메뉴 건너뛰기




Volumn 131, Issue 1, 2008, Pages 33-41

Disuse-induced preferential loss of the giant protein titin depresses muscle performance via abnormal sarcomeric organization

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN;

EID: 38049091591     PISSN: 00221295     EISSN: 00221295     Source Type: Journal    
DOI: 10.1085/jgp.200709888     Document Type: Article
Times cited : (86)

References (31)
  • 1
    • 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
  • 2
    • 0033883216 scopus 로고    scopus 로고
    • Physiology of a microgravity environment invited review: Microgravity and skeletal muscle
    • Fitts, R.H., D.R. Riley, and J.J. Widrick. 2000. Physiology of a microgravity environment invited review: microgravity and skeletal muscle. J. Appl. Physiol. 89:823-839.
    • (2000) J. Appl. Physiol , vol.89 , pp. 823-839
    • Fitts, R.H.1    Riley, D.R.2    Widrick, J.J.3
  • 3
    • 0029909623 scopus 로고    scopus 로고
    • Structural and functional reconstitution of thin filaments in the contractile apparatus of cardiac muscle
    • Fujita, H., K. Yasuda, S. Niitsu, T. Funatsu, and S. Ishiwata. 1996. Structural and functional reconstitution of thin filaments in the contractile apparatus of cardiac muscle. Biophys. J. 71:2307-2318.
    • (1996) Biophys. J , vol.71 , pp. 2307-2318
    • Fujita, H.1    Yasuda, K.2    Niitsu, S.3    Funatsu, T.4    Ishiwata, S.5
  • 4
    • 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
  • 5
    • 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. 2001a. 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
  • 6
    • 0035476172 scopus 로고    scopus 로고
    • Acidosis or inorganic phosphate enhances the length dependence of tension in rat skinned cardiac muscle
    • Fukuda, N., J. O-Uchi, D. Sasaki, H. Kajiwara, S. Ishiwata, and S. Kurihara. 2001b. Acidosis or inorganic phosphate enhances the 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
  • 7
    • 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
  • 8
    • 15244348075 scopus 로고    scopus 로고
    • Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner
    • Fukuda, N., Y. Wu, P. Nair, and H.L. Granzier. 2005. Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner. J. Gen. Physiol. 125:257-271.
    • (2005) J. Gen. Physiol , vol.125 , pp. 257-271
    • Fukuda, N.1    Wu, Y.2    Nair, P.3    Granzier, H.L.4
  • 9
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass, D.J. 2003. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat. Cell Biol. 5:87-90.
    • (2003) Nat. Cell Biol , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 10
    • 0037370942 scopus 로고    scopus 로고
    • Profiles of connectin (titin) in atrophied soleus muscle induced by unloading of rats
    • Goto, K., R. Okuyama, M. Honda, H. Uchida, T. Akema, Y. Ohira, and T. Yoshioka. 2003. Profiles of connectin (titin) in atrophied soleus muscle induced by unloading of rats. J. Appl. Physiol. 94:897-902.
    • (2003) J. Appl. Physiol , vol.94 , pp. 897-902
    • Goto, K.1    Okuyama, R.2    Honda, M.3    Uchida, H.4    Akema, T.5    Ohira, Y.6    Yoshioka, T.7
  • 11
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • Granzier, H., 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.1    Labeit, S.2
  • 12
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments
    • Granzier, H.L., and T.C. Irving. 1995. Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments. Biophys. J. 68:1027-1044.
    • (1995) Biophys. J , vol.68 , pp. 1027-1044
    • Granzier, H.L.1    Irving, T.C.2
  • 14
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • Helmes, M., K. Trombitas, and H. Granzier. 1996. Titin develops restoring force in rat cardiac myocytes. Circ. Res. 79:619-626.
    • (1996) Circ. Res , vol.79 , pp. 619-626
    • Helmes, M.1    Trombitas, K.2    Granzier, H.3
  • 15
    • 0026910654 scopus 로고
    • Myofilament lengths of cat skeletal muscle: Theoretical considerations and functional implications
    • Herzog, W., S. Kamal, and H.D. Clarke. 1992. Myofilament lengths of cat skeletal muscle: theoretical considerations and functional implications. J. Biomech. 25:945-948.
    • (1992) J. Biomech , vol.25 , pp. 945-948
    • Herzog, W.1    Kamal, S.2    Clarke, H.D.3
  • 16
    • 0022780963 scopus 로고
