscle
    • Somlyo A.V., Somlyo A.P. Electromechanical and pharmacomechanical coupling in vascular smooth muscle. J Pharmacol Exp Ther. 159:1968;129-145.
    • (1968) J Pharmacol Exp Ther , vol.159 , pp. 129-145
    • Somlyo, A.V.1    Somlyo, A.P.2
  • 2
    • 0033002762 scopus 로고    scopus 로고
    • Excitation-contraction coupling in gastrointestinal and other smooth muscles
    • Bolton T.B., Prestwich S.A., Zholos A.V., Gordienko D.V. Excitation-contraction coupling in gastrointestinal and other smooth muscles. Annu Rev Physiol. 61:1999;85-115.
    • (1999) Annu Rev Physiol , vol.61 , pp. 85-115
    • Bolton, T.B.1    Prestwich, S.A.2    Zholos, A.V.3    Gordienko, D.V.4
  • 3
    • 0015919772 scopus 로고
    • Carp muscle calcium binding protein
    • Kretsinger R.H., Nockolds C.E. Carp muscle calcium binding protein. J Biol Chem. 248:1973;3313-3326.
    • (1973) J Biol Chem , vol.248 , pp. 3313-3326
    • Kretsinger, R.H.1    Nockolds, C.E.2
  • 4
    • 0019319097 scopus 로고
    • Calcium- and magnesium-dependent conformational states of calmodulin as determined by nuclear magnetic resonance
    • Seamon K.B. Calcium- and magnesium-dependent conformational states of calmodulin as determined by nuclear magnetic resonance. Biochemistry. 19:1980;207-215.
    • (1980) Biochemistry , vol.19 , pp. 207-215
    • Seamon, K.B.1
  • 6
    • 0016795902 scopus 로고
    • Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity
    • Adelstein R.S., Conti M.A. Phosphorylation of platelet myosin increases actin-activated myosin ATPase activity. Nature. 256:1975;597-598.
    • (1975) Nature , vol.256 , pp. 597-598
    • Adelstein, R.S.1    Conti, M.A.2
  • 8
    • 0020592181 scopus 로고
    • Correlation of enzymatic properties and conformation of smooth muscle myosin
    • Ikebe M., Hinkins S., Hartshorne D.J. Correlation of enzymatic properties and conformation of smooth muscle myosin. Biochemistry. 22:1983;4580-4587.
    • (1983) Biochemistry , vol.22 , pp. 4580-4587
    • Ikebe, M.1    Hinkins, S.2    Hartshorne, D.J.3
  • 9
    • 0033520114 scopus 로고    scopus 로고
    • Phosphorylation regulates the ADP-induced rotation of the light chain domain of smooth muscle myosin
    • Gollub J., Cremo C.R., Cooke R. Phosphorylation regulates the ADP-induced rotation of the light chain domain of smooth muscle myosin. Biochemistry. 38:1999;10107-10118.
    • (1999) Biochemistry , vol.38 , pp. 10107-10118
    • Gollub, J.1    Cremo, C.R.2    Cooke, R.3
  • 10
    • 0027049145 scopus 로고
    • The control of protein phosphatase-1 by targeting subunits: The major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1
    • Alessi D., MacDougall L.K., Sola M., Ikebe M., Cohen P. The control of protein phosphatase-1 by targeting subunits: the major myosin phosphatase in avian smooth muscle is a novel form of protein phosphatase-1. Eur J Biochem. 210:1992;1023-1035.
    • (1992) Eur J Biochem , vol.210 , pp. 1023-1035
    • Alessi, D.1    MacDougall, L.K.2    Sola, M.3    Ikebe, M.4    Cohen, P.5
  • 11
    • 0027972853 scopus 로고
    • Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase
    • Shimizu H., Ito M., Miyahara M., Ichikawa K., Okubo S., Konishi T., et al. Characterization of the myosin-binding subunit of smooth muscle myosin phosphatase. J Biol Chem. 269:1994;30407-30411.
    • (1994) J Biol Chem , vol.269 , pp. 30407-30411
    • Shimizu, H.1    Ito, M.2    Miyahara, M.3    Ichikawa, K.4    Okubo, S.5    Konishi, T.6
  • 12
    • 0028152923 scopus 로고
    • Purification and characterization of the mammalian 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 A.P., Somlyo A.V., et al. Purification and characterization of the mammalian light chain phosphatase holoenzyme: the differential effects of the holoenzyme and its subunits on smooth muscle. J Biol Chem. 269:1994;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
  • 14
    • 0026048788 scopus 로고
    • G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle
    • Kitazawa T., Masuo M., Somlyo A.P. G protein-mediated inhibition of myosin light-chain phosphatase in vascular smooth muscle. Proc Natl Acad Sci USA. 88:1991;9307-9310.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9307-9310
    • Kitazawa, T.1    Masuo, M.2    Somlyo, A.P.3
  • 15
    • 0022272322 scopus 로고
    • Calcium-force relationships as detected with aequorin in two different vascular smooth muscles of the ferret
    • DeFeo T.T., Morgan K.G. Calcium-force relationships as detected with aequorin in two different vascular smooth muscles of the ferret. J Physiol. 369:1985;269-282.
