메뉴 건너뛰기




Volumn 73, Issue 4, 1993, Pages 603-611

Ca2+ and segment length dependence of isometric force kinetics in intact ferret cardiac muscle

Author keywords

Ca2+ activation; Crossbridge kinetics; Force redevelopment; Segment length

Indexed keywords

CALCIUM ION; RYANODINE; TROPONIN; CALCIUM;

EID: 0027337513     PISSN: 00097330     EISSN: None     Source Type: Journal    
DOI: 10.1161/01.RES.73.4.603     Document Type: Article
Times cited : (38)

References (54)
  • 1
    • 0000244537 scopus 로고
    • Structural changes in the actin- and myosin-containing filaments during contraction
    • Huxley HE. Structural changes in the actin- and myosin-containing filaments during contraction. Cold Spring Harb Symp Quant Biol. 1973;37:361-376.
    • (1973) Cold Spring Harb Symp Quant Biol , vol.37 , pp. 361-376
    • Huxley, H.E.1
  • 2
    • 0023028948 scopus 로고
    • The role of tropomyosin-troponin in the regulation of skeletal muscle contraction
    • El-Saleh SC, Warber KD, Potter JD. The role of tropomyosin-troponin in the regulation of skeletal muscle contraction. J Muscle Res Cell Motil. 1986;7:387-404.
    • (1986) J Muscle Res Cell Motil , vol.7 , pp. 387-404
    • El-Saleh, S.C.1    Warber, K.D.2    Potter, J.D.3
  • 3
    • 0024007477 scopus 로고
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: Implications for regulation of muscle contraction
    • 2+ on cross-bridge turnover kinetics in skinned single rabbit psoas fibers: implications for regulation of muscle contraction. Proc Natl Acad Sci U S A. 1988;85:3265-3269.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 4
    • 0025061076 scopus 로고
    • Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: Implications for regulation of actin-myosin interaction
    • Sweeney HL, Stull JT. Alteration of cross-bridge kinetics by myosin light chain phosphorylation in rabbit skeletal muscle: implications for regulation of actin-myosin interaction. Proc Natl Acad Sci U S A. 1990;87:414-418.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 414-418
    • Sweeney, H.L.1    Stull, J.T.2
  • 5
    • 0025271805 scopus 로고
    • Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers
    • Metzger JM, Moss RL. Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers. Science. 1990; 247:1088-1090.
    • (1990) Science , vol.247 , pp. 1088-1090
    • Metzger, J.M.1    Moss, R.L.2
  • 6
    • 0025251785 scopus 로고
    • The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers: A steady-state and transient kinetic study
    • Millar NC, Homsher E. The effect of phosphate and calcium on force generation in glycerinated rabbit skeletal muscle fibers: a steady-state and transient kinetic study. J Biol Chem. 1990;265: 20234-20240.
    • (1990) J Biol Chem , vol.265 , pp. 20234-20240
    • Millar, N.C.1    Homsher, E.2
  • 7
    • 0022627157 scopus 로고
    • Comparison between the sarcomere length-force relations of intact and skinned trabeculae from rat right ventricle: Influence of calcium concentrations on these relations
    • Kentish JC, ter Keurs HEDJ, Ricciardi L, Bucx JJ, Noble MI. Comparison between the sarcomere length-force relations of intact and skinned trabeculae from rat right ventricle: influence of calcium concentrations on these relations. Circ Res. 1986;58: 755-768.
    • (1986) Circ Res , vol.58 , pp. 755-768
    • Kentish, J.C.1    Ter Keurs, H.E.D.J.2    Ricciardi, L.3    Bucx, J.J.4    Noble, M.I.5
  • 8
    • 0023280319 scopus 로고
    • Dynamic stiffness measured in central segment of excised rabbit papillary muscles during barium contracture
    • Shibata T, Hunter WC, Yang A, Sagawa K. Dynamic stiffness measured in central segment of excised rabbit papillary muscles during barium contracture. Circ Res. 1987;60:756-769.
    • (1987) Circ Res , vol.60 , pp. 756-769
    • Shibata, T.1    Hunter, W.C.2    Yang, A.3    Sagawa, K.4
  • 9
    • 0021315004 scopus 로고
    • 2+ in cross-bridge kinetics in chemically skinned rabbit psoas fibers
    • Pollack GH, Sugi H, eds. New York, NY: Plenum Publishing Corp
    • 2+ in cross-bridge kinetics in chemically skinned rabbit psoas fibers. In: Pollack GH, Sugi H, eds. Contractile Mechanisms in Muscle. New York, NY: Plenum Publishing Corp; 1984:657-672.
