메뉴 건너뛰기




Volumn 120, Issue 8, 2010, Pages 2672-2683

Dynamic distribution of muscle-specific calpain in mice has a key role in physical-stress adaptation and is impaired in muscular dystrophy

(22)  Ojima, Koichi a,b,c   Kawabata, Yukiko b,d,e   Nakao, Harumi e,f   Nakao, Kazuki g   Doi, Naoko a,b   Kitamura, Fujiko a   Ono, Yasuko a,b   Hata, Shoji a   Suzuki, Hidenori h   Kawahara, Hiroyuki i   Bogomolovas, Julius j   Witt, Christian j   Ottenheijm, Coen k   Labeit, Siegfried j   Granzier, Henk k   Toyama Sorimachi, Noriko l   Sorimachi, Michiko m   Suzuki, Koichi n,o   Maeda, Tatsuya b,o   Abe, Keiko d   more..

g RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; CALPAIN 3; HEAT SHOCK PROTEIN; MUSCLE ANKYRIN REPEAT PROTEIN 2; UNCLASSIFIED DRUG;

EID: 77955298542     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI40658     Document Type: Article
Times cited : (87)

References (45)
  • 2
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard I, et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell. 1995;81(1):27-40.
    • (1995) Cell , vol.81 , Issue.1 , pp. 27-40
    • Richard, I.1
  • 3
    • 36749092258 scopus 로고    scopus 로고
    • Analysis of the UK diagnostic strategy for limb girdle muscular dystrophy 2A
    • Groen EJ, et al. Analysis of the UK diagnostic strategy for limb girdle muscular dystrophy 2A. Brain. 2007;130(pt 12):3237-3249.
    • (2007) Brain , vol.130 , Issue.PART 12 , pp. 3237-3249
    • Groen, E.J.1
  • 4
    • 0346216799 scopus 로고    scopus 로고
    • Molecular bases of autosomal recessive limb-girdle muscular dystrophies
    • Nigro V. Molecular bases of autosomal recessive limb-girdle muscular dystrophies. Acta Myol. 2003;22(2):35-42.
    • (2003) Acta Myol , vol.22 , Issue.2 , pp. 35-42
    • Nigro, V.1
  • 5
    • 33746129198 scopus 로고    scopus 로고
    • Calpain 3: A key regulator of the sarcomere?
    • Duguez S, Bartoli M, Richard I. Calpain 3: a key regulator of the sarcomere? FEBS J. 2006;273(15):3427-3436.
    • (2006) FEBS J , vol.273 , Issue.15 , pp. 3427-3436
    • Duguez, S.1    Bartoli, M.2    Richard, I.3
  • 6
    • 77955300901 scopus 로고    scopus 로고
    • Leiden Muscular Dystrophy pages. Updated March 28, Accessed May 13, 2010
    • Leiden Muscular Dystrophy pages. Leiden Open Variation Database. http://www.dmd.nl/capn3-seqvar.html. Updated March 28, 2010. Accessed May 13, 2010.
    • (2010) Leiden Open Variation Database
  • 7
    • 0842328803 scopus 로고    scopus 로고
    • Structure, activation, and biology of calpain
    • Suzuki K, Hata S, Kawabata Y, Sorimachi H. Structure, activation, and biology of calpain. Diabetes 2004;53(suppl):S12-S18.
    • (2004) Diabetes , vol.53 , Issue.SUPPL.
    • Suzuki, K.1    Hata, S.2    Kawabata, Y.3    Sorimachi, H.4
  • 9
    • 0033361883 scopus 로고    scopus 로고
    • Calpainopathy - A survey of mutations and polymorphisms
    • Richard I, et al. Calpainopathy-a survey of mutations and polymorphisms. Am J Hum Genet. 1999;64(6):1524-1540.