    • (1985) J Physiol , vol.369 , pp. 269-282
    • DeFeo, T.T.1    Morgan, K.G.2
  • 16
    • 0023162273 scopus 로고
    • Alteration in cytoplasmic calcium sensitivity during porcine coronary artery contractions as detected by aequorin
    • Bradley A.B., Morgan K.G. Alteration in cytoplasmic calcium sensitivity during porcine coronary artery contractions as detected by aequorin. J Physiol. 385:1987;437-448.
    • (1987) J Physiol , vol.385 , pp. 437-448
    • Bradley, A.B.1    Morgan, K.G.2
  • 17
    • 0023820267 scopus 로고
    • 2+] determines myosin phosphorylation in agonist-stimulated swine arterial smooth muscle
    • 2+] determines myosin phosphorylation in agonist-stimulated swine arterial smooth muscle. Circ Res. 63:1988;593-603.
    • (1988) Circ Res , vol.63 , pp. 593-603
    • Rembold, C.M.1    Murphy, R.A.2
  • 18
    • 0029132694 scopus 로고
    • Thiophosphorylation of the 130-kDa subunit is associated with a decreased activity of myosin light chain phosphatase in α-toxin permeabilized smooth muscle
    • Trinkle-Mulcahy L., Ichikawaa K., Hartshorne D.J., Siegman M.J., Butler T.M. Thiophosphorylation of the 130-kDa subunit is associated with a decreased activity of myosin light chain phosphatase in α-toxin permeabilized smooth muscle. J Biol Chem. 270:1995;18191-18194.
    • (1995) J Biol Chem , vol.270 , pp. 18191-18194
    • Trinkle-Mulcahy, L.1    Ichikawaa, K.2    Hartshorne, D.J.3    Siegman, M.J.4    Butler, T.M.5
  • 19
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A., Hall A. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16:2002;1587-1609.
    • (2002) Genes Dev , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 20
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung T., Manser E., Tan L., Lim L. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J Biol Chem. 270:1995;29051-29054.
    • (1995) J Biol Chem , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 21
    • 9444242736 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase)
    • Kimura K., Ito M., Amano M., Chihara K., Fukata Y., Nakafuku M., et al. Regulation of myosin phosphatase by Rho and Rho-associated kinase (Rho-kinase). Science. 273:1996;245-248.
    • (1996) Science , vol.273 , pp. 245-248
    • Kimura, K.1    Ito, M.2    Amano, M.3    Chihara, K.4    Fukata, Y.5    Nakafuku, M.6
  • 22
    • 0033601250 scopus 로고    scopus 로고
    • Inhibitory phosphorylation site for Rho-associated kinase on the smooth muscle myosin phosphatase
    • Feng J., Ito M., Ichikawa K., Isaka N., Nishikawa M., Hartshorne D.J., et al. Inhibitory phosphorylation site for Rho-associated kinase on the smooth muscle myosin phosphatase. J Biol Chem. 274:1999;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
  • 23
    • 0037040242 scopus 로고    scopus 로고
    • Agonist-induced force enhancement: The role of isoforms and phosphorylation of the myosin-targeting subunit of myosin light chain phosphatase
    • Richards C.T., Ogut O., Brozovich F.V. Agonist-induced force enhancement: the role of isoforms and phosphorylation of the myosin-targeting subunit of myosin light chain phosphatase. J Biol Chem. 277:2002;4422-4427.
    • (2002) J Biol Chem , vol.277 , pp. 4422-4427
    • Richards, C.T.1    Ogut, O.2    Brozovich, F.V.3
  • 24
    • 0037155782 scopus 로고    scopus 로고
    • Differential association and localization of myosin phosphatase subunits during agonist-induced signal transduction in smooth muscle
    • Shin H.M., Je H.D., Gallant C., Tao T.C., Hartshorne D.J., Ito M., et al. Differential association and localization of myosin phosphatase subunits during agonist-induced signal transduction in smooth muscle. Circ Res. 90:2002;546-553.
    • (2002) Circ Res , vol.90 , pp. 546-553
    • Shin, H.M.1    Je, H.D.2    Gallant, C.3    Tao, T.C.4    Hartshorne, D.J.5    Ito, M.6
  • 25
    • 0037016742 scopus 로고    scopus 로고
    • Rho-dependent agonist-induced spatio-temporal change in myosin phosphorylation in smooth muscle cells
    • Miyazaki K., Yano T., Schmidt D.J., Tokiu T., Shibata M., Lifshitz L.M., et al. Rho-dependent agonist-induced spatio-temporal change in myosin phosphorylation in smooth muscle cells. J Biol Chem. 277:2002;725-734.
    • (2002) J Biol Chem , vol.277 , pp. 725-734
    • Miyazaki, K.1    Yano, T.2    Schmidt, D.J.3    Tokiu, T.4    Shibata, M.5    Lifshitz, L.M.6
  • 28
    • 0035800862 scopus 로고    scopus 로고
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation
    • 2+-free smooth muscle contraction via myosin light chain phosphorylation. J Biol Chem. 276:2001;29567-29574.
