메뉴 건너뛰기




Volumn 96, Issue 1, 2012, Pages 46-52

Cooperation between proteolytic systems in cardiomyocyte recycling

Author keywords

Autophagy; Calpain; Heart failure; Ubiquitin proteasome

Indexed keywords

CALCIUM ION; CALPAIN; CYTOSKELETON PROTEIN; DYSTROPHIN; PROTEASOME; UBIQUITIN;

EID: 84866681808     PISSN: 00086363     EISSN: 17553245     Source Type: Journal    
DOI: 10.1093/cvr/cvs236     Document Type: Review
Times cited : (26)

References (100)
  • 2
    • 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 1):S12-S18.
    • (2004) Diabetes , vol.53 , Issue.SUPPL. 1
    • Suzuki, K.1    Hata, S.2    Kawabata, Y.3    Sorimachi, H.4
  • 3
    • 0020670899 scopus 로고
    • Mechanisms of degradation of myofibrillar and nonmyofibrillar protein in heart
    • Ord JM, Wakeland JR, Crie JS, Wildenthal K. Mechanisms of degradation of myofibrillar and nonmyofibrillar protein in heart. Adv Myocardiol 1983;4:195-199.
    • (1983) Adv Myocardiol , vol.4 , pp. 195-199
    • Ord, J.M.1    Wakeland, J.R.2    Crie, J.S.3    Wildenthal, K.4
  • 4
    • 0021776799 scopus 로고
    • The role of lysosomes in the degradation of myofibrillar and non-myofibrillar proteins in heart
    • Wildenthal K, Wakeland JR. The role of lysosomes in the degradation of myofibrillar and non-myofibrillar proteins in heart. Prog Clin Biol Res 1985;180:511-520.
    • (1985) Prog Clin Biol Res , vol.180 , pp. 511-520
    • Wildenthal, K.1    Wakeland, J.R.2
  • 5
    • 0020806422 scopus 로고
    • Susceptibilities of cardiac myofibrillar proteins to cathepsin D-catalyzed degradation
    • Jones TL, Ogunro EA, Samarel AM, Ferguson AG, Lesch M. Susceptibilities of cardiac myofibrillar proteins to cathepsin D-catalyzed degradation. Am J Physiol 1983;245:H294-H299.
    • (1983) Am J Physiol , vol.245
    • Jones, T.L.1    Ogunro, E.A.2    Samarel, A.M.3    Ferguson, A.G.4    Lesch, M.5
  • 6
    • 0026584008 scopus 로고
    • Autophagy and other vacuolar protein degradation mechanisms
    • Seglen PO, Bohley P. Autophagy and other vacuolar protein degradation mechanisms. Experientia 1992;48:158-172.
    • (1992) Experientia , vol.48 , pp. 158-172
    • Seglen, P.O.1    Bohley, P.2
  • 7
    • 0028222874 scopus 로고
    • Autophagy and related mechanisms of lysosome-mediated protein degradation
    • Dunn WA Jr. Autophagy and related mechanisms of lysosome-mediated protein degradation. Trends Cell Biol 1994;4:139-143.
    • (1994) Trends Cell Biol , vol.4 , pp. 139-143
    • Dunn Jr., W.A.1
  • 8
    • 0030957959 scopus 로고    scopus 로고
    • Autophagic proteolysis: Control and specificity
    • Blommaart EF, Luiken JJ, Meijer AJ. Autophagic proteolysis: control and specificity. Histochem J 1997;29:365-385.
    • (1997) Histochem J , vol.29 , pp. 365-385
    • Blommaart, E.F.1    Luiken, J.J.2    Meijer, A.J.3
  • 10
    • 1842583789 scopus 로고    scopus 로고
    • Development by self-digestion: Molecular mechanisms and biological functions of autophagy
    • Levine B, Klionsky DJ. Development by self-digestion: molecular mechanisms and biological functions of autophagy. Dev Cell 2004;6:463-477.
    • (2004) Dev Cell , vol.6 , pp. 463-477
    • Levine, B.1    Klionsky, D.J.2
  • 11
    • 11144245626 scopus 로고    scopus 로고
    • The role of autophagy during the early neonatal starvation period
    • Kuma A, Hatano M, Matsui M, Yamamoto A, Nakaya H, Yoshimori T et al. The role of autophagy during the early neonatal starvation period. Nature 2004; 432:1032-1036.
    • (2004) Nature , vol.432 , pp. 1032-1036
    • Kuma, A.1    Hatano, M.2    Matsui, M.3    Yamamoto, A.4    Nakaya, H.5    Yoshimori, T.6
  • 12
    • 37649005234 scopus 로고    scopus 로고
    • Autophagy in the pathogenesis of disease
    • Levine B, Kroemer G. Autophagy in the pathogenesis of disease. Cell 2008; 132:27-42.
    • (2008) Cell , vol.132 , pp. 27-42
    • Levine, B.1    Kroemer, G.2
  • 13
    • 0027424777 scopus 로고
    • Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae
    • Tsukada M, Ohsumi Y. Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae. FEBS Lett 1993;333:169-174.