    • (1999) Am J Hum Genet , vol.64 , Issue.6 , pp. 1524-1540
    • Richard, I.1
  • 10
    • 20144389936 scopus 로고    scopus 로고
    • LGMD2A: Genotype-phenotype correlations based on a large mutational survey on the calpain 3 gene
    • Saenz A, et al. LGMD2A: genotype-phenotype correlations based on a large mutational survey on the calpain 3 gene. Brain. 2005;128(pt 4):732-742.
    • (2005) Brain , vol.128 , Issue.PART 4 , pp. 732-742
    • Saenz, A.1
  • 11
    • 24944464625 scopus 로고    scopus 로고
    • Extensive scanning of the calpain-3 gene broadens the spectrum of LGMD2A phenotypes
    • Piluso G, et al. Extensive scanning of the calpain-3 gene broadens the spectrum of LGMD2A phenotypes. J Med Genet. 2005;42(9):686-693.
    • (2005) J Med Genet , vol.42 , Issue.9 , pp. 686-693
    • Piluso, G.1
  • 12
    • 0001634301 scopus 로고    scopus 로고
    • Myopathy phenotype of transgenic mice expressing active site-mutated inactive p94 skeletal muscle-specific calpain, the gene product responsible for limb girdle muscular dystrophy type 2A
    • Tagawa K, et al. Myopathy phenotype of transgenic mice expressing active site-mutated inactive p94 skeletal muscle-specific calpain, the gene product responsible for limb girdle muscular dystrophy type 2A. Hum Mol Genet. 2000;9(9):1393-1402.
    • (2000) Hum Mol Genet , vol.9 , Issue.9 , pp. 1393-1402
    • Tagawa, K.1
  • 13
    • 0034739841 scopus 로고    scopus 로고
    • Loss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IkBa/nuclear factor kB pathway perturbation in mice
    • Richard I, et al. Loss of calpain 3 proteolytic activity leads to muscular dystrophy and to apoptosis-associated IkBa/nuclear factor kB pathway perturbation in mice. J Cell Biol. 2000;151(7):1583-1590.
    • (2000) J Cell Biol , vol.151 , Issue.7 , pp. 1583-1590
    • Richard, I.1
  • 14
    • 3242725958 scopus 로고    scopus 로고
    • Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro
    • Kramerova I, Kudryashova E, Tidball JG, Spencer MJ. Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro. Hum Mol Genet. 2004;13(13):1373-1388.
    • (2004) Hum Mol Genet , vol.13 , Issue.13 , pp. 1373-1388
    • Kramerova, I.1    Kudryashova, E.2    Tidball, J.G.3    Spencer, M.J.4
  • 15
    • 13344285357 scopus 로고
    • Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence
    • Sorimachi H, et al. Muscle-specific calpain, p94, responsible for limb girdle muscular dystrophy type 2A, associates with connectin through IS2, a p94-specific sequence. J Biol Chem. 1995;270(52):31158-31162.
    • (1995) J Biol Chem , vol.270 , Issue.52 , pp. 31158-31162
    • Sorimachi, H.1
  • 16
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • Granzier HL, Labeit S. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ Res. 2004;94(3):284-295.
    • (2004) Circ Res , vol.94 , Issue.3 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 17
    • 47249105570 scopus 로고    scopus 로고
    • Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle
    • Hayashi C, et al. Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle. J Biol Chem. 2008;283(21):14801-14814.
    • (2008) J Biol Chem , vol.283 , Issue.21 , pp. 14801-14814
    • Hayashi, C.1
  • 18
    • 9144273787 scopus 로고    scopus 로고
    • Induction and myofibrillar targeting of CARP, and suppression of the Nkx2.5 pathway in the MDM mouse with impaired titin-based signaling
    • Witt CC, et al. Induction and myofibrillar targeting of CARP, and suppression of the Nkx2.5 pathway in the MDM mouse with impaired titin-based signaling. J Mol Biol. 2004;336(1):145-154.
