메뉴 건너뛰기




Volumn 433, Issue 1-2, 1996, Pages 42-48

Regulation of force and shortening velocity by calcium and myosin phosphorylation in chemically skinned smooth muscle

Author keywords

Force velocity relation; Myosin light chain phosphorylation; Okadaic acid; Skinned fibres

Indexed keywords

CALCIUM; MYOSIN LIGHT CHAIN; OKADAIC ACID;

EID: 0029806862     PISSN: 00316768     EISSN: None     Source Type: Journal    
DOI: 10.1007/s004240050246     Document Type: Article
Times cited : (8)

References (46)
  • 1
    • 0023323023 scopus 로고
    • Force-velocity relation and rate of ATP hydrolysis in osmotically compressed skinned smooth muscle of the guinea pig
    • Arheden H, Arner A, Hellstrand P (1986) Force-velocity relation and rate of ATP hydrolysis in osmotically compressed skinned smooth muscle of the guinea pig. J Muscle Res Cell Motil 8:151-160
    • (1986) J Muscle Res Cell Motil , vol.8 , pp. 151-160
    • Arheden, H.1    Arner, A.2    Hellstrand, P.3
  • 2
    • 0020392227 scopus 로고
    • Mechanical characteristics of chemically skinned guinea-pig taenia coli
    • Arner A (1982) Mechanical characteristics of chemically skinned guinea-pig taenia coli. Pflügers Arch 395:277-284
    • (1982) Pflügers Arch , vol.395 , pp. 277-284
    • Arner, A.1
  • 4
    • 0022034172 scopus 로고
    • Effects of calcium and substrate on force-velocity relation and energy turnover in skinned smooth muscle of the guinea pig
    • Lond
    • Arner A, Hellstrand P (1985) Effects of calcium and substrate on force-velocity relation and energy turnover in skinned smooth muscle of the guinea pig. J Physiol (Lond) 360:347-365
    • (1985) J Physiol , vol.360 , pp. 347-365
    • Arner, A.1    Hellstrand, P.2
  • 5
    • 0022271366 scopus 로고
    • 2+ on force-velocity characteristics of normal and hypertrophic smooth muscle of the rat portal vein
    • 2+ on force-velocity characteristics of normal and hypertrophic smooth muscle of the rat portal vein. Acta Physiol Scand 124: 525-533
    • (1985) Acta Physiol Scand , vol.124 , pp. 525-533
    • Arner, A.1    Malmqvist, U.2    Uvelius, B.3
  • 6
    • 0023461923 scopus 로고
    • Influence of ATP, ADP and AMPPNP on the energetics of contraction in skinned smooth muscle
    • Siegman MJ, Somlyo AP, Stephens NL (eds) Liss, New York
    • Arner A, Hellstrand P, Rüegg JC (1987) Influence of ATP, ADP and AMPPNP on the energetics of contraction in skinned smooth muscle. In: Siegman MJ, Somlyo AP, Stephens NL (eds) Regulation and contraction of smooth muscle. Liss, New York, pp 43-57
    • (1987) Regulation and Contraction of Smooth Muscle , pp. 43-57
    • Arner, A.1    Hellstrand, P.2    Rüegg, J.C.3
  • 9
    • 0019433353 scopus 로고
    • Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle
    • Dillon PF, Aksoy MO, Driska SP, Murphy RA (1981) Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle. Science 211:495-497
    • (1981) Science , vol.211 , pp. 495-497
    • Dillon, P.F.1    Aksoy, M.O.2    Driska, S.P.3    Murphy, R.A.4
  • 10
    • 0019769492 scopus 로고
    • Myoplasmic free calcium concentration reached during twitch of an intact isolated cardiac cell and during calcium induced release of calcium from the sacroplasmatic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle
    • Fabiato A (1981) Myoplasmic free calcium concentration reached during twitch of an intact isolated cardiac cell and during calcium induced release of calcium from the sacroplasmatic reticulum of a skinned cardiac cell from the adult rat or rabbit ventricle. J Gen Physiol 78:457-197
    • (1981) J Gen Physiol , vol.78 , pp. 457-1197
    • Fabiato, A.1
  • 11
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • Paris
    • Fabiato A, Fabiato A (1979) Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J Physiol (Paris) 75:463-505
    • (1979) J Physiol , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, A.2