    • (1984) Contractile Mechanisms in Muscle , pp. 657-672
    • Kawai, M.1    Brandt, P.W.2    Cox, R.N.3
  • 10
    • 0026579874 scopus 로고
    • Effects of calcium on shortening velocity in frog chemically skinned atrial myocytes and in mechanically disrupted ventricular myocardium from rat
    • Hofmann PA, Moss RL. Effects of calcium on shortening velocity in frog chemically skinned atrial myocytes and in mechanically disrupted ventricular myocardium from rat. Circ Res. 1992;70: 885-892.
    • (1992) Circ Res , vol.70 , pp. 885-892
    • Hofmann, P.A.1    Moss, R.L.2
  • 11
    • 0020759723 scopus 로고
    • Myocardial segment velocity at a low load: Time, length, and calcium dependence
    • Martyn DA, Rondinone JF, Huntsman LL. Myocardial segment velocity at a low load: time, length, and calcium dependence. Am J Physiol. 1983;244:H708-H714.
    • (1983) Am J Physiol , vol.244
    • Martyn, D.A.1    Rondinone, J.F.2    Huntsman, L.L.3
  • 12
    • 0026101345 scopus 로고
    • Sarcomere dynamics in cat cardiac trabeculae
    • de Tombe PP, ter Keurs HEDJ. Sarcomere dynamics in cat cardiac trabeculae. Circ Res. 1991;68:588-596.
    • (1991) Circ Res , vol.68 , pp. 588-596
    • De Tombe, P.P.1    Ter Keurs, H.E.D.J.2
  • 13
    • 0023235979 scopus 로고
    • Force, velocity, and power changes during normal and potentiated contractions of cat papillary muscle
    • Chiu YC, Ballou EW, Ford LE. Force, velocity, and power changes during normal and potentiated contractions of cat papillary muscle. Circ Res. 1987;60:446-458.
    • (1987) Circ Res , vol.60 , pp. 446-458
    • Chiu, Y.C.1    Ballou, E.W.2    Ford, L.E.3
  • 14
    • 0026709820 scopus 로고
    • An internal viscous element limits unloaded velocity of sarcomere shortening in rat myocardium
    • de Tombe PP, ter Keurs HEDJ. An internal viscous element limits unloaded velocity of sarcomere shortening in rat myocardium. J Physiol (Lond). 1992;454:619-642.
    • (1992) J Physiol (Lond) , vol.454 , pp. 619-642
    • De Tombe, P.P.1    Ter Keurs, H.E.D.J.2
  • 16
    • 0018926010 scopus 로고
    • Effects of calcium on the sarcomere length-tension relation in rat cardiac muscle
    • Gordon AM, Pollack GH. Effects of calcium on the sarcomere length-tension relation in rat cardiac muscle. Circ Res. 1980;47: 610-619.
    • (1980) Circ Res , vol.47 , pp. 610-619
    • Gordon, A.M.1    Pollack, G.H.2
  • 18
    • 0015530342 scopus 로고
    • X-ray diffraction studies on skinned single fibres of frog skeletal muscle
    • Matsubara I, Elliot GH. X-ray diffraction studies on skinned single fibres of frog skeletal muscle. J Mol Biol. 1972;72:657-669.
    • (1972) J Mol Biol , vol.72 , pp. 657-669
    • Matsubara, I.1    Elliot, G.H.2
  • 19
    • 0020000435 scopus 로고
    • Calcium- and length-dependent force production in rat ventricular muscle
    • Hibberd MG, Jewell BR. Calcium- and length-dependent force production in rat ventricular muscle. J Physiol (Lond). 1982;329: 527-540.
    • (1982) J Physiol (Lond) , vol.329 , pp. 527-540
    • Hibberd, M.G.1    Jewell, B.R.2
  • 20
    • 0022929836 scopus 로고
    • 2+-activated force elicited by tetanization of ferret papillary muscle and whole heart: Mechanism and characteristics of steady contractile activation in intact myocardium
    • 2+-activated force elicited by tetanization of ferret papillary muscle and whole heart: mechanism and characteristics of steady contractile activation in intact myocardium. Circ Res. 1986;59:262-269.
    • (1986) Circ Res , vol.59 , pp. 262-269
    • Marban, E.1    Kusuoka, H.2    Yue, D.T.3    Weisfeldt, M.L.4    Wier, W.G.5
  • 22
    • 0017550206 scopus 로고
    • Nonuniform contraction in the isolated cat papillary muscle
    • Huntsman LL, Day SR, Stewart DK. Nonuniform contraction in the isolated cat papillary muscle. Am J Physiol. 1977;233: H613-H616.