    • (2001) J Biol Chem , vol.276 , pp. 29567-29574
    • Niiro, N.1    Ikebe, M.2
  • 29
    • 0035844257 scopus 로고    scopus 로고
    • 2+ -independent smooth muscle contraction. A novel function for integrin-linked kinase
    • 2+ -independent smooth muscle contraction. A novel function for integrin-linked kinase. J Biol Chem. 276:2001;16365-16373.
    • (2001) J Biol Chem , vol.276 , pp. 16365-16373
    • Deng, J.T.1    Van Lierop, J.E.2    Sutherland, C.3    Walsh, M.P.4
  • 30
    • 0034616292 scopus 로고    scopus 로고
    • Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility
    • Kitazawa T., Eto M., Woodsome T.P., Brauntigan D.L. Agonists trigger G protein-mediated activation of the CPI-17 inhibitor phosphoprotein of myosin light chain phosphatase to enhance vascular smooth muscle contractility. J Biol Chem. 275:2000;9897-9900.
    • (2000) J Biol Chem , vol.275 , pp. 9897-9900
    • Kitazawa, T.1    Eto, M.2    Woodsome, T.P.3    Brauntigan, D.L.4
  • 31
    • 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 (Tokyo). 118:1995;1104-1107.
    • (1995) J Biochem (Tokyo) , vol.118 , pp. 1104-1107
    • Eto, M.1    Ohmori, T.2    Suzuki, M.3    Furuya, K.4    Morita, F.5
  • 33
    • 0026806485 scopus 로고
    • Arachidonic acid inhibits myosin light chain phosphatase and sensitizes smooth muscle to calcium
    • Gong M.C., Fuglsang A., Alessi D., Kobayashi S., Cohen P., Somlyo A.V., et al. Arachidonic acid inhibits myosin light chain phosphatase and sensitizes smooth muscle to calcium. J Biol Chem. 267:1992;14662-14668.
    • (1992) J Biol Chem , vol.267 , pp. 14662-14668
    • Gong, M.C.1    Fuglsang, A.2    Alessi, D.3    Kobayashi, S.4    Cohen, P.5    Somlyo, A.V.6
  • 34
    • 0031798554 scopus 로고    scopus 로고
    • Myosin light chain phosphatase: Subunit composition, interactions and regulation
    • Hartshorne D.J., Ito M., Erdodi F. Myosin light chain phosphatase: subunit composition, interactions and regulation. J Muscle Res Cell. 19:1998;325-341.
    • (1998) J Muscle Res Cell , vol.19 , pp. 325-341
    • Hartshorne, D.J.1    Ito, M.2    Erdodi, F.3
  • 35
    • 0030667513 scopus 로고    scopus 로고
    • Regulation of cGMP by soluble and particulate guanylyl cyclases in cultured human airway smooth muscle
    • Hamad A.M., Range S., Holland E., Knox A.J. Regulation of cGMP by soluble and particulate guanylyl cyclases in cultured human airway smooth muscle. Am J Physiol. 273:1997;L807-813.
    • (1997) Am J Physiol , vol.273 , pp. 807-813
    • Hamad, A.M.1    Range, S.2    Holland, E.3    Knox, A.J.4
  • 36
    • 0033584786 scopus 로고    scopus 로고
    • Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ia
    • Surks H.K., Mochizuki N., Kasai Y., Georgescu S.P., Tang K.M., Ito M., et al. Regulation of myosin phosphatase by a specific interaction with cGMP-dependent protein kinase Ia. Science. 286:1999;1583-1587.
    • (1999) Science , vol.286 , pp. 1583-1587
    • Surks, H.K.1    Mochizuki, N.2    Kasai, Y.3    Georgescu, S.P.4    Tang, K.M.5    Ito, M.6
  • 37
    • 0035813193 scopus 로고    scopus 로고
    • Role of myosin phosphatase isoforms in cGMP-mediated smooth muscle relaxation
    • Khatri J.J., Joyce K.M., Brozovich F.V., Fisher S.A. Role of myosin phosphatase isoforms in cGMP-mediated smooth muscle relaxation. J Biol Chem. 276:2001;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
  • 38
    • 0024421567 scopus 로고
    • Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles
    • Horiuti K., Somlyo A.V., Goldman Y.E., Somlyo A.P. Kinetics of contraction initiated by flash photolysis of caged adenosine triphosphate in tonic and phasic smooth muscles. J Gen Physiol. 94:1989;769-781.
    • (1989) J Gen Physiol , vol.94 , pp. 769-781
    • Horiuti, K.1    Somlyo, A.V.2    Goldman, Y.E.3    Somlyo, A.P.4
  • 39
    • 0027226230 scopus 로고
    • Structure of the actin-myosin complex and its implications for muscle contraction
    • Rayment I., Holden H.M., Whittaker M., Yohn C.B., Lorenz M., Holmes K.C., et al. Structure of the actin-myosin complex and its implications for muscle contraction. Science. 261:1993;58-65.