  • 12
    • 0000387235 scopus 로고
    • A rapidly convergent descent method for minimization
    • Fletcher R, Powell JD (1963) A rapidly convergent descent method for minimization. Computer J 6:163-168
    • (1963) Computer J , vol.6 , pp. 163-168
    • Fletcher, R.1    Powell, J.D.2
  • 14
    • 0023841161 scopus 로고
    • Cross-bridge phosphorylation and regulation of latch state in smooth muscle
    • Hai CM, Murphy RA (1988) Cross-bridge phosphorylation and regulation of latch state in smooth muscle. Am J Physiol 254:C99-C106
    • (1988) Am J Physiol , vol.254
    • Hai, C.M.1    Murphy, R.A.2
  • 15
    • 0023766453 scopus 로고
    • Regulation of shortening velocity by cross-bridge phosphorylation in smooth muscle
    • Hai CM, Murphy RA (1988) Regulation of shortening velocity by cross-bridge phosphorylation in smooth muscle. Am J Physiol 255:C86-C94
    • (1988) Am J Physiol , vol.255
    • Hai, C.M.1    Murphy, R.A.2
  • 16
    • 0025743094 scopus 로고
    • Okadaic acid stimulates the ATP-dependent interaction between actin and myosin of smooth muscle via a direct effect on myosin
    • Hayakawa K, Okagaki T, Dobashi T, Sakanishi A, Kaneko K, Kohama K (1991) Okadaic acid stimulates the ATP-dependent interaction between actin and myosin of smooth muscle via a direct effect on myosin. Biochem Biophys Res Commun 177: 1155-1160
    • (1991) Biochem Biophys Res Commun , vol.177 , pp. 1155-1160
    • Hayakawa, K.1    Okagaki, T.2    Dobashi, T.3    Sakanishi, A.4    Kaneko, K.5    Kohama, K.6
  • 17
    • 0022382511 scopus 로고
    • Myosin light chain phosphorylation and the cross-bridge cycle at low substrate concentration in chemically skinned guinea pig taenia coli
    • Hellstrand P, Arner A (1985) Myosin light chain phosphorylation and the cross-bridge cycle at low substrate concentration in chemically skinned guinea pig taenia coli. Pflügers Arch 405:323-328
    • (1985) Pflügers Arch , vol.405 , pp. 323-328
    • Hellstrand, P.1    Arner, A.2
  • 18
    • 0000682154 scopus 로고
    • The heat of shortening and the dynamic constants of shortening
    • Hill AV (1938) The heat of shortening and the dynamic constants of shortening. Proc Roy Soc [Biol] 126:136-195
    • (1938) Proc Roy Soc [Biol] , vol.126 , pp. 136-195
    • Hill, A.V.1
  • 19
    • 0024471761 scopus 로고
    • 2+ sensitivities of guinea-pig ileum and rabbit pulmonary artery smooth muscle
    • Lond
    • 2+ sensitivities of guinea-pig ileum and rabbit pulmonary artery smooth muscle. J Physiol (Lond) 413:489-503
    • (1989) J Physiol , vol.413 , pp. 489-503
    • Himpens, B.1    Matthijs, G.2    Somlyo, A.P.3
  • 21
    • 0024550123 scopus 로고
    • Regulation of smooth muscle contractile elements by second messengers
    • Kamm KE, Stull JT (1989) Regulation of smooth muscle contractile elements by second messengers. Annu Rev Physiol 51:299-313
    • (1989) Annu Rev Physiol , vol.51 , pp. 299-313
    • Kamm, K.E.1    Stull, J.T.2
  • 22
    • 0025339250 scopus 로고
    • Temporal relationship between force. ATPase activity, and myosin phosphorylation during a contraction/relaxation cycle in a skinned smooth muscle
    • Kühn H, Tewes A, Gagelmann M, Güth K, Arner A, Rüegg JC (1990). Temporal relationship between force. ATPase activity, and myosin phosphorylation during a contraction/relaxation cycle in a skinned smooth muscle. Pflügers Arch 416:512-518
    • (1990) Pflügers Arch , vol.416 , pp. 512-518
    • Kühn, H.1    Tewes, A.2    Gagelmann, M.3    Güth, K.4    Arner, A.5    Rüegg, J.C.6
  • 24
    • 10544241200 scopus 로고
    • Effects of calcium and myosin light chain phosphorylation on the force-velocity relation in smooth muscle
    • Malmqvist U, Arner A (1993) Effects of calcium and myosin light chain phosphorylation on the force-velocity relation in smooth muscle. Biophys J 64:A257
    • (1993) Biophys J , vol.64
    • Malmqvist, U.1    Arner, A.2