    • (1993) FEBS Lett , vol.333 , pp. 169-174
    • Tsukada, M.1    Ohsumi, Y.2
  • 15
    • 33745192802 scopus 로고    scopus 로고
    • Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
    • Hara T, Nakamura K, Matsui M, Yamamoto A, Nakahara Y, Suzuki-Migishima R et al. Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 2006;441:885-889.
    • (2006) Nature , vol.441 , pp. 885-889
    • Hara, T.1    Nakamura, K.2    Matsui, M.3    Yamamoto, A.4    Nakahara, Y.5    Suzuki-Migishima, R.6
  • 16
    • 33646800306 scopus 로고    scopus 로고
    • Loss of autophagy in the central nervous system causes neurodegeneration in mice
    • Komatsu M, Waguri S, Chiba T, Murata S, Iwata J, Tanida I et al. Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 2006; 441:880-884.
    • (2006) Nature , vol.441 , pp. 880-884
    • Komatsu, M.1    Waguri, S.2    Chiba, T.3    Murata, S.4    Iwata, J.5    Tanida, I.6
  • 17
    • 0018827202 scopus 로고
    • Lysosomal alterations in hypoxic and reoxygenated hearts. I. Ultrastructural and cytochemical changes
    • Decker RS, Wildenthal K. Lysosomal alterations in hypoxic and reoxygenated hearts. I. Ultrastructural and cytochemical changes. Am J Pathol 1980;98:425-444.
    • (1980) Am J Pathol , vol.98 , pp. 425-444
    • Decker, R.S.1    Wildenthal, K.2
  • 19
    • 0034755977 scopus 로고    scopus 로고
    • Autophagic degeneration as a possible mechanism of myocardial cell death in dilated cardiomyopathy
    • Shimomura H, Terasaki F, Hayashi T, Kitaura Y, Isomura T, Suma H. Autophagic degeneration as a possible mechanism of myocardial cell death in dilated cardiomyopathy. Jpn Circ J 2001;65:965-968.
    • (2001) Jpn Circ J , vol.65 , pp. 965-968
    • Shimomura, H.1    Terasaki, F.2    Hayashi, T.3    Kitaura, Y.4    Isomura, T.5    Suma, H.6
  • 20
    • 33144463000 scopus 로고    scopus 로고
    • Autophagic cardiomyocyte death in cardiomyopathic hamsters and its prevention by granulocyte colony-stimulating factor
    • Miyata S, Takemura G, Kawase Y, Li Y, Okada H, Maruyama R et al. Autophagic cardiomyocyte death in cardiomyopathic hamsters and its prevention by granulocyte colony-stimulating factor. Am J Pathol 2006;168:386-397.
    • (2006) Am J Pathol , vol.168 , pp. 386-397
    • Miyata, S.1    Takemura, G.2    Kawase, Y.3    Li, Y.4    Okada, H.5    Maruyama, R.6
  • 21
    • 17044440789 scopus 로고    scopus 로고
    • Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)
    • Nishino I, Fu J, Tanji K, Yamada T, Shimojo S, Koori T et al. Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease). Nature 2000;406:906-910.
    • (2000) Nature , vol.406 , pp. 906-910
    • Nishino, I.1    Fu, J.2    Tanji, K.3    Yamada, T.4    Shimojo, S.5    Koori, T.6
  • 23
    • 59849110194 scopus 로고    scopus 로고
    • Autophagy in ischemic heart disease
    • Gustafsson AB, Gottlieb RA. Autophagy in ischemic heart disease. Circ Res 2009; 104:150-158.
    • (2009) Circ Res , vol.104 , pp. 150-158
    • Gustafsson, A.B.1    Gottlieb, R.A.2
  • 26
    • 34249714158 scopus 로고    scopus 로고
    • The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress
    • Nakai A, Yamaguchi O, Takeda T, Higuchi Y, Hikoso S, Taniike M et al. The role of autophagy in cardiomyocytes in the basal state and in response to hemodynamic stress. Nat Med 2007;13:619-624.
    • (2007) Nat Med , vol.13 , pp. 619-624
    • Nakai, A.1    Yamaguchi, O.2    Takeda, T.3    Higuchi, Y.4    Hikoso, S.5    Taniike, M.6
  • 28
    • 34249037565 scopus 로고    scopus 로고
    • Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein
    • Oberstein A, Jeffrey PD, Shi Y. Crystal structure of the Bcl-XL-Beclin 1 peptide complex: Beclin 1 is a novel BH3-only protein. J Biol Chem 2007;282:13123-13132.
    • (2007) J Biol Chem , vol.282 , pp. 13123-13132
    • Oberstein, A.1    Jeffrey, P.D.2    Shi, Y.3
  • 29
    • 0001488499 scopus 로고    scopus 로고
    • Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein
    • Liang XH, Kleeman LK, Jiang HH, Gordon G, Goldman JE, Berry G et al. Protection against fatal Sindbis virus encephalitis by beclin, a novel Bcl-2-interacting protein. J Virol 1998;72:8586-8596.