    • (1977) Am J Physiol , vol.233
    • Huntsman, L.L.1    Day, S.R.2    Stewart, D.K.3
  • 23
    • 0016818556 scopus 로고
    • Myocardial sarcomere dynamics during isometric contraction
    • Kreuger JW, Pollack GH. Myocardial sarcomere dynamics during isometric contraction. J Physiol (Lond). 1975;251:627-643.
    • (1975) J Physiol (Lond) , vol.251 , pp. 627-643
    • Kreuger, J.W.1    Pollack, G.H.2
  • 24
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomyosin ATPase activity in solution
    • Brenner B, Eisenberg E. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc Natl Acad Sci U S A. 1986:83:3542-3546.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 25
    • 0017412670 scopus 로고
    • Swelling of skinned muscle fibers of the frog: Experimental observations
    • Godt RE, Maughan DW. Swelling of skinned muscle fibers of the frog: experimental observations. Biophys J. 1977;19:103-116.
    • (1977) Biophys J , vol.19 , pp. 103-116
    • Godt, R.E.1    Maughan, D.W.2
  • 26
    • 0022407356 scopus 로고
    • Equatorial X-ray diffraction from single skinned rabbit psoas fibres at various degrees of activation
    • Brenner B, Yu LC. Equatorial X-ray diffraction from single skinned rabbit psoas fibres at various degrees of activation. Biophys J. 1985;48:829-834.
    • (1985) Biophys J , vol.48 , pp. 829-834
    • Brenner, B.1    Yu, L.C.2
  • 27
    • 85034940190 scopus 로고
    • Lack of activation dependence of force redevelopment kinetics in skinned muscle fibers with activating troponin C
    • Abstract
    • Chase PB, Martyn DA, Hannon JD. Lack of activation dependence of force redevelopment kinetics in skinned muscle fibers with activating troponin C. Biophys J. 1993;64:A345. Abstract.
    • (1993) Biophys J , vol.64
    • Chase, P.B.1    Martyn, D.A.2    Hannon, J.D.3
  • 28
    • 0017385529 scopus 로고
    • Tension responses to sudden length change in stimulated frog muscle fibres near slack length
    • Ford LE, Huxley AF, Simmons RM. Tension responses to sudden length change in stimulated frog muscle fibres near slack length. J Physiol (Lond). 1977;269:441-515.
    • (1977) J Physiol (Lond) , vol.269 , pp. 441-515
    • Ford, L.E.1    Huxley, A.F.2    Simmons, R.M.3
  • 30
    • 84912589827 scopus 로고
    • Fast response of cardiac muscle to quick length changes
    • Sugi H, Pollack GH, eds. Tokyo, Japan: University of Tokyo Press
    • Delay MJ, Vassallo DV, Iwazumi T, Pollack GH. Fast response of cardiac muscle to quick length changes. In: Sugi H, Pollack GH, eds. Crossbridge Mechanisms in Muscle Contraction. Tokyo, Japan: University of Tokyo Press; 1979:71-83.
    • (1979) Crossbridge Mechanisms in Muscle Contraction , pp. 71-83
    • Delay, M.J.1    Vassallo, D.V.2    Iwazumi, T.3    Pollack, G.H.4
  • 31
    • 85034942019 scopus 로고
    • Measurement of segment stiffness in cardiac muscle
    • Abstract
    • Martyn DA, Huntsman LL. Measurement of segment stiffness in cardiac muscle. Biophys J. 1986;49:81a. Abstract.
    • (1986) Biophys J , vol.49
    • Martyn, D.A.1    Huntsman, L.L.2
  • 32
    • 5944248909 scopus 로고
    • Rapid tension recovery in response to shortening steps following a cycle of ramp shortening and large restretch in skinned rabbit psoas fibers
    • Abstract
    • Burton K. Rapid tension recovery in response to shortening steps following a cycle of ramp shortening and large restretch in skinned rabbit psoas fibers. Biophys J. 1991;59:35a. Abstract.
    • (1991) Biophys J , vol.59
    • Burton, K.1
  • 33
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers
    • Metzger JM, Greaser ML, Moss RL. Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. J Gen Physiol. 1989;93: 855-883.
    • (1989) J Gen Physiol , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 34
    • 0023074678 scopus 로고
    • ATPase activity of intact single muscle fibres of Xenopus laevis is related to the rate of force redevelopment after rapid shortening
    • Jacob R, Just H, Holubarsch C, eds. Cardiac Energetics: Basic Mechanisms and Clinical Implications. New York, NY: Springer-Verlag New York, Inc
    • Stienen GJM, Lannergren J, Elzinga G. ATPase activity of intact single muscle fibres of Xenopus laevis is related to the rate of force redevelopment after rapid shortening. In: Jacob R, Just H, Holubarsch C, eds. Cardiac Energetics: Basic Mechanisms and Clinical Implications. New York, NY: Springer-Verlag New York, Inc; 1987;suppl 2 to Basic Res Cardiol (vol 82):111-117.