    • (1993) Science , vol.261 , pp. 58-65
    • Rayment, I.1    Holden, H.M.2    Whittaker, M.3    Yohn, C.B.4    Lorenz, M.5    Holmes, K.C.6
  • 40
    • 0032483563 scopus 로고    scopus 로고
    • Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: Visualization of the pre-power stroke state
    • Dominguez R., Freyzon Y., Trybus K.M., Cohen C. Crystal structure of a vertebrate smooth muscle myosin motor domain and its complex with the essential light chain: visualization of the pre-power stroke state. Cell. 94:1998;559-571.
    • (1998) Cell , vol.94 , pp. 559-571
    • Dominguez, R.1    Freyzon, Y.2    Trybus, K.M.3    Cohen, C.4
  • 41
    • 0023664431 scopus 로고
    • Two smooth muscle myosin heavy chains in cultured aorta smooth muscle cells. A comparative study
    • Eddinger T.J., Murphy R.A. Two smooth muscle myosin heavy chains in cultured aorta smooth muscle cells. A comparative study. J Biol Chem. 2262:1987;7282-7288.
    • (1987) J Biol Chem , vol.2262 , pp. 7282-7288
    • Eddinger, T.J.1    Murphy, R.A.2
  • 42
    • 0025790141 scopus 로고
    • Characterization of a mammalian smooth musclemyosin heavy-chain gene: Complete nucleotide and protein coding sequence and analysis of the 5' end of the gene
    • Babij P., Kelly C., Periasamy M. Characterization of a mammalian smooth musclemyosin heavy-chain gene: complete nucleotide and protein coding sequence and analysis of the 5' end of the gene. Proc Natl Acad USA. 88:1991;10676-10680.
    • (1991) Proc Natl Acad USA , vol.88 , pp. 10676-10680
    • Babij, P.1    Kelly, C.2    Periasamy, M.3
  • 44
    • 0030662128 scopus 로고    scopus 로고
    • Expression of smooth muscle myosin heavy chains and unloaded shortening in single smooth muscle cells
    • Meer D.P., Eddinger T.J. Expression of smooth muscle myosin heavy chains and unloaded shortening in single smooth muscle cells. Am J Physiol. 273:1997;C1259-1266.
    • (1997) Am J Physiol , vol.273 , pp. 1259-1266
    • Meer, D.P.1    Eddinger, T.J.2
  • 45
    • 0037033785 scopus 로고    scopus 로고
    • The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties
    • Rovner A.S., Fagnant P.M., Lowey S., Trybus K.M. The carboxyl-terminal isoforms of smooth muscle myosin heavy chain determine thick filament assembly properties. J Cell Biol. 156:2002;113-123.
    • (2002) J Cell Biol , vol.156 , pp. 113-123
    • Rovner, A.S.1    Fagnant, P.M.2    Lowey, S.3    Trybus, K.M.4
  • 46
    • 0027258646 scopus 로고
    • An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature
    • Kelley C.A., Takahashi M., Yu J.H., Adelstein R.S. An insert of seven amino acids confers functional differences between smooth muscle myosins from the intestines and vasculature. J Biol Chem. 268:1993;12848-12854.
    • (1993) J Biol Chem , vol.268 , pp. 12848-12854
    • Kelley, C.A.1    Takahashi, M.2    Yu, J.H.3    Adelstein, R.S.4
  • 47
    • 0032411784 scopus 로고    scopus 로고
    • A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap
    • Lauzon A-M., Tyska M.J., Rovner A.S., Freyzon Y., Warshaw D.M., Trybus K.M. A 7-amino-acid insert in the heavy chain nucleotide binding loop alters the kinetics of smooth muscle myosin in the laser trap. J Muscle Res Cell Motil. 19:1998;825-837.
    • (1998) J Muscle Res Cell Motil , vol.19 , pp. 825-837
    • Lauzon, A.-M.1    Tyska, M.J.2    Rovner, A.S.3    Freyzon, Y.4    Warshaw, D.M.5    Trybus, K.M.6
  • 48
    • 0031668167 scopus 로고    scopus 로고
    • Differences in contractile protein content and isoforms in phasic and tonic smooth muscles
    • Szymanski P.T., Chacko T.K., Rovner A.S., Goyal R.J. Differences in contractile protein content and isoforms in phasic and tonic smooth muscles. Am J Physiol. 275:1998;C684-692.
    • (1998) Am J Physiol , vol.275 , pp. 684-692
    • Szymanski, P.T.1    Chacko, T.K.2    Rovner, A.S.3    Goyal, R.J.4
  • 49
    • 0343338187 scopus 로고    scopus 로고
    • Substrate and product dependence of force and shortening in fast and slow smooth muscle
    • Lofgren M., Malmqvist U., Arner A. Substrate and product dependence of force and shortening in fast and slow smooth muscle. J Gen Physiol. 117:2001;407-418.