    • (1998) J Virol , vol.72 , pp. 8586-8596
    • Liang, X.H.1    Kleeman, L.K.2    Jiang, H.H.3    Gordon, G.4    Goldman, J.E.5    Berry, G.6
  • 30
    • 19544373434 scopus 로고    scopus 로고
    • Beclin 1 augmented cisdiamminedichloroplatinum induced apoptosis via enhancing caspase-9 activity
    • Furuya D, Tsuji N, Yagihashi A, Watanabe N. Beclin 1 augmented cisdiamminedichloroplatinum induced apoptosis via enhancing caspase-9 activity. Exp Cell Res 2005;307:26-40.
    • (2005) Exp Cell Res , vol.307 , pp. 26-40
    • Furuya, D.1    Tsuji, N.2    Yagihashi, A.3    Watanabe, N.4
  • 31
    • 25144457455 scopus 로고    scopus 로고
    • Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy
    • Pattingre S, Tassa A, Qu X, Garuti R, Liang XH, Mizushima N et al. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell 2005;122:927-939.
    • (2005) Cell , vol.122 , pp. 927-939
    • Pattingre, S.1    Tassa, A.2    Qu, X.3    Garuti, R.4    Liang, X.H.5    Mizushima, N.6
  • 36
  • 37
    • 57649234905 scopus 로고    scopus 로고
    • Autophagy genes and ageing
    • Vellai T. Autophagy genes and ageing. Cell Death Differ 2009;16:94-102.
    • (2009) Cell Death Differ , vol.16 , pp. 94-102
    • Vellai, T.1
  • 38
    • 67650246357 scopus 로고    scopus 로고
    • Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy
    • Okamoto K, Kondo-Okamoto N, Ohsumi Y. Mitochondria-anchored receptor Atg32 mediates degradation of mitochondria via selective autophagy. Dev Cell 2009;17:87-97.
    • (2009) Dev Cell , vol.17 , pp. 87-97
    • Okamoto, K.1    Kondo-Okamoto, N.2    Ohsumi, Y.3
  • 39
    • 67650264633 scopus 로고    scopus 로고
    • Atg32 is a mitochondrial protein that confers selectivity during mitophagy
    • Kanki T, Wang K, Cao Y, Baba M, Klionsky DJ. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev Cell 2009;17:98-109.
    • (2009) Dev Cell , vol.17 , pp. 98-109
    • Kanki, T.1    Wang, K.2    Cao, Y.3    Baba, M.4    Klionsky, D.J.5
  • 40
    • 79952693640 scopus 로고    scopus 로고
    • Mitophagy and Parkinson's disease: The PINK1-parkin link
    • Deas E,Wood NW, Plun-Favreau H. Mitophagy and Parkinson's disease: the PINK1-parkin link. Biochim Biophys Acta 2011;1813:623-633.
    • (2011) Biochim Biophys Acta , vol.1813 , pp. 623-633
    • Deas, E.1    Wood, N.W.2    Plun-Favreau, H.3
  • 42
    • 78651393239 scopus 로고    scopus 로고
    • A role for mitochondria in NLRP3 inflammasome activation
    • Zhou R, Yazdi AS, Menu P, Tschopp J. A role for mitochondria in NLRP3 inflammasome activation. Nature 2011;469:221-225.
    • (2011) Nature , vol.469 , pp. 221-225
    • Zhou, R.1    Yazdi, A.S.2    Menu, P.3    Tschopp, J.4
  • 44
    • 80355127945 scopus 로고    scopus 로고
    • Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes
    • Lee Y, Lee HY, Hanna RA, Gustafsson A B. Mitochondrial autophagy by Bnip3 involves Drp1-mediated mitochondrial fission and recruitment of Parkin in cardiac myocytes. Am J Physiol Heart Circ Physiol 2011;301:H1924-H1931.
    • (2011) Am J Physiol Heart Circ Physiol , vol.301
    • Lee, Y.1    Lee, H.Y.2    Hanna, R.A.3    Gustafsson, A.B.4
  • 46
    • 33748424981 scopus 로고    scopus 로고
    • Protective effect of autophagy in anoxia-reoxygenation of isolated cardiomyocyte?
    • Dosenko VE, Nagibin VS, Tumanovska LV, Moibenko AA. Protective effect of autophagy in anoxia-reoxygenation of isolated cardiomyocyte? Autophagy 2006; 2:305-306.
    • (2006) Autophagy , vol.2 , pp. 305-306
    • Dosenko, V.E.1    Nagibin, V.S.2    Tumanovska, L.V.3    Moibenko, A.A.4
  • 47
    • 34147168105 scopus 로고    scopus 로고
    • Distinct roles of autophagy in the heart during ischemia and reperfusion: Roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy
    • Matsui Y, Takagi H, Qu X, Abdellatif M, Sakoda H, Asano T et al. Distinct roles of autophagy in the heart during ischemia and reperfusion: roles of AMP-activated protein kinase and Beclin 1 in mediating autophagy. Circ Res 2007;100:914-922.
