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Volumn 137, Issue 2-3, 2003, Pages 141-149

Force and myosin light chain phosphorylation in dog airway smooth muscle activated in different ways

Author keywords

Airway, smooth muscle, activation; Mammals, dog; Muscle, smooth, myosin light chain phosphorylation; Pharmacological agents, wortmannin; Pharmacological agents, Y 27632; Phosphorylation, myosin light chain, isometric force

Indexed keywords

ACETYLCHOLINE; CALYCULIN A; INHIBITOR PROTEIN; MYOSIN LIGHT CHAIN; POTASSIUM CHLORIDE; RHO KINASE INHIBITOR; UNCLASSIFIED DRUG; WORTMANNIN;

EID: 0141606699     PISSN: 15699048     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1569-9048(03)00143-5     Document Type: Article
Times cited : (15)

References (33)
  • 1
    • 0018881743 scopus 로고
    • Regulation and kinetics of the actin-myosin-ATP interaction
    • Adelstein R., Eisenberg E. Regulation and kinetics of the actin-myosin-ATP interaction. Ann. Rev. Biochem. 49:1980;921-956.
    • (1980) Ann. Rev. Biochem. , vol.49 , pp. 921-956
    • Adelstein, R.1    Eisenberg, E.2
  • 2
    • 0009240259 scopus 로고
    • Dissociation of relaxation and myosin light chain dephosphorylation in smooth muscle
    • Bárány M., Hegedüs L., Bárány K. Dissociation of relaxation and myosin light chain dephosphorylation in smooth muscle. Biophys. J. 66:1994;A139.
    • (1994) Biophys. J. , vol.66 , pp. 139
    • Bárány, M.1    Hegedüs, L.2    Bárány, K.3
  • 3
    • 0033964475 scopus 로고    scopus 로고
    • Versatile, high-speed force transducer using a laser diode beam as an optical lever
    • Barb M.B., Morris A.B., Maass-Moreno R., Ragozzino J., Ford L.E. Versatile, high-speed force transducer using a laser diode beam as an optical lever. J. Appl. Physiol. 88:2000;308-314.
    • (2000) J. Appl. Physiol. , vol.88 , pp. 308-314
    • Barb, M.B.1    Morris, A.B.2    Maass-Moreno, R.3    Ragozzino, J.4    Ford, L.E.5
  • 4
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • Bremel R.D., Weber A. Cooperation within actin filament in vertebrate skeletal muscle. Nat. New Biol. 238:1972;97-101.
    • (1972) Nat. New Biol. , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 5
    • 0019423570 scopus 로고
    • Effect of phosphorylation, calcium ion and tropomyosin on actin-activated ATPase activity of mammalian smooth muscle myosin
    • Chacko S. Effect of phosphorylation, calcium ion and tropomyosin on actin-activated ATPase activity of mammalian smooth muscle myosin. Biochemistry. 20:1981;707-712.
    • (1981) Biochemistry , vol.20 , pp. 707-712
    • Chacko, S.1
  • 7
    • 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. Cell Physiol. 242:1982;C102-C108.
    • (1982) Am. J. Physiol. Cell Physiol. , vol.242
    • Dillon, P.F.1    Murphy, R.A.2
  • 8
    • 0019433353 scopus 로고
    • Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle
    • Dillon P.F., Aksoy M.O., Driska S.P., Murphy R.A. Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle. Science. 211:1981;495-497.
    • (1981) Science , vol.211 , pp. 495-497
    • Dillon, P.F.1    Aksoy, M.O.2    Driska, S.P.3    Murphy, R.A.4
  • 9
  • 10
    • 0017385529 scopus 로고
    • Tension responses to sudden length change in stimulated frog muscle fibres near slack length
    • Ford L.E., Huxley A.F., Simmons R.M. Tension responses to sudden length change in stimulated frog muscle fibres near slack length. J. Physiol. 269:1977;441-515.
