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Volumn 296, Issue 5, 2009, Pages

Involvement of calpains in Ca2+-induced disruption of excitation-contraction coupling in mammalian skeletal muscle fibers

Author keywords

calpain; Calpain 3; Knockout mice; Muscle fatigue; Skinned fiber

Indexed keywords

CALCIUM ION; CALPAIN 1; CALPAIN 3; CALCIUM; CALPAIN; CAPN3 PROTEIN, MOUSE; CAPN3 PROTEIN, RAT; ISOENZYME; MU-CALPAIN; MUSCLE PROTEIN;

EID: 66149129918     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00008.2009     Document Type: Article
Times cited : (34)

References (34)
  • 3
    • 56949085969 scopus 로고    scopus 로고
    • Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance
    • Beckmann JS, Spencer M. Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance. Neuromuscul Disord 18: 913-921, 2008.
    • (2008) Neuromuscul Disord , vol.18 , pp. 913-921
    • Beckmann, J.S.1    Spencer, M.2
  • 4
    • 0001493462 scopus 로고    scopus 로고
    • Expression, partial purification and functional properties of the muscle-specific calpain isoform p94
    • DOI 10.1046/j.1432-1327.1999.00817.x
    • Branca D, Gugliucci A, Bano D, Brini M, Carafoli E. Expression, partial purification and functional properties of the muscle-specific calpain isoform p94. Eur J Biochem 265: 839-846, 1999. (Pubitemid 29489018)
    • (1999) European Journal of Biochemistry , vol.265 , Issue.2 , pp. 839-846
    • Branca, D.1    Gugliucci, A.2    Bano, D.3    Brini, M.4    Carafoli, E.5
  • 5
    • 0029984552 scopus 로고    scopus 로고
    • 2+] in the development of low frequency fatigue in mouse single muscle fibres
    • 2+] in the development of low frequency fatigue in mouse single muscle fibres. J Physiol 491: 813-824, 1996.
    • (1996) J Physiol , vol.491 , pp. 813-824
    • Chin, E.R.1    Allen, D.G.2
  • 6
    • 0030894688 scopus 로고    scopus 로고
    • Role of intracellular calcium and metabolites in low-frequency fatigue of mouse skeletal muscle
    • Chin ER, Balnave CD, Allen DG. Role of intracellular calcium and metabolites in low-frequency fatigue of mouse skeletal muscle. Am J Physiol Cell Physiol 272: C550-C559, 1997.
    • (1997) Am J Physiol Cell Physiol , vol.272
    • Chin, E.R.1    Balnave, C.D.2    Allen, D.G.3
  • 7
    • 33845230658 scopus 로고    scopus 로고
    • Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice
    • Cohen N, Kudryashova E, Kramerova I, Anderson LV, Beckmann JS, Bushby K, Spencer MJ. Identification of putative in vivo substrates of calpain 3 by comparative proteomics of overexpressing transgenic and nontransgenic mice. Proteomics 6: 6075-6084, 2006.
    • (2006) Proteomics , vol.6 , pp. 6075-6084
    • Cohen, N.1    Kudryashova, E.2    Kramerova, I.3    Anderson, L.V.4    Beckmann, J.S.5    Bushby, K.6    Spencer, M.J.7
  • 8
    • 33746129198 scopus 로고    scopus 로고
    • Calpain 3: A key regulator of the sarcomere?
    • DOI 10.1111/j.1742-4658.2006.05351.x
    • Duguez S, Bartoli M, Richard I. Calpain 3: a key regulator of the sarcomere? FEBS J 273: 3427-3436, 2006. (Pubitemid 44086943)
    • (2006) FEBS Journal , vol.273 , Issue.15 , pp. 3427-3436
    • Duguez, S.1    Bartoli, M.2    Richard, I.3
  • 9
    • 33747045217 scopus 로고    scopus 로고
    • Excitation-contraction coupling from the 1950s into the new millennium
    • Dulhunty AF. Excitation-contraction coupling from the 1950s into the new millennium. Clin Exp Pharmacol Physiol 33: 763-772, 2006.
    • (2006) Clin Exp Pharmacol Physiol , vol.33 , pp. 763-772
    • Dulhunty, A.F.1
  • 11
    • 3042597817 scopus 로고    scopus 로고
    • Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide
    • DOI 10.1074/jbc.M313290200
    • Garcia Diaz BE, Moldoveanu T, Kuiper MJ, Campbell RL, Davies PL. Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide. J Biol Chem 279: 27656-27666, 2004. (Pubitemid 38812607)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27656-27666
    • Diaz, B.G.1    Moldoveanu, T.2    Kuiper, M.J.3    Campbell, R.L.4    Davies, P.L.5
  • 12
    • 0026644847 scopus 로고
    • Calcium-activated neutral protease effects upon skeletal muscle sarcoplasmic reticulum protein structure and calcium release
    • Gilchrist JS, Wang KK, Katz S, Belcastro AN. Calcium-activated neutral protease effects upon skeletal muscle sarcoplasmic reticulum protein structure and calcium release. J Biol Chem 267: 20857-20865, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 20857-20865
    • Gilchrist, J.S.1    Wang, K.K.2    Katz, S.3    Belcastro, A.N.4
  • 14
    • 0038308480 scopus 로고    scopus 로고
    • Localization of calpain 3 in human skeletal muscle and its alteration in limb-girdle muscular dystrophy 2A muscle
    • DOI 10.1093/jb/mvg084