    • Lattice shrinkage with increasing resting tension in stretched, single skinned fibers of frog muscle
    • Higuchi, H., and Y. Umazume. 1986. Lattice shrinkage with increasing resting tension in stretched, single skinned fibers of frog muscle. Biophys. J. 50:385-389.
    • (1986) Biophys. J , vol.50 , pp. 385-389
    • Higuchi, H.1    Umazume, Y.2
  • 17
    • 0023655206 scopus 로고
    • Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements
    • Ishiwata, S., K. Kinosita Jr., H. Yoshimura, and A. Ikegami. 1987. Rotational motions of myosin heads in myofibril studied by phosphorescence anisotropy decay measurements. J. Biol. Chem. 262:8314-8317.
    • (1987) J. Biol. Chem , vol.262 , pp. 8314-8317
    • Ishiwata, S.1    Kinosita Jr., K.2    Yoshimura, H.3    Ikegami, A.4
  • 20
    • 0032407540 scopus 로고    scopus 로고
    • Defining actin filament length in striated muscle: Rulers and caps or dynamic stability?
    • Littlefield, R., and V.M. Fowler. 1998. Defining actin filament length in striated muscle: rulers and caps or dynamic stability? Annu. Rev. Cell Dev. Biol. 14:487-525.
    • (1998) Annu. Rev. Cell Dev. Biol , vol.14 , pp. 487-525
    • Littlefield, R.1    Fowler, V.M.2
  • 21
    • 33847685896 scopus 로고    scopus 로고
    • Therapeutic approaches for muscle wasting disorders
    • Lynch, G.S., J.D. Schertzer, and J.G. Ryall. 2006. Therapeutic approaches for muscle wasting disorders. Pharmacol. Ther. 113:461-487.
    • (2006) Pharmacol. Ther , vol.113 , pp. 461-487
    • Lynch, G.S.1    Schertzer, J.D.2    Ryall, J.G.3
  • 22
    • 0028128224 scopus 로고
    • Coordinate changes in C protein and myosin expression during skeletal muscle hypertrophy
    • McCormick, K.M., K.M. Baldwin, and A.F. Schachat. 1994. Coordinate changes in C protein and myosin expression during skeletal muscle hypertrophy. Am. J. Physiol. 267:C443-C449.
    • (1994) Am. J. Physiol , vol.267
    • McCormick, K.M.1    Baldwin, K.M.2    Schachat, A.F.3
  • 26
    • 0035079433 scopus 로고    scopus 로고
    • Characterization of control and immobilized skeletal muscle: An overview from genetic engineering
    • St-Amand, J., K. Okamura, K. Matsumoto, S. Shimizu, and Y. Sogawa. 2001. Characterization of control and immobilized skeletal muscle: an overview from genetic engineering. FASEB J. 15:684-692.
    • (2001) FASEB J , vol.15 , pp. 684-692
    • St-Amand, J.1    Okamura, K.2    Matsumoto, K.3    Shimizu, S.4    Sogawa, Y.5
  • 27
    • 0036089996 scopus 로고    scopus 로고
    • Passive tension of rat skeletal soleus muscle fibers: Effects of unloading conditions
    • Toursel, T., L. Stevens, H. Granzier, and Y. Mounier. 2002. Passive tension of rat skeletal soleus muscle fibers: effects of unloading conditions. J. Appl. Physiol. 92:1465-1472.
    • (2002) J. Appl. Physiol , vol.92 , pp. 1465-1472
    • Toursel, T.1    Stevens, L.2    Granzier, H.3    Mounier, Y.4
  • 28
    • 0028091960 scopus 로고
    • Titin and nebulin: Protein rulers in muscle?
    • Trinick, J. 1994. Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci. 19:405-409.
    • (1994) Trends Biochem. Sci , vol.19 , pp. 405-409
    • Trinick, J.1
  • 29
    • 0034010296 scopus 로고    scopus 로고
    • A functional knock-out of titin results in defective myofibril assembly
    • van der Ven, P.F., J.W. Batsch, M. Gautel, H. Jockusch, and D.O. Furst. 2000. A functional knock-out of titin results in defective myofibril assembly. J. Cell Sci. 113:1405-1414.
    • (2000) J. Cell Sci , vol.113 , pp. 1405-1414
    • van der Ven, P.F.1    Batsch, J.W.2    Gautel, M.3    Jockusch, H.4    Furst, D.O.5
  • 30
    • 0024961666 scopus 로고
    • Does titin regulate the length of muscle thick filaments?
    • Whiting, A., J. Wardale, and J. Trinick. 1989. Does titin regulate the length of muscle thick filaments? J. Mol. Biol. 205:263-268.
    • (1989) J. Mol. Biol , vol.205 , pp. 263-268
    • Whiting, A.1    Wardale, J.2    Trinick, J.3
  • 31
    • 85004619259 scopus 로고
    • Length regulation of thin filaments without nebulin
    • Yasuda, K., H. Fujita, Y. Fujiki, and S. Ishiwata. 1994. Length regulation of thin filaments without nebulin. Proc. Jpn. Acad. 70:151-156.
    • (1994) Proc. Jpn. Acad , vol.70 , pp. 151-156
    • Yasuda, K.1    Fujita, H.2    Fujiki, Y.3    Ishiwata, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.