    • (1977) J. Physiol. , vol.269 , pp. 441-515
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 12
    • 0032573607 scopus 로고    scopus 로고
    • The effects of the Rho-kinase inhibitor, Y-27632 on arachidonic acid-, GTP-gamma-S-, and phorbol ester-induced Ca2+-sensitization of smooth muscle
    • Fu X., Gong M.C., Jia T., Somlyo A.V., Somlyo A.P. The effects of the Rho-kinase inhibitor, Y-27632 on arachidonic acid-, GTP-gamma-S-, and phorbol ester-induced Ca2+-sensitization of smooth muscle. FEBS Lett. 440:(1-2):1998;183-187.
    • (1998) FEBS Lett. , vol.440 , Issue.1-2 , pp. 183-187
    • Fu, X.1    Gong, M.C.2    Jia, T.3    Somlyo, A.V.4    Somlyo, A.P.5
  • 13
    • 0023126886 scopus 로고
    • Dissociation of myosin phosphorylation and active tension during muscarinic stimulation of tracheal smooth muscle
    • Gerthoffer W.T. Dissociation of myosin phosphorylation and active tension during muscarinic stimulation of tracheal smooth muscle. J. Pharmacol. Exp. Ther. 240:1987;8-15.
    • (1987) J. Pharmacol. Exp. Ther. , vol.240 , pp. 8-15
    • Gerthoffer, W.T.1
  • 14
    • 0016248148 scopus 로고
    • Calcium-activated tension of skinned muscle fibers of the frog. Dependence on magnesium adenosine triphosphate concentration
    • Godt R.E. Calcium-activated tension of skinned muscle fibers of the frog. Dependence on magnesium adenosine triphosphate concentration. J. Gen. Physiol. 63:1974;722-730.
    • (1974) J. Gen. Physiol. , vol.63 , pp. 722-730
    • Godt, R.E.1
  • 15
    • 0022115851 scopus 로고
    • A radioimmunoblotting method for measuring myosin light chain phosphorylation levels in smooth muscle
    • Hathaway D.R., Haeberle J.R. A radioimmunoblotting method for measuring myosin light chain phosphorylation levels in smooth muscle. Am. J. Physiol. 249:1985;C345-C351.
    • (1985) Am. J. Physiol. , vol.249
    • Hathaway, D.R.1    Haeberle, J.R.2
  • 17
    • 0014466965 scopus 로고
    • Force measurements in skinned muscle fibres
    • Hellam D.C., Podolsky R.J. Force measurements in skinned muscle fibres. J. Physiol. 200:1969;807-819.
    • (1969) J. Physiol. , vol.200 , pp. 807-819
    • Hellam, D.C.1    Podolsky, R.J.2
  • 18
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley A.F. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:1957;255-318.
    • (1957) Prog. Biophys. Biophys. Chem. , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 19
    • 0015236610 scopus 로고
    • Proposed mechanism of force generation in striated muscle
    • Huxley A.F., Simmons R.M. Proposed mechanism of force generation in striated muscle. Nature. 233:1971;533-538.
    • (1971) Nature , vol.233 , pp. 533-538
    • Huxley, A.F.1    Simmons, R.M.2
  • 22
    • 0022115276 scopus 로고
    • Myosin phosphorylation, force, and maximal shortening velocity in neurally stimulated tracheal smooth muscle
    • Kamm K.E., Stull J.T. Myosin phosphorylation, force, and maximal shortening velocity in neurally stimulated tracheal smooth muscle. Am. J. Physiol. Cell Physiol. 249:1985;C238-C247.
    • (1985) Am. J. Physiol. Cell Physiol. , vol.249
    • Kamm, K.E.1    Stull, J.T.2
  • 23
    • 0030977123 scopus 로고    scopus 로고
    • Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation
