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Volumn 26, Issue 6-8, 2005, Pages 409-417

Possible functions of p94 in connectin-mediated signaling pathways in skeletal muscle cells

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ACTININ; ANKYRIN; BINDING PROTEIN; CALCIUM ION; CALPAIN; CALPAIN 3; CONNECTIN; MUSCLE ANKYRIN REPEAT PROTEIN; MUSCLE PROTEIN; MUSCLE RING FINGER PROTEIN; PROTEINASE; TITIN CAPPING PROTEIN; UNCLASSIFIED DRUG;

EID: 33745712380     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-005-9023-8     Document Type: Conference Paper
Times cited : (29)

References (64)
  • 2
    • 0030781392 scopus 로고    scopus 로고
    • Accumulation of muscle ankyrin repeat protein transcript reveals local activation of primary myotube endcompartments during muscle morphogenesis
    • Baumeister A, Arber S and Caroni P (1997) Accumulation of muscle ankyrin repeat protein transcript reveals local activation of primary myotube endcompartments during muscle morphogenesis. J Cell Biol 139: 1231-1242.
    • (1997) J Cell Biol , vol.139 , pp. 1231-1242
    • Baumeister, A.1    Arber, S.2    Caroni, P.3
  • 3
    • 0022573858 scopus 로고
    • Proliferation of muscle satellite cells on intact myofibers in culture
    • Bischoff R (1986) Proliferation of muscle satellite cells on intact myofibers in culture. Dev Biol 115: 129-139.
    • (1986) Dev Biol , vol.115 , pp. 129-139
    • Bischoff, R.1
  • 7
    • 0035968313 scopus 로고    scopus 로고
    • A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain
    • Dai K-S and Liew C-C (2001) A novel human striated muscle RING zinc finger protein, SMRZ, interacts with SMT3b via its RING domain. J Biol Chem 276: 23992-23999.
    • (2001) J Biol Chem , vol.276 , pp. 23992-23999
    • Dai, K.-S.1    Liew, C.-C.2
  • 8
    • 0038190993 scopus 로고    scopus 로고
    • Costameres: The Achilles' heel of Herculean muscle
    • Evarsti J (2003) Costameres: the Achilles' heel of Herculean muscle. J Biol Chem 278: 13591-13594.
    • (2003) J Biol Chem , vol.278 , pp. 13591-13594
    • Evarsti, J.1
  • 10
    • 0035798418 scopus 로고    scopus 로고
    • Specific interaction of the potassium channel-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system
    • Furukawa T, Ono Y, Tsuchiya H, Katayama Y, Bang M-L, Labeit D, Labeit S, Inagaki N and Gregorio CC (2001) Specific interaction of the potassium channel-subunit minK with the sarcomeric protein T-cap suggests a T-tubule-myofibril linking system. J Mol Biol 313: 775-784.
    • (2001) J Mol Biol , vol.313 , pp. 775-784
    • Furukawa, T.1    Ono, Y.2    Tsuchiya, H.3    Katayama, Y.4    Bang, M.-L.5    Labeit, D.6    Labeit, S.7    Inagaki, N.8    Gregorio, C.C.9
  • 11
    • 0035707910 scopus 로고    scopus 로고
    • The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin
    • Garvey SM, Rajan C, Lerner AP, Frankel WN and Cox GA (2002) The muscular dystrophy with myositis (mdm) mouse mutation disrupts a skeletal muscle-specific domain of titin. Genomics 79: 146-149.
    • (2002) Genomics , vol.79 , pp. 146-149
    • Garvey, S.M.1    Rajan, C.2    Lerner, A.P.3    Frankel, W.N.4    Cox, G.A.5
  • 12
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: Calpain proteases in cell motility
    • Glading A, Lauffenburger DA and Wells A (2002) Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol 12: 46-54.