    • (2004) J Mol Biol , vol.336 , Issue.1 , pp. 145-154
    • Witt, C.C.1
  • 19
    • 34347221228 scopus 로고    scopus 로고
    • Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain
    • Ojima K, et al. Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain. J Biol Chem. 2007;282(19):14493-14504.
    • (2007) J Biol Chem , vol.282 , Issue.19 , pp. 14493-14504
    • Ojima, K.1
  • 20
    • 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
    • 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. 2007;103(3):926-931.
    • (2007) J Appl Physiol , 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
  • 21
    • 0026729383 scopus 로고
    • Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage
    • McNeil PL, Khakee R. Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage. Am J Pathol. 1992;140(5):1097-1109.
    • (1992) Am J Pathol , vol.140 , Issue.5 , pp. 1097-1109
    • McNeil, P.L.1    Khakee, R.2
  • 22
    • 18044365204 scopus 로고    scopus 로고
    • Dynamics of Z-band based proteins in developing skeletal muscle cells
    • Wang J, et al. Dynamics of Z-band based proteins in developing skeletal muscle cells. Cell Motil Cytoskeleton. 2005;61(1):34-48.
    • (2005) Cell Motil Cytoskeleton , vol.61 , Issue.1 , pp. 34-48
    • Wang, J.1
  • 23
    • 33646715144 scopus 로고    scopus 로고
    • NFATc1 nucleocytoplasmic shuttling is controlled by nerve activity in skeletal muscle
    • Tothova J, et al. NFATc1 nucleocytoplasmic shuttling is controlled by nerve activity in skeletal muscle. J Cell Sci. 2006;119(pt 8):1604-1611.
    • (2006) J Cell Sci , vol.119 , Issue.PART 8 , pp. 1604-1611
    • Tothova, J.1
  • 24
    • 51649101588 scopus 로고    scopus 로고
    • Mechanoenzymatics of titin kinase
    • Puchner EM, et al. Mechanoenzymatics of titin kinase. Proc Natl Acad Sci U S A. 2008;105(36):13385-13390.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , Issue.36 , pp. 13385-13390
    • Puchner, E.M.1
  • 25
    • 33745817771 scopus 로고    scopus 로고
    • Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system
    • Ono Y, et al. Suppressed disassembly of autolyzing p94/CAPN3 by N2A connectin/titin in a genetic reporter system. J Biol Chem. 2006;281(27):18519- 18531.
    • (2006) J Biol Chem , vol.281 , Issue.27 , pp. 18519-18531
    • Ono, Y.1
  • 26
    • 33645944669 scopus 로고    scopus 로고
    • Stress-dependent and -independent expression of the myogenic regulatory factors and the MARP genes after eccentric contractions in rats
    • Hentzen ER, et al. Stress-dependent and -independent expression of the myogenic regulatory factors and the MARP genes after eccentric contractions in rats. J Physiol. 2006;570(pt 1):157-167.
    • (2006) J Physiol , vol.570 , Issue.PART 1 , pp. 157-167
    • Hentzen, E.R.1
  • 27
    • 66149156297 scopus 로고    scopus 로고
    • Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains
    • Lehti M, Kivela R, Komi P, Komulainen J, Kainulainen H, Kyrolainen H. Effects of fatiguing jumping exercise on mRNA expression of titin-complex proteins and calpains. J Appl Physiol. 2009;106(4):1419-1424.
    • (2009) J Appl Physiol , vol.106 , Issue.4 , pp. 1419-1424
    • Lehti, M.1    Kivela, R.2    Komi, P.3    Komulainen, J.4    Kainulainen, H.5    Kyrolainen, H.6
  • 28
    • 2342479800 scopus 로고    scopus 로고
    • The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle
    • Kojic S, et al. The Ankrd2 protein, a link between the sarcomere and the nucleus in skeletal muscle. J Mol Biol. 2004;339(2):313-325.