    • (2007) Circ Res , vol.100 , pp. 914-922
    • Matsui, Y.1    Takagi, H.2    Qu, X.3    Abdellatif, M.4    Sakoda, H.5    Asano, T.6
  • 48
    • 33744536558 scopus 로고    scopus 로고
    • Urocortin inhibits Beclin1-mediated autophagic cell death in cardiac myocytes exposed to ischaemia/reperfusion injury
    • Valentim L, Laurence KM, Townsend PA, Carroll CJ, Soond S, Scarabelli TM et al. Urocortin inhibits Beclin1-mediated autophagic cell death in cardiac myocytes exposed to ischaemia/reperfusion injury. J Mol Cell Cardiol 2006;40:846-852.
    • (2006) J Mol Cell Cardiol , vol.40 , pp. 846-852
    • Valentim, L.1    Laurence, K.M.2    Townsend, P.A.3    Carroll, C.J.4    Soond, S.5    Scarabelli, T.M.6
  • 49
    • 0024340134 scopus 로고
    • The role of autolysis in activity of the Ca2+-dependent proteinases (m-calpain and m-calpain)
    • Cong J, Goll DE, Peterson AM, Kapprell HP. The role of autolysis in activity of the Ca2+-dependent proteinases (m-calpain and m-calpain). J Biol Chem 1989; 264:10096-10103.
    • (1989) J Biol Chem , vol.264 , pp. 10096-10103
    • Cong, J.1    Goll, D.E.2    Peterson, A.M.3    Kapprell, H.P.4
  • 50
    • 0025831476 scopus 로고
    • Calcium-activated neutral protease (calpain) system: Structure, function, and regulation
    • Croall DE, DeMartino GN. Calcium-activated neutral protease (calpain) system: structure, function, and regulation. Physiol Rev 1991;71:813-847.
    • (1991) Physiol Rev , vol.71 , pp. 813-847
    • Croall, D.E.1    Demartino, G.N.2
  • 51
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N, Bhatt AK, Dutt P, Greer PA, Arthur JS, Elce JS et al. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J Biol Chem 2001;276:48382-48388.
    • (2001) J Biol Chem , vol.276 , pp. 48382-48388
    • Dourdin, N.1    Bhatt, A.K.2    Dutt, P.3    Greer, P.A.4    Arthur, J.S.5    Elce, J.S.6
  • 52
    • 33745826605 scopus 로고    scopus 로고
    • Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli
    • Tan Y, Wu C, De Veyra T, Greer PA. Ubiquitous calpains promote both apoptosis and survival signals in response to different cell death stimuli. J Biol Chem 2006; 281:17689-17698.
    • (2006) J Biol Chem , vol.281 , pp. 17689-17698
    • Tan, Y.1    Wu, C.2    De Veyra, T.3    Greer, P.A.4
  • 54
    • 34047273570 scopus 로고    scopus 로고
    • Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane
    • Mellgren RL, Zhang W, Miyake K, McNeil PL. Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane. J Biol Chem 2007; 282:2567-2575.
    • (2007) J Biol Chem , vol.282 , pp. 2567-2575
    • Mellgren, R.L.1    Zhang, W.2    Miyake, K.3    McNeil, P.L.4
  • 55
    • 42449114824 scopus 로고    scopus 로고
    • Genetic disruption of calpain correlates with loss of membrane blebbing and differential expression of RhoGDI-1, cofilin and tropomyosin
    • Larsen AK, Lametsch R, Elce J, Larsen JK, Thomsen B, Larsen MR et al. Genetic disruption of calpain correlates with loss of membrane blebbing and differential expression of RhoGDI-1, cofilin and tropomyosin. Biochem J 2008;411:657-666.
    • (2008) Biochem J , vol.411 , pp. 657-666
    • Larsen, A.K.1    Lametsch, R.2    Elce, J.3    Larsen, J.K.4    Thomsen, B.5    Larsen, M.R.6
  • 56
    • 0027313425 scopus 로고
    • Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion
    • Yoshida K, Yamasaki Y, Kawashima S. Calpain activity alters in rat myocardial subfractions after ischemia or reperfusion. Biochim Biophys Acta 1993;1182:215-220.
    • (1993) Biochim Biophys Acta , vol.1182 , pp. 215-220
    • Yoshida, K.1    Yamasaki, Y.2    Kawashima, S.3
  • 57
    • 0032514704 scopus 로고    scopus 로고
    • Role of calpain in skeletal-muscle protein degradation
    • Huang J, Forsberg NE. Role of calpain in skeletal-muscle protein degradation. Proc Natl Acad Sci USA 1998;95:12100-12105.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 12100-12105
    • Huang, J.1    Forsberg, N.E.2
  • 58
    • 0026248168 scopus 로고
    • Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride
    • Whipple G, Koohmaraie M. Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. J Anim Sci 1991; 69:4449-4460.