    • (2001) J Gen Physiol , vol.117 , pp. 407-418
    • Lofgren, M.1    Malmqvist, U.2    Arner, A.3
  • 50
    • 0035024573 scopus 로고    scopus 로고
    • Single rabbit stomach smooth muscle cell heavy chain SMB expression and shortening velocity
    • Meer D.P., Eddinger T.J. Single rabbit stomach smooth muscle cell heavy chain SMB expression and shortening velocity. Am J Physiol. 280:2001;C309-316.
    • (2001) Am J Physiol , vol.280 , pp. 309-316
    • Meer, D.P.1    Eddinger, T.J.2
  • 51
    • 0035735747 scopus 로고    scopus 로고
    • Loss of SM-B myosin affects muscle shortening velocity and maximal force development
    • Babu G.J., Loukianov E., Loukianova T., Pyne G.J., Huke S., Osol G., et al. Loss of SM-B myosin affects muscle shortening velocity and maximal force development. Nature Cell Biol. 3:2001;1025-1029.
    • (2001) Nature Cell Biol , vol.3 , pp. 1025-1029
    • Babu, G.J.1    Loukianov, E.2    Loukianova, T.3    Pyne, G.J.4    Huke, S.5    Osol, G.6
  • 53
    • 0023645308 scopus 로고
    • Nonmuscle and smooth muscle myosin light chain mRNAs are generated from a single gene by the tissue-specific alternative RNA splicing
    • Nabeshima Y., Nonomura Y., Fujii-Kuriyama Y. Nonmuscle and smooth muscle myosin light chain mRNAs are generated from a single gene by the tissue-specific alternative RNA splicing. J Biol Chem. 262:1987;10608-10612.
    • (1987) J Biol Chem , vol.262 , pp. 10608-10612
    • Nabeshima, Y.1    Nonomura, Y.2    Fujii-Kuriyama, Y.3
  • 54
    • 0025817957 scopus 로고
    • Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening in smooth muscle
    • Malmqvist U., Arner A. Correlation between isoform composition of the 17 kDa myosin light chain and maximal shortening in smooth muscle. Pflugers Arch. 418:1991;523-530.
    • (1991) Pflugers Arch , vol.418 , pp. 523-530
    • Malmqvist, U.1    Arner, A.2
  • 55
    • 0030980825 scopus 로고    scopus 로고
    • Endothelin-1 alters the contractile phenotype of cultured embryonic smooth muscle cells
    • Fisher S.A., Ikebe M., Brozovich F.V. Endothelin-1 alters the contractile phenotype of cultured embryonic smooth muscle cells. Circ Res. 80:1997;885-893.
    • (1997) Circ Res , vol.80 , pp. 885-893
    • Fisher, S.A.1    Ikebe, M.2    Brozovich, F.V.3
  • 56
    • 0023756765 scopus 로고
    • Distribution of isoelectric variants of the 17,000-dalton myosin light chain in mammalian smooth muscle
    • Helper D.J., Lash J.A., Hathaway D.R. Distribution of isoelectric variants of the 17,000-dalton myosin light chain in mammalian smooth muscle. J Biol Chem. 263:1988;15748-15753.
    • (1988) J Biol Chem , vol.263 , pp. 15748-15753
    • Helper, D.J.1    Lash, J.A.2    Hathaway, D.R.3
  • 57
    • 0032553296 scopus 로고    scopus 로고
    • Myosin essential light chain isoforms modulate the velocity of shortening propelled by nonphosphorylated cross-bridges
    • Matthew J.D., Khromov A.S., Trybus K.M., Somlyo A.P., Somlyo A.V. Myosin essential light chain isoforms modulate the velocity of shortening propelled by nonphosphorylated cross-bridges. J Biol Chem. 273:1998;31289-31296.
    • (1998) J Biol Chem , vol.273 , pp. 31289-31296
    • Matthew, J.D.1    Khromov, A.S.2    Trybus, K.M.3    Somlyo, A.P.4    Somlyo, A.V.5
  • 58
    • 0033916693 scopus 로고    scopus 로고
    • Expression of smooth muscle myosin light chain 17 and unloaded shortening in single smooth muscle cells
    • Eddinger T.J., Korwek A.A., Meer D.P., Sherwood J.J. Expression of smooth muscle myosin light chain 17 and unloaded shortening in single smooth muscle cells. Am J Physiol. 278:2000;C1133-1142.
    • (2000) Am J Physiol , vol.278 , pp. 1133-1142
    • Eddinger, T.J.1    Korwek, A.A.2    Meer, D.P.3    Sherwood, J.J.4
  • 59
    • 0033521035 scopus 로고    scopus 로고
    • Forced expression of essential myosin ight chain isoforms demonstrates their role in smooth muscle force production
    • Huang Q.Q., Fisher S.A., Brozovich F.V. Forced expression of essential myosin ight chain isoforms demonstrates their role in smooth muscle force production. J Biol Chem. 274:1999;35095-35098.