    • (1987) Basic Res Cardiol , vol.82 , Issue.2 SUPPL. , pp. 111-117
    • Stienen, G.J.M.1    Lannergren, J.2    Elzinga, G.3
  • 35
    • 0025228949 scopus 로고
    • 2+ sensitivity of myofibrillar ATPase activity in skinned fibres from pig ventricles
    • 2+ sensitivity of myofibrillar ATPase activity in skinned fibres from pig ventricles. Pflugers Arch. 1990;415:741-746.
    • (1990) Pflugers Arch , vol.415 , pp. 741-746
    • Kuhn, H.J.1    Bletz, C.2    Ruegg, J.C.3
  • 36
    • 0023488538 scopus 로고
    • Evidence for a force-dependent component of calcium binding to cardiac troponin C
    • Hofmann PA, Fuchs F. Evidence for a force-dependent component of calcium binding to cardiac troponin C. Am J Physiol. 1987;253:C541-C546.
    • (1987) Am J Physiol , vol.253
    • Hofmann, P.A.1    Fuchs, F.2
  • 37
    • 0026319614 scopus 로고
    • 2+-troponin C affinity in skeletal muscle
    • 2+-troponin C affinity in skeletal muscle. Am J Physiol. 1991;261:C787-C792.
    • (1991) Am J Physiol , vol.261
    • Fuchs, F.1    Wang, Y.P.2
  • 38
    • 0020002214 scopus 로고
    • The effects of muscle length on intracellular calcium transients in mammalian cardiac muscle
    • Allen DG, Kurihara S. The effects of muscle length on intracellular calcium transients in mammalian cardiac muscle. J Physiol (Lond). 1982;327:79-94.
    • (1982) J Physiol (Lond) , vol.327 , pp. 79-94
    • Allen, D.G.1    Kurihara, S.2
  • 39
    • 0020549120 scopus 로고
    • Active shortening retards the decline of the intracellular calcium transient in mammalian heart muscle
    • Housmans PR, Lee NKM, Blinks JR. Active shortening retards the decline of the intracellular calcium transient in mammalian heart muscle. Science. 1983;221:159-161.
    • (1983) Science , vol.221 , pp. 159-161
    • Housmans, P.R.1    Lee, N.K.M.2    Blinks, J.R.3
  • 40
    • 0027512192 scopus 로고
    • Fluorescent properties of rat cardiac trabeculae microinjected with fura-2 salt
    • Backx PH, ter Keurs HEDJ. Fluorescent properties of rat cardiac trabeculae microinjected with fura-2 salt. Am J Physiol. 1993;264: H1098-H1110.
    • (1993) Am J Physiol , vol.264
    • Backx, P.H.1    Ter Keurs, H.E.D.J.2
  • 41
    • 0027418357 scopus 로고
    • Alterations in intracellular calcium and tension of activated ferret papillary muscle in response to step length changes
    • Saeki Y, Kurihara S, Hongo K, Tanaka E. Alterations in intracellular calcium and tension of activated ferret papillary muscle in response to step length changes. J Physiol (Lond). 1993;463: 291-306.
    • (1993) J Physiol (Lond) , vol.463 , pp. 291-306
    • Saeki, Y.1    Kurihara, S.2    Hongo, K.3    Tanaka, E.4
  • 42
    • 0024242326 scopus 로고
    • Calcium concentration in the myoplasm of skinned ferret ventricular muscle following changes in muscle length
    • Allen DG, Kentish JC. Calcium concentration in the myoplasm of skinned ferret ventricular muscle following changes in muscle length. J Physiol (Lond). 1988;407:489-503.
    • (1988) J Physiol (Lond) , vol.407 , pp. 489-503
    • Allen, D.G.1    Kentish, J.C.2
  • 43
    • 0023472695 scopus 로고
    • Extra calcium on shortening in barnacle muscle: Is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length?
    • Gordon AM, Ridgway EB. Extra calcium on shortening in barnacle muscle: is the decrease in calcium binding related to decreased cross-bridge attachment, force, or length? J Gen Physiol. 1987;90:321-340.
    • (1987) J Gen Physiol , vol.90 , pp. 321-340
    • Gordon, A.M.1    Ridgway, E.B.2
  • 44
    • 0021363595 scopus 로고
    • Muscle calcium transient: Effect of post-stimulus length changes in single fibers
    • Ridgway EB, Gordon AM. Muscle calcium transient: effect of post-stimulus length changes in single fibers. J Gen Physiol. 1984; 83:75-103.