    • (2002) Trends Cell Biol , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 15
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling and disease
    • Granzier HL and Labeit S (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
  • 19
    • 0034867549 scopus 로고    scopus 로고
    • Both the conserved and the unique gene structure of stomach-specific calpains reveal processes of calpain gene evolution
    • Hata S, Sorimachi H, Nakagawa K, Maeda T, Abe K and Suzuki K (2001) Both the conserved and the unique gene structure of stomach-specific calpains reveal processes of calpain gene evolution. J Mol Evol 53: 191-203.
    • (2001) J Mol Evol , vol.53 , pp. 191-203
    • Hata, S.1    Sorimachi, H.2    Nakagawa, K.3    Maeda, T.4    Abe, K.5    Suzuki, K.6
  • 21
    • 0033772073 scopus 로고    scopus 로고
    • Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus
    • Horikawa Y, Oda N, Cox NJ, Li X, Orho-Melander M, Hara M, Hinokio Y, et al. (2000) Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus. Nat Genet 26: 163-175.
    • (2000) Nat Genet , vol.26 , pp. 163-175
    • Horikawa, Y.1    Oda, N.2    Cox, N.J.3    Li, X.4    Orho-Melander, M.5    Hara, M.6    Hinokio, Y.7
  • 22
    • 0037423195 scopus 로고    scopus 로고
    • Molecular identification and characterization of a novel nuclear protein whose expression is up-regulated in insulin-resistant animals
    • Ikeda K, Emoto N, Matsuo M and Yokoyama M (2003) Molecular identification and characterization of a novel nuclear protein whose expression is up-regulated in insulin-resistant animals. J Biol Chem 278: 3514-3520.
    • (2003) J Biol Chem , vol.278 , pp. 3514-3520
    • Ikeda, K.1    Emoto, N.2    Matsuo, M.3    Yokoyama, M.4
  • 24
    • 0346366816 scopus 로고    scopus 로고
    • Newly identified exons encoding novel variants of p94/calpain 3 are expressed ubiquitously and overlap the -glucosidase C gene
    • Kawabata Y, Hata S, Ono Y, Ito Y, Suzuki K, Abe K and Sorimachi H (2003) Newly identified exons encoding novel variants of p94/calpain 3 are expressed ubiquitously and overlap the -glucosidase C gene. FEBS Lett 555: 623-630.
    • (2003) FEBS Lett , vol.555 , pp. 623-630
    • Kawabata, Y.1    Hata, S.2    Ono, Y.3    Ito, Y.4    Suzuki, K.5    Abe, K.6    Sorimachi, H.7
  • 25
    • 0038308480 scopus 로고    scopus 로고
    • Localization of calpain 3 in human skeletal muscle and its alteration in limb-girdle muscular dystrophy 2A muscle
    • Keira Y, Noguchi S, Minami N, Hayashi YK and Nishino I (2003) 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) J BioChem (Tokyo) , vol.133 , pp. 659-664
    • Keira, Y.1    Noguchi, S.2    Minami, N.3    Hayashi, Y.K.4    Nishino, I.5
  • 27
    • 0031172869 scopus 로고    scopus 로고
    • Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs
    • Kinbara K, Sorimachi H, Ishiura S and Suzuki K (1997) Muscle-specific calpain, p94, interacts with the extreme C-terminal region of connectin, a unique region flanked by two immunoglobulin C2 motifs. Arch BioChem Biophys 342: 99-107.
    • (1997) Arch BioChem Biophys , vol.342 , pp. 99-107
    • Kinbara, K.1    Sorimachi, H.2    Ishiura, S.3    Suzuki, K.4
  • 28
    • 0032749982 scopus 로고    scopus 로고
    • Control of segmental expression of the cardiac-restricted ankyrin repeat protein gene by distinct regulatory pathways in marine cardiogenesis
    • Kuo H, Chen J, Ruiz-Lozano P, Zou Y, Nemer M and Chien KR (1999) Control of segmental expression of the cardiac-restricted ankyrin repeat protein gene by distinct regulatory pathways in marine cardiogenesis. Devlopment 126: 4223-4234.