  • 25
    • 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 (1996) The effects of caldesmon extraction on mechanical properties of skinned smooth muscle fibre preparations. Pflügers Arch 432: 241-247
    • (1996) Pflügers Arch , vol.432 , pp. 241-247
    • Malmqvist, U.1    Arner, A.2    Makuch, R.3    Dabrowska, R.4
  • 26
    • 0018837552 scopus 로고
    • Calcium ion-regulated thin from vascular smooth muscle
    • Marston SB, Trevett R, Walters M (1980) Calcium ion-regulated thin from vascular smooth muscle. Biochem J 185:355-365
    • (1980) Biochem J , vol.185 , pp. 355-365
    • Marston, S.B.1    Trevett, R.2    Walters, M.3
  • 27
    • 0026009590 scopus 로고
    • Force-velocity relation and myosin light chain phosphorylation in bovine coronary arterial smooth muscle
    • Miller-Hance WC, Kamm KE (1991) Force-velocity relation and myosin light chain phosphorylation in bovine coronary arterial smooth muscle. Circ Res 69:1207-1214
    • (1991) Circ Res , vol.69 , pp. 1207-1214
    • Miller-Hance, W.C.1    Kamm, K.E.2
  • 28
    • 0027408994 scopus 로고
    • The effects of Mg ADP on cross-bridge kinetics: A laser flash photolysis study of guinea-pig smooth muscle
    • Lond
    • Nishiye E, Somlyo AV, Török K, Somlyo AP (1993) The effects of Mg ADP on cross-bridge kinetics: a laser flash photolysis study of guinea-pig smooth muscle. J Physiol (Lond) 460:247-271
    • (1993) J Physiol , vol.460 , pp. 247-271
    • Nishiye, E.1    Somlyo, A.V.2    Török, K.3    Somlyo, A.P.4
  • 29
    • 0028967798 scopus 로고
    • Effects of inorganic phosphate on cross-bridge kinetics at different activation levels in skinned guinea-pig smooth muscle
    • Lond
    • Österman Å, Arner A (1995) Effects of inorganic phosphate on cross-bridge kinetics at different activation levels in skinned guinea-pig smooth muscle. J Physiol (Lond) 482:369-383
    • (1995) J Physiol , vol.482 , pp. 369-383
    • Österman, Å.1    Arner, A.2
  • 30
    • 0027160263 scopus 로고
    • Effects of 2,3-butanedione monoxime on activation of contraction and cross-bridge kinetics in intact and chemically skinned smooth muscle fibres from guinea pig taenia coli
    • Osterman A, Arner A, Malmqvist U (1993) Effects of 2,3-butanedione monoxime on activation of contraction and cross-bridge kinetics in intact and chemically skinned smooth muscle fibres from guinea pig taenia coli. J Muscle Res Cell Motil 14:186-194
    • (1993) J Muscle Res Cell Motil , vol.14 , pp. 186-194
    • Osterman, A.1    Arner, A.2    Malmqvist, U.3
  • 32
    • 0020562525 scopus 로고
    • 2+, calmodulin, and duration of contraction in "chemically skinned" smooth muscle
    • 2+, calmodulin, and duration of contraction in "chemically skinned" smooth muscle. Circ Res 53:342-351
    • (1983) Circ Res , vol.53 , pp. 342-351
    • Paul, R.J.1    Doerman, G.2    Zeugner, C.3    Rüegg, J.C.4
  • 33
    • 0025197314 scopus 로고
    • 2+] sensitivity of myosin phosphorylation in intact swine arterial smooth muscle
    • Lond
    • 2+] sensitivity of myosin phosphorylation in intact swine arterial smooth muscle. J Physiol (Lond) 429:77-94
    • (1990) J Physiol , vol.429 , pp. 77-94
    • Rembold, C.M.1
  • 34
    • 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 63:593-603
    • (1988) Circ Res , vol.63 , pp. 593-603
    • Rembold, C.M.1    Murphy, R.A.2
  • 35
    • 0027255857 scopus 로고
    • Models of the mechanism for cross-bridge attachment in smooth muscle
    • Rembold CM, Murphy RA (1993) Models of the mechanism for cross-bridge attachment in smooth muscle. J Muscle Res Cell Motil 14:325-333
    • (1993) J Muscle Res Cell Motil , vol.14 , pp. 325-333
    • Rembold, C.M.1    Murphy, R.A.2
  • 36
    • 0014981534 scopus 로고
    • Smooth muscle tone
    • Rüegg JC (1971) Smooth muscle tone. Physiol Rev 51:201-248
    • (1971) Physiol Rev , vol.51 , pp. 201-248
    • Rüegg, J.C.1
  • 37