    • (1984) J Gen Physiol , vol.83 , pp. 75-103
    • Ridgway, E.B.1    Gordon, A.M.2
  • 45
    • 0023042009 scopus 로고
    • Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction
    • Kress M, Huxley HE, Faruqi AR. Structural changes during activation of frog muscle studied by time-resolved X-ray diffraction. J Mol Biol. 1986;188:325-342.
    • (1986) J Mol Biol , vol.188 , pp. 325-342
    • Kress, M.1    Huxley, H.E.2    Faruqi, A.R.3
  • 47
    • 0025824168 scopus 로고
    • 2+-sensitive cross-bridge state transition in skeletal muscle fibers: Effects due to variations in thin filament activation by extraction of troponin C
    • 2+-sensitive cross-bridge state transition in skeletal muscle fibers: effects due to variations in thin filament activation by extraction of troponin C. J Gen Physiol. 1991;98:233-248.
    • (1991) J Gen Physiol , vol.98 , pp. 233-248
    • Metzger, J.M.1    Moss, R.L.2
  • 48
    • 0026646783 scopus 로고
    • Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle
    • Metzger JM, Moss RL. Myosin light chain 2 modulates calcium-sensitive cross-bridge transitions in vertebrate skeletal muscle. Biophys J. 1992;63:460-468.
    • (1992) Biophys J , vol.63 , pp. 460-468
    • Metzger, J.M.1    Moss, R.L.2
  • 49
    • 0018873792 scopus 로고
    • Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene
    • Wilkinson JM. Troponin C from rabbit slow skeletal and cardiac muscle is the product of a single gene. Eur J Biochem. 1980;103: 179-188.
    • (1980) Eur J Biochem , vol.103 , pp. 179-188
    • Wilkinson, J.M.1
  • 50
    • 0021153417 scopus 로고
    • Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated
    • Lompre A-M, Nadal-Ginard B, Mahdavi V. Expression of the cardiac ventricular α- and β-myosin heavy chain genes is developmentally and hormonally regulated. J Biol Chem. 1984;259: 6437-6446.
    • (1984) J Biol Chem , vol.259 , pp. 6437-6446
    • Lompre, A.-M.1    Nadal-Ginard, B.2    Mahdavi, V.3
  • 51
    • 0026774946 scopus 로고
    • Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers
    • Swartz DR, Moss RL. Influence of a strong-binding myosin analogue on calcium-sensitive mechanical properties of skinned skeletal muscle fibers. J Biol Chem. 1992;267:20497-20506.
    • (1992) J Biol Chem , vol.267 , pp. 20497-20506
    • Swartz, D.R.1    Moss, R.L.2
  • 52
    • 25944460202 scopus 로고
    • Activation of skinned skeletal muscle fibers by N-ethylmaleimide-modified-S1 versus calcium-activation
    • Abstract
    • Kraft T, Schnekenbuhl S, Messerli M, Yu LC, Chalovich JM, Brenner B. Activation of skinned skeletal muscle fibers by N-ethylmaleimide-modified-S1 versus calcium-activation. Biophys J. 1993;64:A346. Abstract.
    • (1993) Biophys J , vol.64
    • Kraft, T.1    Schnekenbuhl, S.2    Messerli, M.3    Yu, L.C.4    Chalovich, J.M.5    Brenner, B.6
  • 53
    • 0027479115 scopus 로고
    • Formation of inter- and intramolecular disulfide bonds can activate cardiac troponin C
    • Putkey JA, Dotson DG, Mouawad P. Formation of inter- and intramolecular disulfide bonds can activate cardiac troponin C. J Biol Chem. 1993;268:6827-6830.
    • (1993) J Biol Chem , vol.268 , pp. 6827-6830
    • Putkey, J.A.1    Dotson, D.G.2    Mouawad, P.3
  • 54
    • 0027205101 scopus 로고
    • Calcium-independent activation of skeletal muscle fibers by a modified form of cardiac Troponin C
    • Hannon JD, Chase PB, Martyn DA, Huntsman LL, Kushmeric MJ, Gordon AM. Calcium-independent activation of skeletal muscle fibers by a modified form of cardiac Troponin C. Biophys J. 1993;64:1632-1637.
    • (1993) Biophys J , vol.64 , pp. 1632-1637
    • Hannon, J.D.1    Chase, P.B.2    Martyn, D.A.3    Huntsman, L.L.4    Kushmeric, M.J.5    Gordon, A.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.