    • (1999) J Biol Chem , vol.274 , pp. 35095-35098
    • Huang, Q.Q.1    Fisher, S.A.2    Brozovich, F.V.3
  • 60
    • 0033635907 scopus 로고    scopus 로고
    • Determinants of the contractile properties in the embryonic chicken gizzard and aorta
    • Ogut O., Brozovich F.V. Determinants of the contractile properties in the embryonic chicken gizzard and aorta. Am J Physiol. 279:2000;C1722-1732.
    • (2000) Am J Physiol , vol.279 , pp. 1722-1732
    • Ogut, O.1    Brozovich, F.V.2
  • 61
    • 0010707918 scopus 로고
    • Tonic force maintenance with reduced shortening velocity in arterial smooth muscle
    • Dillon P.F., Murphy R.A. Tonic force maintenance with reduced shortening velocity in arterial smooth muscle. Am J Physiol. 242:1982;C102-108.
    • (1982) Am J Physiol , vol.242 , pp. 102-108
    • Dillon, P.F.1    Murphy, R.A.2
  • 62
    • 0023212340 scopus 로고
    • Effects of dihydropyridines on stress, myosin phosphorylation, and Vo in smooth muscle
    • Moreland S., Moreland R.S. Effects of dihydropyridines on stress, myosin phosphorylation, and Vo in smooth muscle. Am J Physiol. 252:1987;H1049-1058.
    • (1987) Am J Physiol , vol.252 , pp. 1049-1058
    • Moreland, S.1    Moreland, R.S.2
  • 63
    • 0024554764 scopus 로고
    • Agonist-specific myosin phosphorylation and intracellular calcium during isometric contractions of arterial smooth muscle
    • Jiang M.J., Morgan K.G. Agonist-specific myosin phosphorylation and intracellular calcium during isometric contractions of arterial smooth muscle. Pflugers Arch. 413:1989;637-643.
    • (1989) Pflugers Arch , vol.413 , pp. 637-643
    • Jiang, M.J.1    Morgan, K.G.2
  • 64
    • 0023841161 scopus 로고
    • Cross-bridge phosphorylation and regulation of latch state in smooth muscle
    • Hai C.M., Murphy R.A. Cross-bridge phosphorylation and regulation of latch state in smooth muscle. Am J Physiol. 254:1988;C99-106.
    • (1988) Am J Physiol , vol.254 , pp. 99-106
    • Hai, C.M.1    Murphy, R.A.2
  • 66
    • 0028237238 scopus 로고
    • Cross-bridge cycling at rest and during activation. Turnover of myosin-bound ADP in permeabilized smooth muscle
    • Vyas T.B., Mooers S.U., Narayan S.R., Siegman M.J., Butler T.M. Cross-bridge cycling at rest and during activation. Turnover of myosin-bound ADP in permeabilized smooth muscle. J Biol Chem. 269:1994;7316-7322.
    • (1994) J Biol Chem , vol.269 , pp. 7316-7322
    • Vyas, T.B.1    Mooers, S.U.2    Narayan, S.R.3    Siegman, M.J.4    Butler, T.M.5
  • 67
    • 0031709567 scopus 로고    scopus 로고
    • MgADP promotes a catch-like state developed through force-calcium hysteresis in tonic smooth muscle
    • Khromov A., Somlyo A.V., Somlyo A.P. MgADP promotes a catch-like state developed through force-calcium hysteresis in tonic smooth muscle. Biophys J. 75:1998;1926-1934.
    • (1998) Biophys J , vol.75 , pp. 1926-1934
    • Khromov, A.1    Somlyo, A.V.2    Somlyo, A.P.3
  • 68
    • 0034921574 scopus 로고    scopus 로고
    • Invited review: Cross-bridge regulation by thin filament-associated proteins
    • Morgan K.G., Gangopadhyay S.S. Invited review: cross-bridge regulation by thin filament-associated proteins. J Appl Physiol. 91:2001;953-962.
    • (2001) J Appl Physiol , vol.91 , pp. 953-962
    • Morgan, K.G.1    Gangopadhyay, S.S.2
  • 69
    • 0034925225 scopus 로고    scopus 로고
    • Invited review: Focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle
    • Gerthoffer W.T., Funst S.J. Invited review: focal adhesion and small heat shock proteins in the regulation of actin remodeling and contractility in smooth muscle. J Appl Physiol. 91:2001;963-972.
    • (2001) J Appl Physiol , vol.91 , pp. 963-972
    • Gerthoffer, W.T.1    Funst, S.J.2
  • 70
    • 0028906470 scopus 로고
    • Activation of mitogen-activated protein kinase in porcine carotid arteries
    • Adam L.P., Franklin M.T., Raff G.J., Hathaway D.R. Activation of mitogen-activated protein kinase in porcine carotid arteries. Circ Res. 76:1995;183-190.
    • (1995) Circ Res , vol.76 , pp. 183-190
    • Adam, L.P.1    Franklin, M.T.2    Raff, G.J.3    Hathaway, D.R.4
  • 71
    • 0028843312 scopus 로고
    • Thin filament regulation of force activation is not essential in single vascular smooth muscle cells
    • Brozovich F.V., Yamakawa M. Thin filament regulation of force activation is not essential in single vascular smooth muscle cells. Am J Physiol. 268:1995;C237-242.