    • (1999) Devlopment , vol.126 , pp. 4223-4234
    • Kuo, H.1    Chen, J.2    Ruiz-Lozano, P.3    Zou, Y.4    Nemer, M.5    Chien, K.R.6
  • 29
    • 0026582867 scopus 로고
    • Towards a molecular understanding of titin
    • Labeit S, Gautel M, Lakey A and Trinick J (1992) Towards a molecular understanding of titin. EMBO J 11: 1711-1716.
    • (1992) EMBO J , vol.11 , pp. 1711-1716
    • Labeit, S.1    Gautel, M.2    Lakey, A.3    Trinick, J.4
  • 30
    • 0028824480 scopus 로고
    • Titins: Giant proteins in charge of muscle ultrastructure and elasticity
    • Labeit S and Kolmerer B (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270: 293-296.
    • (1995) Science , vol.270 , pp. 293-296
    • Labeit, S.1    Kolmerer, B.2
  • 32
    • 0031892439 scopus 로고    scopus 로고
    • Cloning and expression of mRNA for calpain Lp82 from rat lens: Splice variant of p94
    • Ma H, Fukiage C, Azuma M and Shearer TR (1998) Cloning and expression of mRNA for calpain Lp82 from rat lens: splice variant of p94. Invest Ophthalmol Vis Sci 39: 454-461.
    • (1998) Invest Ophthalmol Vis Sci , vol.39 , pp. 454-461
    • Ma, H.1    Fukiage, C.2    Azuma, M.3    Shearer, T.R.4
  • 33
    • 0017163222 scopus 로고
    • Connectin, an elastic protein from myofibrils
    • Maruyama K (1976) Connectin, an elastic protein from myofibrils. J BioChem 80: 405-407.
    • (1976) J BioChem , vol.80 , pp. 405-407
    • Maruyama, K.1
  • 34
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • McElhinny AS, Kakinuma K, Sorimachi H, Labeit S and Gregorio CC (2002) Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol 157: 125-136.
    • (2002) J Cell Biol , vol.157 , pp. 125-136
    • McElhinny, A.S.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.C.5
  • 38
    • 0032557642 scopus 로고    scopus 로고
    • Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin
    • Mues A, Ven PFMvd , Young P, Fürst DO and Gautel M (1998) Two immunoglobulin-like domains of the Z-disc portion of titin interact in a conformation-dependent way with telethonin. FEBS Lett 428: 111-114.
    • (1998) FEBS Lett , vol.428 , pp. 111-114
    • Mues, A.1    Ven, P.F.Mvd.2    Young, P.3    Fürst, D.O.4    Gautel, M.5
  • 40
    • 0031027371 scopus 로고    scopus 로고
    • Binding of the N-terminal 63 kDa portion of connectin/titin to alpha-actinin as Rev.ealed by the yeast two-hybrid system
    • Ohtsuka H, Yajima H, Maruyama K and Kimura S (1997) Binding of the N-terminal 63 kDa portion of connectin/titin to alpha-actinin as Rev.ealed by the yeast two-hybrid system. FEBS Lett 401: 65-67.
    • (1997) FEBS Lett , vol.401 , pp. 65-67
    • Ohtsuka, H.1    Yajima, H.2    Maruyama, K.3    Kimura, S.4
  • 43
    • 0032479445 scopus 로고    scopus 로고
    • Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A
    • Ono Y, Shimada H, Sorimachi H, Richard I, Saido TC, Beckmann JS, Ishiura S and Suzuki K (1998) Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J Biol Chem 273: 17073-17078.
    • (1998) J Biol Chem , vol.273 , pp. 17073-17078
    • Ono, Y.1    Shimada, H.2    Sorimachi, H.3    Richard, I.4    Saido, T.C.5    Beckmann, J.S.6    Ishiura, S.7    Suzuki, K.8
  • 45
    • 3042822256 scopus 로고    scopus 로고
    • m-calpain implication in cell cycle during muscle precursor activation
    • Raynaud F, Carnac G, Marcihac A and Benyamin Y (2004) m-calpain implication in cell cycle during muscle precursor activation. Exp Cell Res 298: 48-57.