    • (1991) J Anim Sci , vol.69 , pp. 4449-4460
    • Whipple, G.1    Koohmaraie, M.2
  • 59
    • 0028126638 scopus 로고
    • Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T
    • Ho CY, Stromer MH, Robson RM. Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie 1994; 76:369-375.
    • (1994) Biochimie , vol.76 , pp. 369-375
    • Ho, C.Y.1    Stromer, M.H.2    Robson, R.M.3
  • 61
    • 0033962648 scopus 로고    scopus 로고
    • Calpain-I induced alterations in the cytoskeletal structure and impaired mechanical properties of single myocytes of rat heart
    • Papp Z, van der Velden J, Stienen GJ. Calpain-I induced alterations in the cytoskeletal structure and impaired mechanical properties of single myocytes of rat heart. Cardiovasc Res 2000;45:981-993.
    • (2000) Cardiovasc Res , vol.45 , pp. 981-993
    • Papp, Z.1    Van Der Velden, J.2    Stienen, G.J.3
  • 62
    • 0037047326 scopus 로고    scopus 로고
    • Calpain and mitochondria in ischemia/reperfusion injury
    • Chen M, Won DJ, Krajewski S, Gottlieb RA. Calpain and mitochondria in ischemia/reperfusion injury. J Biol Chem 2002;277:29181-29186.
    • (2002) J Biol Chem , vol.277 , pp. 29181-29186
    • Chen, M.1    Won, D.J.2    Krajewski, S.3    Gottlieb, R.A.4
  • 63
    • 0032934742 scopus 로고    scopus 로고
    • Calpain inhibitor-1 reduces infarct size and DNA fragmentation of myocardium in ischemic/reperfused rat heart
    • Iwamoto H, Miura T, Okamura T, Shirakawa K, Iwatate M, Kawamura S et al. Calpain inhibitor-1 reduces infarct size and DNA fragmentation of myocardium in ischemic/reperfused rat heart. J Cardiovasc Pharmacol 1999;33:580-586.
    • (1999) J Cardiovasc Pharmacol , vol.33 , pp. 580-586
    • Iwamoto, H.1    Miura, T.2    Okamura, T.3    Shirakawa, K.4    Iwatate, M.5    Kawamura, S.6
  • 64
    • 3142654669 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum proteins are targets for calpain action in the ischemic-reperfused heart
    • Singh RB, Chohan PK, Dhalla NS, Netticadan T. The sarcoplasmic reticulum proteins are targets for calpain action in the ischemic-reperfused heart. J Mol Cell Cardiol 2004;37:101-110.
    • (2004) J Mol Cell Cardiol , vol.37 , pp. 101-110
    • Singh, R.B.1    Chohan, P.K.2    Dhalla, N.S.3    Netticadan, T.4
  • 65
    • 28844468063 scopus 로고    scopus 로고
    • Calpain inhibition reduces infarct size and improves global hemodynamics and left ventricular contractility in a porcine myocardial ischemia/reperfusion model
    • Khalil PN, Neuhof C, Huss R, Pollhammer M, Khalil MN, Neuhof H et al. Calpain inhibition reduces infarct size and improves global hemodynamics and left ventricular contractility in a porcine myocardial ischemia/reperfusion model. Eur J Pharmacol 2005;528:124-131.
    • (2005) Eur J Pharmacol , vol.528 , pp. 124-131
    • Khalil, P.N.1    Neuhof, C.2    Huss, R.3    Pollhammer, M.4    Khalil, M.N.5    Neuhof, H.6
  • 67
    • 2442552968 scopus 로고    scopus 로고
    • Translocation and cleavage of myocardial dystrophin as a common pathway to advanced heart failure: A scheme for the progression of cardiac dysfunction
    • Toyo-Oka T, Kawada T, Nakata J, Xie H, Urabe M, Masui F et al. Translocation and cleavage of myocardial dystrophin as a common pathway to advanced heart failure: a scheme for the progression of cardiac dysfunction. Proc Natl Acad Sci USA 2004; 101:7381-7385.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 7381-7385
    • Toyo-Oka, T.1    Kawada, T.2    Nakata, J.3    Xie, H.4    Urabe, M.5    Masui, F.6
  • 68
    • 0035936792 scopus 로고    scopus 로고
    • The genetic basis for cardiomyopathy: From mutation identification to mechanistic paradigms
    • Seidman JG, Seidman C. The genetic basis for cardiomyopathy: from mutation identification to mechanistic paradigms. Cell 2001;104:557-567.
    • (2001) Cell , vol.104 , pp. 557-567
    • Seidman, J.G.1    Seidman, C.2
  • 69
    • 1542331747 scopus 로고    scopus 로고
    • Molecular normalization of dystrophin in the failing left and right ventricle of patients treated with either pulsatile or continuous flow-type ventricular assist devices
    • Vatta M, Stetson SJ, Jimenez S, Entman ML, Noon GP, Bowles NE et al. Molecular normalization of dystrophin in the failing left and right ventricle of patients treated with either pulsatile or continuous flow-type ventricular assist devices. J Am Coll Cardiol 2004;43:811-817.
