메뉴 건너뛰기




Volumn 131, Issue 3, 2008, Pages 275-283

Troponin and titin coordinately regulate length-dependent activation in skinned porcine ventricular muscle

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; TROPONIN;

EID: 40849097709     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200709895     Document Type: Article
Times cited : (46)

References (38)
  • 1
    • 0016337078 scopus 로고
    • The contribution of activation processes to the length-tension relation of cardiac muscle
    • Allen, D.G., B.R. Jewell, and J.W. Murray. 1974. The contribution of activation processes to the length-tension relation of cardiac muscle. Nature. 248:606-607.
    • (1974) Nature , vol.248 , pp. 606-607
    • Allen, D.G.1    Jewell, B.R.2    Murray, J.W.3
  • 2
    • 0022393490 scopus 로고
    • The cellular basis of the length-tension relation in cardiac muscle
    • Allen, D.G., and J.C. Kentish. 1985. The cellular basis of the length-tension relation in cardiac muscle. J. Mol. Cell. Cardiol. 17:821-840.
    • (1985) J. Mol. Cell. Cardiol , vol.17 , pp. 821-840
    • Allen, D.G.1    Kentish, J.C.2
  • 3
    • 0033841530 scopus 로고    scopus 로고
    • Attenuation of length dependence of calcium activation in myofilaments of transgenic mouse hearts expressing slow skeletal troponin I
    • Arteaga, G.M., K.A. Palmiter, J.M. Leiden, and R.J. Solaro. 2000. Attenuation of length dependence of calcium activation in myofilaments of transgenic mouse hearts expressing slow skeletal troponin I. J. Physiol. 526:541-549.
    • (2000) J. Physiol , vol.526 , pp. 541-549
    • Arteaga, G.M.1    Palmiter, K.A.2    Leiden, J.M.3    Solaro, R.J.4
  • 4
    • 0023986488 scopus 로고
    • Molecular basis for the influence of muscle length on myocardial performance
    • Babu, A., E. Sonnenblick, and J. Gulati. 1988. Molecular basis for the influence of muscle length on myocardial performance. Science. 240:74-76.
    • (1988) Science , vol.240 , pp. 74-76
    • Babu, A.1    Sonnenblick, E.2    Gulati, J.3
  • 5
    • 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. USA. 85:3265-3269.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3265-3269
    • Brenner, B.1
  • 6
    • 2042451727 scopus 로고
    • Rate of force generation in muscle: Correlation with actomyosin ATPase activity in solution
    • Brenner, B., and E. Eisenberg. 1986. Rate of force generation in muscle: correlation with actomyosin ATPase activity in solution. Proc. Natl. Acad. Sci. USA. 83:3542-3546.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3542-3546
    • Brenner, B.1    Eisenberg, E.2
  • 7
    • 0035947754 scopus 로고    scopus 로고
    • Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes
    • Cazorla, O., Y. Wu, T.C. Irving, and H. Granzier. 2001. Titin-based modulation of calcium sensitivity of active tension in mouse skinned cardiac myocytes. Circ. Res. 88:1028-1035.
    • (2001) Circ. Res , vol.88 , pp. 1028-1035
    • Cazorla, O.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 8
    • 33646172748 scopus 로고    scopus 로고
    • Troponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle
    • Chandra, M., M.L. Tschirgi, I. Rajapakse, and K.B. Campbell. 2006. Troponin T modulates sarcomere length-dependent recruitment of cross-bridges in cardiac muscle. Biophys. J. 90:2867-2876.
    • (2006) Biophys. J , vol.90 , pp. 2867-2876
    • Chandra, M.1    Tschirgi, M.L.2    Rajapakse, I.3    Campbell, K.B.4
  • 11
    • 0034614288 scopus 로고    scopus 로고
    • Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle
    • Fukuda, N., H. Kajiwara, S. Ishiwata, and S. Kurihara. 2000. Effects of MgADP on length dependence of tension generation in skinned rat cardiac muscle. Circ. Res. 86:e1-e6.
    • (2000) Circ. Res , vol.86
    • Fukuda, N.1    Kajiwara, H.2    Ishiwata, S.3    Kurihara, S.4
  • 12
    • 0035476172 scopus 로고    scopus 로고
    • Acidosis or inorganic phosphate enhances length dependence of tension in rat skinned cardiac muscle