    • (1995) Am J Physiol , vol.268 , pp. 237-242
    • Brozovich, F.V.1    Yamakawa, M.2
  • 73
    • 0026695761 scopus 로고
    • Regulation of vascular smooth muscle tone by caldesmon
    • Katsuyama H., Wang C.L., Morgan K.G. Regulation of vascular smooth muscle tone by caldesmon. J Biol Chem. 267:1992;14555-14558.
    • (1992) J Biol Chem , vol.267 , pp. 14555-14558
    • Katsuyama, H.1    Wang, C.L.2    Morgan, K.G.3
  • 74
    • 0029957346 scopus 로고    scopus 로고
    • The effects of caldesmon extraction on mechanical properties of skinned smooth muscle fibre preparations
    • Malmqvist U., Arner A., Makuch R., Dabrowska R. The effects of caldesmon extraction on mechanical properties of skinned smooth muscle fibre preparations. Pflugers Arch. 432:1996;241-247.
    • (1996) Pflugers Arch , vol.432 , pp. 241-247
    • Malmqvist, U.1    Arner, A.2    Makuch, R.3    Dabrowska, R.4
  • 75
    • 0027749388 scopus 로고
    • Calponin: Thin filament-linked regulation of smooth muscle contraction
    • Winder S.J., Walsh M.P. Calponin: thin filament-linked regulation of smooth muscle contraction. Cell Signal. 5:1993;677-686.
    • (1993) Cell Signal , vol.5 , pp. 677-686
    • Winder, S.J.1    Walsh, M.P.2
  • 77
    • 0026586912 scopus 로고
    • Caldesmon binds to smooth muscle myosin and myosin rod and crosslinks thick filaments to actin filaments
    • Marston S., Pinter K., Bennett P. Caldesmon binds to smooth muscle myosin and myosin rod and crosslinks thick filaments to actin filaments. J Mucle Res Cell Motil. 13:1992;206-218.
    • (1992) J Mucle Res Cell Motil , vol.13 , pp. 206-218
    • Marston, S.1    Pinter, K.2    Bennett, P.3
  • 78
    • 0024477919 scopus 로고
    • 2+ regulation of the activity of synthetic smooth-muscle thin filaments
    • 2+ regulation of the activity of synthetic smooth-muscle thin filaments. Biochem J. 257:1989;839-843.
    • (1989) Biochem J , vol.257 , pp. 839-843
    • Pritchard, K.1    Marston, S.B.2
  • 79
    • 0022400733 scopus 로고
    • Caldesmon-induced inhibition of ATPase activity of actomyosin and contraction of skinned chicken gizzard smooth muscle
    • Szpacenko A., Wagner J., Dabrowska R., Ruegg J.C. Caldesmon-induced inhibition of ATPase activity of actomyosin and contraction of skinned chicken gizzard smooth muscle. FEBS Lett. 192:1985;9-12.
    • (1985) FEBS Lett , vol.192 , pp. 9-12
    • Szpacenko, A.1    Wagner, J.2    Dabrowska, R.3    Ruegg, J.C.4
  • 80
    • 0025799684 scopus 로고
    • The molecular anatomy of caldesmon
    • Marston S.B., Redwood C.S. The molecular anatomy of caldesmon. Biochem J. 279:1991;1-16.
    • (1991) Biochem J , vol.279 , pp. 1-16
    • Marston, S.B.1    Redwood, C.S.2
  • 81
    • 0024585166 scopus 로고
    • Phosphorylation of caldesmon prevents its interaction with smooth muscle myosin
    • Sutherland C., Walsh M.P. Phosphorylation of caldesmon prevents its interaction with smooth muscle myosin. J Biol Chem. 264:1989;578-583.
    • (1989) J Biol Chem , vol.264 , pp. 578-583
    • Sutherland, C.1    Walsh, M.P.2
  • 83
    • 0029757474 scopus 로고    scopus 로고
    • Activation of MAP kinases and phosphorylation of caldesmon in canine colonic smooth muscle
    • Gerthoffer W.T., Yamboliev I.A., Shearer M., Pohl J., Haynes R., Dang S., et al. Activation of MAP kinases and phosphorylation of caldesmon in canine colonic smooth muscle. J Physiol. 495:1996;597-609.
    • (1996) J Physiol , vol.495 , pp. 597-609
    • Gerthoffer, W.T.1    Yamboliev, I.A.2    Shearer, M.3    Pohl, J.4    Haynes, R.5    Dang, S.6
  • 85
    • 0024514394 scopus 로고
    • Phosphorylation of caldesmon in arterial smooth muscle
    • Adam L.P., Haeberle J.R., Hathaway D.R. Phosphorylation of caldesmon in arterial smooth muscle. J Biol Chem. 264:1989;7698-7703.