    • (2004) J Am Coll Cardiol , vol.43 , pp. 811-817
    • Vatta, M.1    Stetson, S.J.2    Jimenez, S.3    Entman, M.L.4    Noon, G.P.5    Bowles, N.E.6
  • 70
    • 80755132135 scopus 로고    scopus 로고
    • Calpain-mediated dystrophin disruption may be a potential structural culprit behind chronic doxorubicin-induced cardiomyopathy
    • Campos EC, O'Connell JL, Malvestio LM, Romano MM, Ramos SG, Celes MR et al. Calpain-mediated dystrophin disruption may be a potential structural culprit behind chronic doxorubicin-induced cardiomyopathy. Eur J Pharmacol 2011;670:541-553.
    • (2011) Eur J Pharmacol , vol.670 , pp. 541-553
    • Campos, E.C.1    O'Connell, J.L.2    Malvestio, L.M.3    Romano, M.M.4    Ramos, S.G.5    Celes, M.R.6
  • 71
    • 34447620317 scopus 로고    scopus 로고
    • Progression of heart failure was suppressed by inhibition of apoptosis signal-regulating kinase 1 via transcoronary gene transfer
    • Hikoso S, Ikeda Y, Yamaguchi O, Takeda T, Higuchi Y, Hirotani S et al. Progression of heart failure was suppressed by inhibition of apoptosis signal-regulating kinase 1 via transcoronary gene transfer. J Am Coll Cardiol 2007;50:453-462.
    • (2007) J Am Coll Cardiol , vol.50 , pp. 453-462
    • Hikoso, S.1    Ikeda, Y.2    Yamaguchi, O.3    Takeda, T.4    Higuchi, Y.5    Hirotani, S.6
  • 72
    • 11444264720 scopus 로고    scopus 로고
    • Effects of ACE inhibitor and AT1 blocker on dystrophin-related proteins and calpain in failing heart
    • Takahashi M, Tanonaka K, Yoshida H, Oikawa R, Koshimizu M, Daicho T et al. Effects of ACE inhibitor and AT1 blocker on dystrophin-related proteins and calpain in failing heart. Cardiovasc Res 2005;65:356-365.
    • (2005) Cardiovasc Res , vol.65 , pp. 356-365
    • Takahashi, M.1    Tanonaka, K.2    Yoshida, H.3    Oikawa, R.4    Koshimizu, M.5    Daicho, T.6
  • 73
    • 65549097680 scopus 로고    scopus 로고
    • Chronic beta-AR activation-induced calpain activation and impaired eNOS-Akt signaling mediates cardiac injury in ovariectomized female rats
    • Bhuiyan MS, Shioda N, Fukunaga K. Chronic beta-AR activation-induced calpain activation and impaired eNOS-Akt signaling mediates cardiac injury in ovariectomized female rats. Expert Opin Ther Targets 2009;13:275-286.
    • (2009) Expert Opin Ther Targets , vol.13 , pp. 275-286
    • Bhuiyan, M.S.1    Shioda, N.2    Fukunaga, K.3
  • 74
    • 34247121951 scopus 로고    scopus 로고
    • Cardiomyocyte degeneration with calpain deficiency reveals a critical role in protein homeostasis
    • Galvez AS, Diwan A, Odley AM, Hahn HS, Osinska H, Melendez JG et al. Cardiomyocyte degeneration with calpain deficiency reveals a critical role in protein homeostasis. Circ Res 2007;100:1071-1078.
    • (2007) Circ Res , vol.100 , pp. 1071-1078
    • Galvez, A.S.1    Diwan, A.2    Odley, A.M.3    Hahn, H.S.4    Osinska, H.5    Melendez, J.G.6
  • 75
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur JS, Elce JS, Hegadorn C, Williams K, Greer PA. Disruption of the murine calpain small subunit gene, Capn4: calpain is essential for embryonic development but not for cell growth and division. Mol Cell Biol 2000;20:4474-4481.
    • (2000) Mol Cell Biol , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 76
    • 0033788531 scopus 로고    scopus 로고
    • The calpain small subunit gene is essential: Its inactivation results in embryonic lethality
    • Zimmerman UJ, Boring L, Pak JH, Mukerjee N, Wang KK. The calpain small subunit gene is essential: its inactivation results in embryonic lethality. IUBMB life 2000;50: 63-68.
    • (2000) IUBMB Life , vol.50 , pp. 63-68
    • Zimmerman, U.J.1    Boring, L.2    Pak, J.H.3    Mukerjee, N.4    Wang, K.K.5
  • 78
    • 80053589785 scopus 로고    scopus 로고
    • Vital role of the calpain-calpastatin system for placental-integrity- dependent embryonic survival
    • Takano J, Mihira N, Fujioka R, Hosoki E, Chishti AH, Saido TC. Vital role of the calpain-calpastatin system for placental-integrity-dependent embryonic survival. Mol Cell Biol 2011;31:4097-4106.