    • Kureishi Y., Kobayashi S., Amano M., Kimura K., Kanaide H., Nakano T., Kaibuchi K., Ito M. Rho-associated kinase directly induces smooth muscle contraction through myosin light chain phosphorylation. J. Biol. Chem. 272:1997;12257-12260.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12257-12260
    • Kureishi, Y.1    Kobayashi, S.2    Amano, M.3    Kimura, K.4    Kanaide, H.5    Nakano, T.6    Kaibuchi, K.7    Ito, M.8
  • 24
    • 0035015336 scopus 로고    scopus 로고
    • Simple freezing apparatus for resolving rapid metabolic events associated with smooth muscle activation
    • Maass-Moreno R., Burdyga T., Mitchell R.W., Seow C.Y., Ragozzino J., Ford L.E. Simple freezing apparatus for resolving rapid metabolic events associated with smooth muscle activation. J. Appl. Physiol. 90:2001;2453-2459.
    • (2001) J. Appl. Physiol. , vol.90 , pp. 2453-2459
    • Maass-Moreno, R.1    Burdyga, T.2    Mitchell, R.W.3    Seow, C.Y.4    Ragozzino, J.5    Ford, L.E.6
  • 27
    • 0023019582 scopus 로고
    • Different phosphorylated forms of myosin in contracting tracheal smooth muscle
    • Persechini A., Kamm K.E., Stull J.T. Different phosphorylated forms of myosin in contracting tracheal smooth muscle. J. Biol. Chem. 261:1986;6293-6299.
    • (1986) J. Biol. Chem. , vol.261 , pp. 6293-6299
    • Persechini, A.1    Kamm, K.E.2    Stull, J.T.3
  • 28
    • 0036083694 scopus 로고    scopus 로고
    • Myosin light chain phosphorylation facilitates in vivo myosin filament reassembly after mechanical perturbations
    • Qi D., Mitchell R.W., Burdyga T., Ford L.E., Kuo K.-H., Seow C.Y. Myosin light chain phosphorylation facilitates in vivo myosin filament reassembly after mechanical perturbations. Am. J. Physiol. Cell Physiol. 282:2002;C1298-C1305.
    • (2002) Am. J. Physiol. Cell Physiol. , vol.282
    • Qi, D.1    Mitchell, R.W.2    Burdyga, T.3    Ford, L.E.4    Kuo, K.-H.5    Seow, C.Y.6
  • 29
    • 0034495866 scopus 로고    scopus 로고
    • Series-to-parallel transition in the filament lattice of airway smooth muscle
    • Seow C.W., Pratusevich V.R., Ford L.E. Series-to-parallel transition in the filament lattice of airway smooth muscle. J. Appl. Physiol. 89:2000;869-876.
    • (2000) J. Appl. Physiol. , vol.89 , pp. 869-876
    • Seow, C.W.1    Pratusevich, V.R.2    Ford, L.E.3
  • 30
    • 0017323872 scopus 로고
    • 2+-linked phosphorylation of a light chain of vertebrate smooth-muscle myosin
    • 2+-linked phosphorylation of a light chain of vertebrate smooth-muscle myosin. Eur. J. Biochem. 73:1977;477-483.
    • (1977) Eur. J. Biochem. , vol.73 , pp. 477-483
    • Sobieszek, A.1
  • 31
    • 0031023787 scopus 로고    scopus 로고
    • Quantitative densitometry of proteins stained with coomassie blue using a Hewlett Packard scanjet scanner and SCANPLOT software
    • Vincent S.G., Cunningham P.R., Stephens N.L., Halayko A.J., Fisher J.T. Quantitative densitometry of proteins stained with coomassie blue using a Hewlett Packard scanjet scanner and SCANPLOT software. Electrophoresis. 18:1997;67-71.
    • (1997) Electrophoresis , vol.18 , pp. 67-71
    • Vincent, S.G.1    Cunningham, P.R.2    Stephens, N.L.3    Halayko, A.J.4    Fisher, J.T.5
  • 32
    • 0026289054 scopus 로고
    • Calcium-dependent mechanisms of regulation of smooth muscle contraction
    • Walsh M. Calcium-dependent mechanisms of regulation of smooth muscle contraction. Biochem. Cell. Biol. 69:1991;771-800.
    • (1991) Biochem. Cell. Biol. , vol.69 , pp. 771-800
    • Walsh, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.