    • (1989) J Biol Chem , vol.264 , pp. 7698-7703
    • Adam, L.P.1    Haeberle, J.R.2    Hathaway, D.R.3
  • 86
    • 0031722643 scopus 로고    scopus 로고
    • A role for MAP kinase in differentiated smooth muscle contraction evoked by alpha-adrenoceptor stimulation
    • Dessy C., Kim I., Sougnez C.L., Laporte R., Morgan K.G. A role for MAP kinase in differentiated smooth muscle contraction evoked by alpha-adrenoceptor stimulation. Am J Physiol. 275:1998;C1081-1086.
    • (1998) Am J Physiol , vol.275 , pp. 1081-1086
    • Dessy, C.1    Kim, I.2    Sougnez, C.L.3    Laporte, R.4    Morgan, K.G.5
  • 88
    • 0033864990 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinases regulate ERK and p38 MAP kinases in canine colonic smooth muscle
    • Yamboliev I.A., Wiesmann K.M., Singer C.A., Hedges J.C., Gerthoffer W.T. Phosphatidylinositol 3-kinases regulate ERK and p38 MAP kinases in canine colonic smooth muscle. Am J Physiol. 279:2000;C352-C360.
    • (2000) Am J Physiol , vol.279
    • Yamboliev, I.A.1    Wiesmann, K.M.2    Singer, C.A.3    Hedges, J.C.4    Gerthoffer, W.T.5
  • 89
    • 0029008415 scopus 로고
    • Calponin reduces shortening velocity in skinned Taenia coli smooth muscle fibres
    • Jaworowski A., Anderson K.I., Arner A., Engstrom M., Gimona M., Strasser P., et al. Calponin reduces shortening velocity in skinned Taenia coli smooth muscle fibres. FEBS Lett. 265:1995;167-171.
    • (1995) FEBS Lett , vol.265 , pp. 167-171
    • Jaworowski, A.1    Anderson, K.I.2    Arner, A.3    Engstrom, M.4    Gimona, M.5    Strasser, P.6
  • 90
    • 0033798958 scopus 로고    scopus 로고
    • The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin
    • Facemire C., Brozovich F.V., Jin J.P. The maximal velocity of vascular smooth muscle shortening is independent of the expression of calponin. J Muscle Res Cell Motil. 21:2000;367-373.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 367-373
    • Facemire, C.1    Brozovich, F.V.2    Jin, J.P.3
  • 91
    • 0029824794 scopus 로고    scopus 로고
    • Inhibition by calponin of isometric force in demembranated vascular smooth muscle strips: The critical role of serine-175
    • Uyama Y., Imaizumi Y., Watanabe M., Walsh M.P. Inhibition by calponin of isometric force in demembranated vascular smooth muscle strips: the critical role of serine-175. Biochem J. 319:1996;551-558.
    • (1996) Biochem J , vol.319 , pp. 551-558
    • Uyama, Y.1    Imaizumi, Y.2    Watanabe, M.3    Walsh, M.P.4
  • 92
    • 0033693870 scopus 로고    scopus 로고
    • Live dynamics of GFP-calponin: Isoform-specific modulation of the actin cytoskeleton and autoregulation by C-terminal sequences
    • Danninger C., Gimona M. Live dynamics of GFP-calponin: isoform-specific modulation of the actin cytoskeleton and autoregulation by C-terminal sequences. J Cell Sci. 21:2000;3725-3736.
    • (2000) J Cell Sci , vol.21 , pp. 3725-3736
    • Danninger, C.1    Gimona, M.2
  • 93
    • 0037213601 scopus 로고    scopus 로고
    • Developmentally regulated expression of calponin isoforms and the effect of h2-calponin on cell proliferation
    • Hossain M., Hwang D.Y., Huang Q.Q., Sasaki Y., Jin J.P. Developmentally regulated expression of calponin isoforms and the effect of h2-calponin on cell proliferation. Am J Physiol. 248:2003;C156-C167.
    • (2003) Am J Physiol , vol.248
    • Hossain, M.1    Hwang, D.Y.2    Huang, Q.Q.3    Sasaki, Y.4    Jin, J.P.5
  • 94
    • 0031957434 scopus 로고    scopus 로고
    • Relationship between paxillin and myosin phosphorylation during muscarinic stimulation of smooth muscle
    • Mehta D., Wang Z., Wu M.F., Gunst S.J. Relationship between paxillin and myosin phosphorylation during muscarinic stimulation of smooth muscle. Am J Physiol. 274:1998;C741-C747.
    • (1998) Am J Physiol , vol.274
    • Mehta, D.1    Wang, Z.2    Wu, M.F.3    Gunst, S.J.4
  • 95
    • 0037101563 scopus 로고    scopus 로고
    • The focal adhesion protein paxillin regulates contraction in canine tracheal smooth muscle
    • Tang D.D., Wu M.F., Opazo Saez A.M., Gunst S.J. The focal adhesion protein paxillin regulates contraction in canine tracheal smooth muscle. J Physiol. 545:2002;501-513.
    • (2002) J Physiol , vol.545 , pp. 501-513
    • Tang, D.D.1    Wu, M.F.2    Opazo Saez, A.M.3    Gunst, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.