    • Fukuda, N., J. O-Uchi, D. Sasaki, H. Kajiwara, S. Ishiwata, and S. Kurihara. 2001a. Acidosis or inorganic phosphate enhances length dependence of tension in rat skinned cardiac muscle. J. Physiol. 536:153-160.
    • (2001) J. Physiol , vol.536 , pp. 153-160
    • Fukuda, N.1    O-Uchi, J.2    Sasaki, D.3    Kajiwara, H.4    Ishiwata, S.5    Kurihara, S.6
  • 13
    • 0035797846 scopus 로고    scopus 로고
    • Length dependence of tension generation in rat skinned cardiac muscle: Role of titin in the Frank-Starling mechanism of the heart
    • Fukuda, N., D. Sasaki, S. Ishiwata, and S. Kurihara. 2001b. Length dependence of tension generation in rat skinned cardiac muscle: role of titin in the Frank-Starling mechanism of the heart. Circulation. 104:1639-1645.
    • (2001) Circulation , vol.104 , pp. 1639-1645
    • Fukuda, N.1    Sasaki, D.2    Ishiwata, S.3    Kurihara, S.4
  • 14
    • 0344896768 scopus 로고    scopus 로고
    • Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle
    • Fukuda, N., Y. Wu, T.C. Irving, and H. Granzier. 2003. Titin isoform variance and length dependence of activation in skinned bovine cardiac muscle. J. Physiol. 553:147-154.
    • (2003) J. Physiol , vol.553 , pp. 147-154
    • Fukuda, N.1    Wu, Y.2    Irving, T.C.3    Granzier, H.4
  • 15
    • 33745698398 scopus 로고    scopus 로고
    • Titin/connectin-based modulation of the Frank-Starling mechanism of the heart
    • Fukuda, N., and H.L. Granzier. 2005. Titin/connectin-based modulation of the Frank-Starling mechanism of the heart. J. Muscle Res. Cell Motil. 26:319-323.
    • (2005) J. Muscle Res. Cell Motil , vol.26 , pp. 319-323
    • Fukuda, N.1    Granzier, H.L.2
  • 16
    • 0032555957 scopus 로고    scopus 로고
    • 2+ activation of rat ventricular myocytes
    • 2+ activation of rat ventricular myocytes. Circ. Res. 83:602-607.
    • (1998) Circ. Res , vol.83 , pp. 602-607
    • Fitzsimons, D.P.1    Moss, R.L.2
  • 17
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • Granzier, H.L., and S. Labeit. 2004. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ. Res. 94:284-295.
    • (2004) Circ. Res , vol.94 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 18
    • 0025776651 scopus 로고
    • 2+ -sensitive force of mammalian skeletal and cardiac muscles
    • 2+ -sensitive force of mammalian skeletal and cardiac muscles. J. Physiol. 441:305-324.
    • (1991) J. Physiol , vol.441 , pp. 305-324
    • Gulati, J.1    Sonnenblick, E.2    Babu, A.3
  • 19
    • 12544260027 scopus 로고    scopus 로고
    • Inherited cardiomyopathies as a troponin disease
    • Harada, K., and S. Morimoto. 2004. Inherited cardiomyopathies as a troponin disease. Jpn. J. Physiol. 54:307-318.
    • (2004) Jpn. J. Physiol , vol.54 , pp. 307-318
    • Harada, K.1    Morimoto, S.2
  • 20
    • 33847013578 scopus 로고
    • Muscle structure and theories of contraction
    • Huxley, A.F. 1957. Muscle structure and theories of contraction. Prog. Biophys. Biophys. Chem. 7:255-318.
    • (1957) Prog. Biophys. Biophys. Chem , vol.7 , pp. 255-318
    • Huxley, A.F.1
  • 21
    • 0037015915 scopus 로고    scopus 로고
    • Ernest Henry Starling, his predecessors, and the "Law of the Heart
    • Katz, A.M. 2002. Ernest Henry Starling, his predecessors, and the "Law of the Heart". Circulation. 106:2986-2992.
    • (2002) Circulation , vol.106 , pp. 2986-2992
    • Katz, A.M.1
  • 22
    • 0037059456 scopus 로고    scopus 로고
    • Myofilament calcium sensitivity in skinned rat cardiac trabeculae: Role of interfilament spacing
    • Konhilas, J.P., T.C. Irving, and P.P. de Tombe. 2002a. Myofilament calcium sensitivity in skinned rat cardiac trabeculae: role of interfilament spacing. Circ. Res. 90:59-65.
    • (2002) Circ. Res , vol.90 , pp. 59-65
    • Konhilas, J.P.1    Irving, T.C.2    de Tombe, P.P.3
  • 23
    • 0036795565 scopus 로고    scopus 로고
    • Length-dependent activation in three striated muscle types of the rat