    • 0022341943 scopus 로고
    • Light chain phosphorylation regulates the movement of smooth muscle on actin filaments
    • Sellers JR, Spudich JA, Sheetz MP (1985) Light chain phosphorylation regulates the movement of smooth muscle on actin filaments. J Cell Biol 101:1897-1902
    • (1985) J Cell Biol , vol.101 , pp. 1897-1902
    • Sellers, J.R.1    Spudich, J.A.2    Sheetz, M.P.3
  • 39
    • 0024323715 scopus 로고
    • Phosphatase inhibition with okadaic acid does not alter the relationship between force and myosin light chain phosphorylation in permeabilized smooth muscle
    • Siegman MJ, Butler TM, Moors SU (1989) Phosphatase inhibition with okadaic acid does not alter the relationship between force and myosin light chain phosphorylation in permeabilized smooth muscle. Biochem Biophys Res Commun 161:838-842
    • (1989) Biochem Biophys Res Commun , vol.161 , pp. 838-842
    • Siegman, M.J.1    Butler, T.M.2    Moors, S.U.3
  • 40
    • 0038860948 scopus 로고
    • Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin
    • Sobue K, Muramoto Y, Fujita M, Kakiuchi S (1981) Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc Natl Acad Sci USA 78:5652-5655
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 5652-5655
    • Sobue, K.1    Muramoto, Y.2    Fujita, M.3    Kakiuchi, S.4
  • 41
    • 0023832001 scopus 로고
    • Cross-bridge kinetics, cooperatively, and negatively strained cross-bridges in vertebrate smooth muscle. A laser flash photolysis study
    • Somlyo AV, Goldman YE, Fujimori T, Bond M, Trentham DR, Somlyo AP (1988) Cross-bridge kinetics, cooperatively, and negatively strained cross-bridges in vertebrate smooth muscle. A laser flash photolysis study. Journal of General Physiology 91: 165-192
    • (1988) Journal of General Physiology , vol.91 , pp. 165-192
    • Somlyo, A.V.1    Goldman, Y.E.2    Fujimori, T.3    Bond, M.4    Trentham, D.R.5    Somlyo, A.P.6
  • 42
    • 0024585166 scopus 로고
    • Phosphorylation of caldesinon prevents its interaction with smooth muscle myosin
    • Sutherland C, Walsh MP (1989) Phosphorylation of caldesinon prevents its interaction with smooth muscle myosin. J Biol Chem 264:578-583
    • (1989) J Biol Chem , vol.264 , pp. 578-583
    • Sutherland, C.1    Walsh, M.P.2
  • 43
    • 0023648079 scopus 로고
    • Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin
    • Takai A, Bialojan C, Troschka M, Rüegg JC (1987) Smooth muscle myosin phosphatase inhibition and force enhancement by black sponge toxin. FEBS Lett 217:81-84
    • (1987) FEBS Lett , vol.217 , pp. 81-84
    • Takai, A.1    Bialojan, C.2    Troschka, M.3    Rüegg, J.C.4
  • 44
    • 0023232078 scopus 로고
    • Effect of low extracellular calcium on shortening velocity in isolated single smooth muscle cells
    • Warshaw DM, Work SS, McBride WJ (1987) Effect of low extracellular calcium on shortening velocity in isolated single smooth muscle cells. Pflügers Arch 410:185-191
    • (1987) Pflügers Arch , vol.410 , pp. 185-191
    • Warshaw, D.M.1    Work, S.S.2    McBride, W.J.3
  • 45
    • 0025335344 scopus 로고
    • Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro
    • Warshaw DM, Desrosiers JM, Work SS, Tryhus KM (1990) Smooth muscle myosin cross-bridge interactions modulate actin filament sliding velocity in vitro. J Cell Biol 111:453-463
    • (1990) J Cell Biol , vol.111 , pp. 453-463
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Tryhus, K.M.4
  • 46
    • 0026348646 scopus 로고
    • Effects of MgATP, MgADP, and Pi on actin movement by smooth muscle myosin
    • Warshaw DM, Desrosiers JM, Work SS, Trybus KM (1991) Effects of MgATP, MgADP, and Pi on actin movement by smooth muscle myosin. J Biol Chem 166:24339-24343
    • (1991) J Biol Chem , vol.166 , pp. 24339-24343
    • Warshaw, D.M.1    Desrosiers, J.M.2    Work, S.S.3    Trybus, K.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.