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Volumn 34, Issue 5, 2002, Pages 547-554

Length dependence of cardiac myofilament Ca2+ sensitivity in the presence of substitute nucleoside triphosphates

Author keywords

Ca2+ sensitivity; Length dependence; Myofilaments; Nucleoside triphosphates; Thin filament activation

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM MAGNESIUM); ADENOSINE TRIPHOSPHATE; ADENOSINE TRIPHOSPHATE MAGNESIUM; CALCIUM ION; MYOSIN; NUCLEOSIDE TRIPHOSPHATE; URIDINE TRIPHOSPHATE;

EID: 0036586484     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmcc.2002.1537     Document Type: Article
Times cited : (6)

References (36)
  • 1
    • 0022393490 scopus 로고
    • The cellular basis of the length-tension relation in cardiac muscle
    • ALLEN DG. KENTISH JC. The cellular basis of the length-tension relation in cardiac muscle. J Mol Cell Cardiol 1985: 17: 821-840.
    • (1985) J Mol Cell Cardiol , vol.17 , pp. 821-840
    • Allen, D.G.1    Kentish, J.C.2
  • 2
    • 21844517087 scopus 로고
    • 2+ regulatory protein complex in cardiac muscle
    • 2+ regulatory protein complex in cardiac muscle. News Physiol Sci 1995: 10: 106-112.
    • (1995) News Physiol Sci , vol.10 , pp. 106-112
    • Fuchs, F.1
  • 3
    • 0032944254 scopus 로고    scopus 로고
    • The role of calcium in the response of cardiac muscle to stretch
    • CALAGHAN SC. WHITE E. The role of calcium in the response of cardiac muscle to stretch. Prog Biophys Mol Biol 1999; 71: 59-90.
    • (1999) Prog Biophys Mol Biol , vol.71 , pp. 59-90
    • Calaghan, S.C.1    White, E.2
  • 4
    • 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
  • 6
    • 0023694749 scopus 로고
    • Bound calcium and force development in skinned cardiac muscle bundles: Effect of sarcomere length
    • HOFMANN PA, FUCHS F. Bound calcium and force development in skinned cardiac muscle bundles: effect of sarcomere length. J Mol Cell Cardiol 1988; 20: 667-677.
    • (1988) J Mol Cell Cardiol , vol.20 , pp. 667-677
    • Hofmann, P.A.1    Fuchs, F.2
  • 7
    • 0027974349 scopus 로고
    • 2+-troponin C affinity in cardiac and slow skeletal muscle
    • 2+-troponin C affinity in cardiac and slow skeletal muscle. Am J Physiol 1994; 266: C1077-C1082.
    • (1994) Am J Physiol , vol.266
    • Wang, Y.P.1    Fuchs, F.2
  • 8
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • TOBACMAN LS. Thin filament-mediated regulation of cardiac contraction. Ann Rev Physiol 1996; 58: 447-481.
    • (1996) Ann Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 9
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • SOLARO RJ, RARICK HM. Troponin and tropomyosin: proteins that switch on and tune in the activity of cardiac myofilaments. Circ Res 1998; 83: 471-480.
    • (1998) Circ Res , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.M.2
  • 10
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • GORDON AM, HOMSHER E, REGNIER M. Regulation of contraction in striated muscle. Physiol Rev 2000; 80: 853-924.
    • (2000) Physiol Rev , vol.80 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 11
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • MCKILLOP DFA, GEEVES MA. Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament. Biophys J 1993; 65: 693-701.
    • (1993) Biophys J , vol.65 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 13
    • 0031566964 scopus 로고    scopus 로고
    • Steric model for activation of muscle thin filaments
    • VIBERT P, CRAIG R, LEHMAN W. Steric model for activation of muscle thin filaments. J Mol Biol 1997; 266: 8-14.
    • (1997) J Mol Biol , vol.266 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 14
    • 0029029477 scopus 로고
    • 2+ sensitivity of tension at short sarcomere length
    • 2+ sensitivity of tension at short sarcomere length. Circ Res 1995; 77: 199-205.
    • (1995) Circ Res , vol.77 , pp. 199-205
    • McDonald, K.S.1    Moss, R.L.2
  • 17
    • 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
  • 18
    • 0032555957 scopus 로고    scopus 로고
    • 2+ activation of rat ventricular myocytes
    • 2+ activation of rat ventricular myocytes. Circ Res 1998: 83: 602-607.
    • (1998) Circ Res , vol.83 , pp. 602-607
    • Fitzsimons, D.P.1    Moss, R.L.2
  • 19
    • 0033391877 scopus 로고    scopus 로고
    • 2+ activation in skinned cardiac muscle
    • 2+ activation in skinned cardiac muscle. J Mol Cell Cardiol 1999; 31: 2115-2125.
    • (1999) J Mol Cell Cardiol , vol.31 , pp. 2115-2125
    • Smith, S.H.1    Fuchs, F.2
  • 20
    • 0033837627 scopus 로고    scopus 로고
    • Length-dependence of cross-bridge mediated activation of the cardiac thin filament
    • SMITH SH, FUCHS F. Length-dependence of cross-bridge mediated activation of the cardiac thin filament. J Mol Cell Cardiol 2000; 32: 831-838.
    • (2000) J Mol Cell Cardiol , vol.32 , pp. 831-838
    • Smith, S.H.1    Fuchs, F.2
  • 21
    • 0014528144 scopus 로고
    • Parallel response of myofibrillar contraction and relaxation to four different nucleoside triphosphates
    • WEBER A. Parallel response of myofibrillar contraction and relaxation to four different nucleoside triphosphates. J Gen Physiol 1969: 53: 781-791.