    • (2004) Exp Cell Res , vol.298 , pp. 48-57
    • Raynaud, F.1    Carnac, G.2    Marcihac, A.3    Benyamin, Y.4
  • 46
    • 0037132543 scopus 로고    scopus 로고
    • 2+ dependent intramolecular autolysis
    • 2+ dependent intramolecular autolysis. FEBS Lett 532: 401-406.
    • (2002) FEBS Lett , vol.532 , pp. 401-406
    • Rey, M.A.1    Davies, P.L.2
  • 48
    • 0027474051 scopus 로고
    • Widespread activation of calcium-activated neutral proteinase (Calpain) in the brain in Alzheimer disease: A potential molecular basis for neuronal degeneration
    • Saito K, Elce JS, Hamos JE and Nixon RA (1993) Widespread activation of calcium-activated neutral proteinase (Calpain) in the brain in Alzheimer disease: a potential molecular basis for neuronal degeneration. Pro Natl Acad Sci USA 90: 2628-2632.
    • (1993) Pro Natl Acad Sci USA , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.A.4
  • 49
    • 0344759163 scopus 로고    scopus 로고
    • Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy
    • Salmikangas P, Mykkanen OM, Gronholm M, Heiska L, Kere J and Carpen O (1999) Myotilin, a novel sarcomeric protein with two Ig-like domains, is encoded by a candidate gene for limb-girdle muscular dystrophy. Hum Mol Genet 8: 1329-1336.
    • (1999) Hum Mol Genet , vol.8 , pp. 1329-1336
    • Salmikangas, P.1    Mykkanen, O.M.2    Gronholm, M.3    Heiska, L.4    Kere, J.5    Carpen, O.6
  • 52
    • 0034992155 scopus 로고    scopus 로고
    • The structure of calpain
    • Sorimachi H and Suzuki K (2001) The structure of calpain. J BioChem 129: 653-664.
    • (2001) J BioChem , vol.129 , pp. 653-664
    • Sorimachi, H.1    Suzuki, K.2
  • 54
    • 0027536473 scopus 로고
    • A survey of interactions made by the giant protein titin
    • Soteriou A, Gamage M and Trinick J (1993) A survey of interactions made by the giant protein titin. J Cell Sci 104: 119-123.
    • (1993) J Cell Sci , vol.104 , pp. 119-123
    • Soteriou, A.1    Gamage, M.2    Trinick, J.3
  • 57
    • 0036803243 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins
    • Tompa P (2002) Intrinsically unstructured proteins. Trends BioChem Sci 27: 523-533.
    • (2002) Trends BioChem Sci , vol.27 , pp. 523-533
    • Tompa, P.1
  • 61
    • 0011450535 scopus 로고
    • Titin: Major myofibrillar components of striated muscle
    • Wang K, McClure J and Tu A (1979) Titin: major myofibrillar components of striated muscle. Pro Natl Acad Sci USA 76: 3698-3702.
    • (1979) Pro Natl Acad Sci USA , vol.76 , pp. 3698-3702
    • Wang, K.1    McClure, J.2    Tu, A.3
  • 64
    • 0031029447 scopus 로고    scopus 로고
    • CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5 homeobox gene pathway
    • Zou Y, Evans S, Chen J, Kuo HC, Harvey RP and Chien KR (1997) CARP, a cardiac ankyrin repeat protein, is downstream in the Nkx2-5 homeobox gene pathway. Development 124: 793-804.
    • (1997) Development , vol.124 , pp. 793-804
    • Zou, Y.1    Evans, S.2    Chen, J.3    Kuo, H.C.4    Harvey, R.P.5    Chien, K.R.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.