    • Konhilas, J.P., T.C. Irving, and P.P. de Tombe. 2002b. Length-dependent activation in three striated muscle types of the rat. J. Physiol. 544:225-236.
    • (2002) J. Physiol , vol.544 , pp. 225-236
    • Konhilas, J.P.1    Irving, T.C.2    de Tombe, P.P.3
  • 24
  • 25
    • 0029029477 scopus 로고
    • 2+ sensitivity of tension at short sarcomere length
    • 2+ sensitivity of tension at short sarcomere length. Circ. Res. 77:199-205.
    • (1995) Circ. Res , vol.77 , pp. 199-205
    • McDonald, K.S.1    Moss, R.L.2
  • 27
    • 0024312136 scopus 로고
    • Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle
    • Metzger, J.M., M.L. Greaser, and R.L. Moss. 1989. Variations in cross-bridge attachment rate and tension with phosphorylation of myosin in mammalian skinned skeletal muscle fibers. Implications for twitch potentiation in intact muscle. J. Gen. Physiol. 93:855-883.
    • (1989) J. Gen. Physiol , vol.93 , pp. 855-883
    • Metzger, J.M.1    Greaser, M.L.2    Moss, R.L.3
  • 29
    • 0025870931 scopus 로고
    • Substitution of cardiac troponin C into rabbit muscle does not alter the length dependence of Ca sensitivity of tension
    • Moss, R.L., L.O. Nwoye, and M.L. Greaser. 1991. Substitution of cardiac troponin C into rabbit muscle does not alter the length dependence of Ca sensitivity of tension. J. Physiol. 440:273-289.
    • (1991) J. Physiol , vol.440 , pp. 273-289
    • Moss, R.L.1    Nwoye, L.O.2    Greaser, M.L.3
  • 31
    • 0242475138 scopus 로고    scopus 로고
    • Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils
    • Piroddi, N., C. Tesi, M.A. Pellegrino, L.S. Tobacman, E. Homsher, and C. Poggesi. 2003. Contractile effects of the exchange of cardiac troponin for fast skeletal troponin in rabbit psoas single myofibrils. J. Physiol. 552:917-931.
    • (2003) J. Physiol , vol.552 , pp. 917-931
    • Piroddi, N.1    Tesi, C.2    Pellegrino, M.A.3    Tobacman, L.S.4    Homsher, E.5    Poggesi, C.6
  • 32
    • 0027252481 scopus 로고
    • Replacement of troponin in bullfrog skeletal myofibrils by rabbit skeletal and bovine cardiac troponins
    • Shiraishi, F., Y. Nakamura, and I. Ohtsuki. 1993. Replacement of troponin in bullfrog skeletal myofibrils by rabbit skeletal and bovine cardiac troponins. Biomed. Res. 14:93-97.
    • (1993) Biomed. Res , vol.14 , pp. 93-97
    • Shiraishi, F.1    Nakamura, Y.2    Ohtsuki, I.3
  • 35
    • 0032494188 scopus 로고    scopus 로고
    • Troponin and tropomyosin: Proteins that switch on and tune in the activity of cardiac myofilaments
    • Solaro, R.J., and H.M. Rarick. 1998. Troponin and tropomyosin: proteins that switch on and tune in the activity of cardiac myofilaments. Circ. Res. 83:471-480.
    • (1998) Circ. Res , vol.83 , pp. 471-480
    • Solaro, R.J.1    Rarick, H.M.2
  • 36
    • 37349057143 scopus 로고    scopus 로고
    • Mechanisms of the Frank-Starling law of the heart: The beat goes on
    • Solaro, R.J. 2007. Mechanisms of the Frank-Starling law of the heart: the beat goes on. Biophys. J. 93:4095-4096.
    • (2007) Biophys. J , vol.93 , pp. 4095-4096
    • Solaro, R.J.1
  • 37
    • 36349031141 scopus 로고    scopus 로고
    • Cardiac troponin I threonine 144: Role in myofilament length-dependent activation
    • Tachampa, K., H. Wang, G.P. Farman, and P.P. de Tombe. 2007. Cardiac troponin I threonine 144: role in myofilament length-dependent activation. Circ. Res. 101:1081-1083.
    • (2007) Circ. Res , vol.101 , pp. 1081-1083
    • Tachampa, K.1    Wang, H.2    Farman, G.P.3    de Tombe, P.P.4
  • 38
    • 38049091591 scopus 로고    scopus 로고
    • Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization
    • Udaka, J., S. Ohmori, T. Terui, I. Ohtsuki, S. Ishiwata, S. Kurihara, and N. Fukuda. 2008. Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization. J. Gen. Physiol. 131:33-41.
    • (2008) J. Gen. Physiol , vol.131 , pp. 33-41
    • Udaka, J.1    Ohmori, S.2    Terui, T.3    Ohtsuki, I.4    Ishiwata, S.5    Kurihara, S.6    Fukuda, N.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.