    • (1969) J Gen Physiol , vol.53 , pp. 781-791
    • Weber, A.1
  • 22
    • 0027287625 scopus 로고
    • Kinetics of binding and hydrolysis of a series of nucleoside triphosphates by actomyosin-S1. Relationship between solution rate constants and properties of muscle fibers
    • WHITE HD, BELKNAP B, JIANG W. Kinetics of binding and hydrolysis of a series of nucleoside triphosphates by actomyosin-S1. Relationship between solution rate constants and properties of muscle fibers. J Biol Chem 1993; 268: 10039-10045.
    • (1993) J Biol Chem , vol.268 , pp. 10039-10045
    • White, H.D.1    Belknap, B.2    Jiang, W.3
  • 23
    • 0027232755 scopus 로고
    • The use of differing nucleotides to investigate cross-bridge kinetics
    • PATE E, FRANKS-SKIBA K, WHITE H, COOKE R. The use of differing nucleotides to investigate cross-bridge kinetics. J Biol Chem 1993; 268: 10046-10053.
    • (1993) J Biol Chem , vol.268 , pp. 10046-10053
    • Pate, E.1    Franks-Skiba, K.2    White, H.3    Cooke, R.4
  • 25
    • 0031806429 scopus 로고    scopus 로고
    • ATP analogs and muscle contraction: Mechanics and kinetics of nucleoside triphosphate binding and hydrolysis
    • REGNIER M, LEE DM, HOMSHER E. ATP analogs and muscle contraction: mechanics and kinetics of nucleoside triphosphate binding and hydrolysis. Biophys J 1998; 74: 3044-3058.
    • (1998) Biophys J , vol.74 , pp. 3044-3058
    • Regnier, M.1    Lee, D.M.2    Homsher, E.3
  • 26
    • 0031834714 scopus 로고    scopus 로고
    • The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers
    • REGNIER M, HOMSHER E. The effect of ATP analogs on posthydrolytic and force development steps in skinned skeletal muscle fibers. Biophys J 1998: 74: 3059-3071.
    • (1998) Biophys J , vol.74 , pp. 3059-3071
    • Regnier, M.1    Homsher, E.2
  • 27
    • 85031448464 scopus 로고    scopus 로고
    • Cardiac thin filament activation in the presence of MgITP
    • Abstract
    • SMITH SH, FUCHS F. Cardiac thin filament activation in the presence of MgITP. Biophys J 1998; 74: A362 (Abstract).
    • (1998) Biophys J , vol.74
    • Smith, S.H.1    Fuchs, F.2
  • 28
    • 0018733531 scopus 로고
    • Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells
    • FABIATO A, FABIATO F. Calculator programs for computing the composition of the solutions containing multiple metals and ligands used for experiments in skinned muscle cells. J Physiol (Paris) 1979; 75: 463-505.
    • (1979) J Physiol (Paris) , vol.75 , pp. 463-505
    • Fabiato, A.1    Fabiato, F.2
  • 30
    • 0019824784 scopus 로고
    • Calcium ion-sensitive contraction of glycerinated porcine cardiac muscle fibers by Mg-inosine triphosphate. ITP as a tool to dissociate the contraction mechanism from the regulatory mechanism
    • TOYO-OKA T. Calcium ion-sensitive contraction of glycerinated porcine cardiac muscle fibers by Mg-inosine triphosphate. ITP as a tool to dissociate the contraction mechanism from the regulatory mechanism. Circ Res 1981: 49: 1350-1355.
    • (1981) Circ Res , vol.49 , pp. 1350-1355
    • Toyo-Oka, T.1
  • 31
    • 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
  • 32
    • 0034614288 scopus 로고    scopus 로고
    • Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle
    • FUKUDA N, KAJIWARA H, ISHIWATA S, KURIHARA S. Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle. Circ Res 2000; 86: E1-E6.
    • (2000) Circ Res , vol.86
    • Fukuda, N.1    Kajiwara, H.2    Ishiwata, S.3    Kurihara, S.4
  • 33
    • 0028887715 scopus 로고
    • Characterization of the equilibrium between blocked and closed states of muscle thin filaments
    • HEAD JG, RITCHIE MD, GEEVES MA. Characterization of the equilibrium between blocked and closed states of muscle thin filaments. Eur J Biochem 1995: 227: 694-699.
    • (1995) Eur J Biochem , vol.227 , pp. 694-699
    • Head, J.G.1    Ritchie, M.D.2    Geeves, M.A.3
  • 34
    • 0010430661 scopus 로고
    • Actin activation of heavy meromyosin and subfragment-1 ATPases; steady state kinetic studies
    • MOOS C. Actin activation of heavy meromyosin and subfragment-1 ATPases; steady state kinetic studies. Cold Spring Harbor Symp Quant Biol 1972; 37: 137-143.
    • (1972) Cold Spring Harbor Symp Quant Biol , vol.37 , pp. 137-143
    • Moos, C.1
  • 35
    • 0021881139 scopus 로고
    • Role of myofibrillar creatine kinase in the relaxation of rigor tension in skinned cardiac muscle
    • VENTURA-CLAPIER R, VASSORT G. Role of myofibrillar creatine kinase in the relaxation of rigor tension in skinned cardiac muscle. Pfügers Arch 1985; 404: 157-161.
    • (1985) Pfügers Arch , vol.404 , pp. 157-161
    • Ventura-Clapier, R.1    Vassort, G.2
  • 36
    • 0010470813 scopus 로고
    • The reaction of nucleotide substrate analogues with adenosine triphosphate-creatine phosphotransferase
    • JAMES E, MORRISON JF. The reaction of nucleotide substrate analogues with adenosine triphosphate-creatine phosphotransferase. J Biol Chem 1966; 254: 3497-3502.
    • (1966) J Biol Chem , vol.254 , pp. 3497-3502
    • James, E.1    Morrison, J.F.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.