    • (2011) Mol Cell Biol , vol.31 , pp. 4097-4106
    • Takano, J.1    Mihira, N.2    Fujioka, R.3    Hosoki, E.4    Chishti, A.H.5    Saido, T.C.6
  • 79
    • 0030892186 scopus 로고    scopus 로고
    • Calpain: A cytosolic proteinase active at the membranes
    • Molinari M, Carafoli E. Calpain: a cytosolic proteinase active at the membranes. J Membr Biol 1997;156:1-8.
    • (1997) J Membr Biol , vol.156 , pp. 1-8
    • Molinari, M.1    Carafoli, E.2
  • 80
    • 33745829449 scopus 로고    scopus 로고
    • Spatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation
    • Shao H, Chou J, Baty CJ, Burke NA,Watkins SC, Stolz DB et al. Spatial localization of m-calpain to the plasma membrane by phosphoinositide biphosphate binding during epidermal growth factor receptor-mediated activation. Mol Cell Biol 2006; 26:5481-5496.
    • (2006) Mol Cell Biol , vol.26 , pp. 5481-5496
    • Shao, H.1    Chou, J.2    Baty, C.J.3    Burke Nawatkins, S.C.4    Stolz, D.B.5
  • 81
    • 34548299555 scopus 로고    scopus 로고
    • Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability
    • Ding WX, Ni HM, Gao W, Yoshimori T, Stolz DB, Ron D et al. Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. Am J Pathol 2007;171:513-524.
    • (2007) Am J Pathol , vol.171 , pp. 513-524
    • Ding, W.X.1    Ni, H.M.2    Gao, W.3    Yoshimori, T.4    Stolz, D.B.5    Ron, D.6
  • 82
  • 83
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice
    • Komatsu M, Waguri S, Koike M, Sou YS, Ueno T, Hara T et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice. Cell 2007;131:1149-1163.
    • (2007) Cell , vol.131 , pp. 1149-1163
    • Komatsu, M.1    Waguri, S.2    Koike, M.3    Sou, Y.S.4    Ueno, T.5    Hara, T.6
  • 84
    • 60549093730 scopus 로고    scopus 로고
    • Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates
    • Korolchuk VI, Mansilla A, Menzies FM, Rubinsztein DC. Autophagy inhibition compromises degradation of ubiquitin-proteasome pathway substrates. Mol Cell 2009; 33:517-527.
    • (2009) Mol Cell , vol.33 , pp. 517-527
    • Korolchuk, V.I.1    Mansilla, A.2    Menzies, F.M.3    Rubinsztein, D.C.4
  • 85
    • 60849099049 scopus 로고    scopus 로고
    • A role for NBR1 in autophagosomal degradation of ubiquitinated substrates
    • Kirkin V, Lamark T, Sou YS, Bjørkøy G, Nunn JL, Bruun JA et al. A role for NBR1 in autophagosomal degradation of ubiquitinated substrates. Mol Cell 2009;33:505-516.
    • (2009) Mol Cell , vol.33 , pp. 505-516
    • Kirkin, V.1    Lamark, T.2    Sou, Y.S.3    Bjørkøy, G.4    Nunn, J.L.5    Bruun, J.A.6
  • 86
    • 37649024076 scopus 로고    scopus 로고
    • Small molecule regulators of autophagy identified by an image-based high-throughput screen
    • Zhang L, Yu J, Pan H, Hu P, Hao Y, Cai W et al. Small molecule regulators of autophagy identified by an image-based high-throughput screen. Proc Natl Acad Sci USA 2007;104:19023-19028.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19023-19028
    • Zhang, L.1    Yu, J.2    Pan, H.3    Hu, P.4    Hao, Y.5    Cai, W.6
  • 87
    • 0038504839 scopus 로고    scopus 로고
    • Analgesic action of loperamide, an opioid agonist, and its blocking action on voltagedependent Ca2+ channels
    • Hagiwara K, Nakagawasai O, Murata A, Yamadera F, Miyoshi I, Tan-No K et al. Analgesic action of loperamide, an opioid agonist, and its blocking action on voltagedependent Ca2+ channels. Neurosci Res 2003;46:493-497.
    • (2003) Neurosci Res , vol.46 , pp. 493-497
    • Hagiwara, K.1    Nakagawasai, O.2    Murata, A.3    Yamadera, F.4    Miyoshi, I.5    Tan-No, K.6
  • 88
    • 0028229992 scopus 로고
    • Fluspirilene block of N-type calcium current in NGF-differentiated PC12 cells
    • Grantham CJ, Main MJ, Cannell MB. Fluspirilene block of N-type calcium current in NGF-differentiated PC12 cells. Br J Pharmacol 1994;111:483-488.