    • (2004) J Mol Biol , vol.339 , Issue.2 , pp. 313-325
    • Kojic, S.1
  • 29
    • 0032955751 scopus 로고    scopus 로고
    • Dysferlin is a plasma membrane protein and is expressed early in human development
    • Anderson LV, et al. Dysferlin is a plasma membrane protein and is expressed early in human development. Hum Mol Genet. 1999;8(5):855-861.
    • (1999) Hum Mol Genet , vol.8 , Issue.5 , pp. 855-861
    • Anderson, L.V.1
  • 30
    • 33344455688 scopus 로고    scopus 로고
    • Intracellular localization of dysferlin and its association with the dihydropyridine receptor
    • Ampong BN, Imamura M, Matsumiya T, Yoshida M, Takeda S. Intracellular localization of dysferlin and its association with the dihydropyridine receptor. Acta Myol. 2005;24(2):134-144.
    • (2005) Acta Myol , vol.24 , Issue.2 , pp. 134-144
    • Ampong, B.N.1    Imamura, M.2    Matsumiya, T.3    Yoshida, M.4    Takeda, S.5
  • 32
    • 3042597817 scopus 로고    scopus 로고
    • Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide
    • Diaz BG, Moldoveanu T, Kuiper MJ, Campbell RL, Davies PL. Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide. J Biol Chem. 2004;279(26):27656-27666.
    • (2004) J Biol Chem , 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
  • 33
    • 0037132543 scopus 로고    scopus 로고
    • 2+ dependent intramolecular autolysis
    • 2+ dependent intramolecular autolysis. FEBS Lett. 2002;532(3):401-406.
    • (2002) FEBS Lett , vol.532 , Issue.3 , pp. 401-406
    • Rey, M.A.1    Davies, P.L.2
  • 34
    • 0142247618 scopus 로고    scopus 로고
    • The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules
    • Miller MK, et al. The muscle ankyrin repeat proteins: CARP, ankrd2/Arpp and DARP as a family of titin filament-based stress response molecules. J Mol Biol. 2003;333(5):951-964.
    • (2003) J Mol Biol , vol.333 , Issue.5 , pp. 951-964
    • Miller, M.K.1
  • 35
    • 0034816094 scopus 로고    scopus 로고
    • Characterization of human skeletal muscle Ankrd2
    • Pallavicini A, et al. Characterization of human skeletal muscle Ankrd2. Biochem Biophys Res Commun. 2001;285(2):378-386.
    • (2001) Biochem Biophys Res Commun , vol.285 , Issue.2 , pp. 378-386
    • Pallavicini, A.1
  • 36
    • 43549116105 scopus 로고    scopus 로고
    • The effects of Ankrd2 alteration indicate its involvement in cell cycle regulation during muscle differentiation
    • Bean C, Facchinello N, Faulkner G, Lanfranchi G. The effects of Ankrd2 alteration indicate its involvement in cell cycle regulation during muscle differentiation. Biochim Biophys Acta. 2008;1783(6):1023-1035.
    • (2008) Biochim Biophys Acta , vol.1783 , Issue.6 , pp. 1023-1035
    • Bean, C.1    Facchinello, N.2    Faulkner, G.3    Lanfranchi, G.4
  • 37
    • 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, Nishino I. Localization of calpain 3 in human skeletal muscle and its alteration in limb-girdle muscular dystrophy 2A muscle. J Biochem. 2003;133(5):659-664.
    • (2003) J Biochem , vol.133 , Issue.5 , pp. 659-664
    • Keira, Y.1    Noguchi, S.2    Minami, N.3    Hayashi, Y.K.4    Nishino, I.5
  • 38
    • 34447127547 scopus 로고    scopus 로고
    • Mutations of CAPN3 in Korean patients with limb-girdle muscular dystrophy
    • Shin JH, Kim HS, Lee CH, Kim CM, Park KH, Kim DS. Mutations of CAPN3 in Korean patients with limb-girdle muscular dystrophy. J Korean Med Sci. 2007;22(3):463-469.