    • Keira Y, Noguchi S, Minami N, Hayashi YK, Nishino I. Localization of calpain 3 in human skeletal muscle and its alteration in limb-girdle muscular dystrophy 2A muscle. J Biochem (Tokyo) 133: 659-664, 2003. (Pubitemid 36759474)
    • (2003) Journal of Biochemistry , vol.133 , Issue.5 , pp. 659-664
    • Keira, Y.1    Noguchi, S.2    Minami, N.3    Hayashi, Y.K.4    Nishino, I.5
  • 15
    • 0025095222 scopus 로고
    • Identification of a new subpopulation of triad junctions isolated from skeletal muscle; morphological correlations with intact muscle
    • Kim KC, Caswell AH, Brunschwig JP, Brandt NR. Identification of a new subpopulation of triad junctions isolated from skeletal muscle; morphological correlations with intact muscle. J Membr Biol 113: 221-235, 1990.
    • (1990) J Membr Biol , vol.113 , pp. 221-235
    • Kim, K.C.1    Caswell, A.H.2    Brunschwig, J.P.3    Brandt, N.R.4
  • 16
    • 54449100812 scopus 로고    scopus 로고
    • Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle
    • Kramerova I, Kudryashova E, Wu B, Ottenheijm C, Granzier H, Spencer MJ. Novel role of calpain-3 in the triad-associated protein complex regulating calcium release in skeletal muscle. Hum Mol Genet 17: 3271-3280, 2008.
    • (2008) Hum Mol Genet , vol.17 , pp. 3271-3280
    • Kramerova, I.1    Kudryashova, E.2    Wu, B.3    Ottenheijm, C.4    Granzier, H.5    Spencer, M.J.6
  • 17
    • 0029416980 scopus 로고
    • 2+] abolishes excitation-contraction coupling in skeletal muscle fibres of rat and toad
    • 2+] abolishes excitation-contraction coupling in skeletal muscle fibres of rat and toad. J Physiol 489: 349-362, 1995.
    • (1995) J Physiol , vol.489 , pp. 349-362
    • Lamb, G.D.1    Junankar, P.R.2    Stephenson, D.G.3
  • 18
    • 0028108096 scopus 로고
    • 2+] on excitation- contraction coupling in skeletal muscle fibres of the rat
    • 2+] on excitation-contraction coupling in skeletal muscle fibres of the rat. J Physiol 478: 331-339, 1994.
    • (1994) J Physiol , vol.478 , pp. 331-339
    • Lamb, G.D.1    Stephenson, D.G.2
  • 21
    • 34548432545 scopus 로고    scopus 로고
    • Calpain-3 is autolyzed and hence activated in human skeletal muscle 24 h following a single bout of eccentric exercise
    • DOI 10.1152/japplphysiol.01422.2006
    • Murphy RM, Goodman CA, McKenna MJ, Bennie J, Leikis M, Lamb GD. Calpain-3 is autolyzed and hence activated in human skeletal muscle 24 h following a single bout of eccentric exercise. J Appl Physiol 103: 926-931, 2007. (Pubitemid 47358876)
    • (2007) Journal of Applied Physiology , vol.103 , Issue.3 , pp. 926-931
    • Murphy, R.M.1    Goodman, C.A.2    McKenna, M.J.3    Bennie, J.4    Leikis, M.5    Lamb, G.D.6
  • 22
    • 65549087562 scopus 로고    scopus 로고
    • 2+] and is not dependent on stretch
    • 2+] and is not dependent on stretch. J Biol Chem 284: 7811-7819, 2009.
    • (2009) J Biol Chem , vol.284 , pp. 7811-7819
    • Murphy, R.M.1    Lamb, G.D.2
  • 23
    • 33644824974 scopus 로고    scopus 로고
    • μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans
    • Murphy RM, Snow RJ, Lamb GD. μ-Calpain and calpain-3 are not autolyzed with exhaustive exercise in humans. Am J Physiol Cell Physiol 290: C116-C122, 2006.
    • (2006) Am J Physiol Cell Physiol , vol.290
    • Murphy, R.M.1    Snow, R.J.2    Lamb, G.D.3
  • 24
    • 33749344685 scopus 로고    scopus 로고
    • 2+-activation of diffusible and bound pools of μ-calpain in rat skeletal muscle
    • 2+-activation of diffusible and bound pools of μ-calpain in rat skeletal muscle. J Physiol 576: 595-612, 2006.
    • (2006) J Physiol , vol.576 , pp. 595-612
    • Murphy, R.M.1    Verburg, E.2    Lamb, G.D.3
  • 26
    • 18944385186 scopus 로고    scopus 로고
    • Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril
    • DOI 10.1111/j.1742-4658.2005.04683.x
    • Raynaud F, Fernandez E, Coulis G, Aubry L, Vignon X, Bleimling N, Gautel M, Benyamin Y, Ouali A. Calpain 1-titin interactions concentrate calpain 1 in the Z-band edges and in the N2-line region within the skeletal myofibril. FEBS J 272: 2578-2590, 2005. (Pubitemid 40705077)
    • (2005) FEBS Journal , vol.272 , Issue.10 , pp. 2578-2590
    • Raynaud, F.1    Fernandez, E.2    Coulis, G.3    Aubry, L.4    Vignon, X.5    Bleimling, N.6    Gautel, M.7    Benyamin, Y.8    Ouali, A.9
  • 32
    • 0344629442 scopus 로고    scopus 로고
    • Calpain 3 Is Activated through Autolysis within the Active Site and Lyses Sarcomeric and Sarcolemmal Components
    • DOI 10.1128/MCB.23.24.9127-9135.2003
    • Taveau M, Bourg N, Sillon G, Roudaut C, Bartoli M, Richard I. Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol Cell Biol 23: 9127-9135, 2003. (Pubitemid 37499802)
    • (2003) Molecular and Cellular Biology , vol.23 , Issue.24 , pp. 9127-9135
    • Taveau, M.1    Bourg, N.2    Sillon, G.3    Roudaut, C.4    Bartoli, M.5    Richard, I.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.