    • (1994) Br J Pharmacol , vol.111 , pp. 483-488
    • Grantham, C.J.1    Main, M.J.2    Cannell, M.B.3
  • 89
    • 0030600507 scopus 로고    scopus 로고
    • Inhibition by antipsychotic drugs of L-type Ca2+ channel current in PC12 cells
    • Ito K, Nakazawa K, Koizumi S, Liu M, Takeuchi K, Hashimoto T et al. Inhibition by antipsychotic drugs of L-type Ca2+ channel current in PC12 cells. Eur J Pharmacol 1996;314:143-150.
    • (1996) Eur J Pharmacol , vol.314 , pp. 143-150
    • Ito, K.1    Nakazawa, K.2    Koizumi, S.3    Liu, M.4    Takeuchi, K.5    Hashimoto, T.6
  • 91
    • 75149171923 scopus 로고    scopus 로고
    • Control of basal autophagy by calpain1 mediated cleavage of ATG5
    • Xia HG, Zhang L, Chen G, Zhang T, Liu J, Jin M et al. Control of basal autophagy by calpain1 mediated cleavage of ATG5. Autophagy 2010;6:61-66.
    • (2010) Autophagy , vol.6 , pp. 61-66
    • Xia, H.G.1    Zhang, L.2    Chen, G.3    Zhang, T.4    Liu, J.5    Jin, M.6
  • 92
    • 33646204392 scopus 로고    scopus 로고
    • Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size
    • Hosokawa N, Hara Y, Mizushima N. Generation of cell lines with tetracycline-regulated autophagy and a role for autophagy in controlling cell size. FEBS Lett 2006;580:2623-2629.
    • (2006) FEBS Lett , vol.580 , pp. 2623-2629
    • Hosokawa, N.1    Hara, Y.2    Mizushima, N.3
  • 93
    • 38049098543 scopus 로고    scopus 로고
    • The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy
    • Hanada T, Noda NN, Satomi Y, Ichimura Y, Fujioka Y, Takao T et al. The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 2007;282:37298-37302.
    • (2007) J Biol Chem , vol.282 , pp. 37298-37302
    • Hanada, T.1    Noda, N.N.2    Satomi, Y.3    Ichimura, Y.4    Fujioka, Y.5    Takao, T.6
  • 95
    • 84455172960 scopus 로고    scopus 로고
    • Autophagy Induced by Deficiency of Sphingosine-1-phosphate Phosphohydrolase 1 Is Switched to Apoptosis by Calpain-mediated Autophagy-related Gene 5 (Atg5) Cleavage
    • Lépine S, Allegood JC, Edmonds Y, Milstien S, Spiegel S. Autophagy Induced by Deficiency of Sphingosine-1-phosphate Phosphohydrolase 1 Is Switched to Apoptosis by Calpain-mediated Autophagy-related Gene 5 (Atg5) Cleavage. J Biol Chem 2011;286:44380-44390.
    • (2011) J Biol Chem , vol.286 , pp. 44380-44390
    • Lépine, S.1    Allegood, J.C.2    Edmonds, Y.3    Milstien, S.4    Spiegel, S.5
  • 97
    • 78649636176 scopus 로고    scopus 로고
    • Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria
    • Wirawan E, VandeWalle L, Kersse K, Cornelis S, Claerhout S, Vanoverberghe I et al. Caspase-mediated cleavage of Beclin-1 inactivates Beclin-1-induced autophagy and enhances apoptosis by promoting the release of proapoptotic factors from mitochondria. Cell Death Dis 2010;1:e18.
    • (2010) Cell Death Dis , vol.1
    • Wirawan, E.1    Vande Walle, L.2    Kersse, K.3    Cornelis, S.4    Claerhout, S.5    Vanoverberghe, I.6
  • 99
    • 43949096967 scopus 로고    scopus 로고
    • Impaired autophagy: A mechanism of mitochondrial dysfunction in anoxic rat hepatocytes
    • Kim JS, Nitta T, Mohuczy D, O'Malley KA, Moldawer LL, DunnWA Jr. et al. Impaired autophagy: A mechanism of mitochondrial dysfunction in anoxic rat hepatocytes. Hepatology 2008;47:1725-1736.
    • (2008) Hepatology , vol.47 , pp. 1725-1736
    • Kim, J.S.1    Nitta, T.2    Mohuczy, D.3    O'Malley, K.A.4    Moldawer, L.L.5    Dunn Jr., W.A.6
  • 100
    • 79960029137 scopus 로고    scopus 로고
    • Calpainmediated cleavage of Beclin-1 and autophagy deregulation following retinal ischemic injury in vivo
    • Russo R, Berliocchi L, Adornetto A, Varano GP, Cavaliere F, Nucci C et al. Calpainmediated cleavage of Beclin-1 and autophagy deregulation following retinal ischemic injury in vivo. Cell Death Dis 2011;2:e144.
    • (2011) Cell Death Dis , vol.2
    • Russo, R.1    Berliocchi, L.2    Adornetto, A.3    Varano, G.P.4    Cavaliere, F.5    Nucci, C.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.