    • (2007) J Korean Med Sci , vol.22 , Issue.3 , pp. 463-469
    • Shin, J.H.1    Kim, H.S.2    Lee, C.H.3    Kim, C.M.4    Park, K.H.5    Kim, D.S.6
  • 39
    • 0022455570 scopus 로고
    • Myofibrillogenesis in living cells microinjected with fluorescently labeled alpha-actinin
    • Sanger JM, Mittal B, Pochapin MB, Sanger JW. Myofibrillogenesis in living cells microinjected with fluorescently labeled alpha-actinin. J Cell Biol. 1986;102(6):2053-2066.
    • (1986) J Cell Biol , vol.102 , Issue.6 , pp. 2053-2066
    • Sanger, J.M.1    Mittal, B.2    Pochapin, M.B.3    Sanger, J.W.4
  • 40
    • 0035368688 scopus 로고    scopus 로고
    • Eccentric exercise-induced morphological changes in the membrane systems involved in excitation-contraction coupling in rat skeletal muscle
    • Takekura H, Fujinami N, Nishizawa T, Ogasawara H, Kasuga N. Eccentric exercise-induced morphological changes in the membrane systems involved in excitation-contraction coupling in rat skeletal muscle. J Physiol. 2001;533(pt 2):571-583.
    • (2001) J Physiol , vol.533 , Issue.PART 2 , pp. 571-583
    • Takekura, H.1    Fujinami, N.2    Nishizawa, T.3    Ogasawara, H.4    Kasuga, N.5
  • 41
    • 0028817970 scopus 로고
    • Visualization of dystrophic muscle fibers in mdx mouse by vital staining with Evans blue: Evidence of apoptosis in dystrophin-deficient muscle
    • Matsuda R, Nishikawa A, Tanaka H. Visualization of dystrophic muscle fibers in mdx mouse by vital staining with Evans blue: evidence of apoptosis in dystrophin-deficient muscle. J Biochem. 1995;118(5):959-964.
    • (1995) J Biochem , vol.118 , Issue.5 , pp. 959-964
    • Matsuda, R.1    Nishikawa, A.2    Tanaka, H.3
  • 42
    • 3843108956 scopus 로고    scopus 로고
    • Mac-1(low) early myeloid cells in the bone marrow-derived SP fraction migrate into injured skeletal muscle and participate in muscle regeneration
    • Ojima K, et al. Mac-1(low) early myeloid cells in the bone marrow-derived SP fraction migrate into injured skeletal muscle and participate in muscle regeneration. Biochem Biophys Res Commun. 2004;321(4):1050-1061.
    • (2004) Biochem Biophys Res Commun , vol.321 , Issue.4 , pp. 1050-1061
    • Ojima, K.1
  • 43
    • 0027276561 scopus 로고
    • Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle
    • Sorimachi H, et al. Muscle-specific calpain, p94, is degraded by autolysis immediately after translation, resulting in disappearance from muscle. J Biol Chem. 1993;268(14):10593-10605.
    • (1993) J Biol Chem , vol.268 , Issue.14 , pp. 10593-10605
    • Sorimachi, H.1
  • 44
    • 34249657818 scopus 로고    scopus 로고
    • Comprehensive survey of p94/calpain 3 substrates by comparative proteomics-possible regulation of protein synthesis by p94
    • Ono Y, et al. Comprehensive survey of p94/calpain 3 substrates by comparative proteomics-possible regulation of protein synthesis by p94. Biotechnol J. 2007;2(5):565-576.
    • (2007) Biotechnol J , vol.2 , Issue.5 , pp. 565-576
    • Ono, Y.1
  • 45
    • 0030305457 scopus 로고    scopus 로고
    • A language for data analysis and graphics
    • Ihaka R, Gentleman R. R: a language for data analysis and graphics. J Comp Graph Stat. 1996;(3):299-314.
    • (1996) J Comp Graph Stat , Issue.3 , pp. 299-314
    • Ihaka, R.1    Gentleman, R.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.