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Volumn 1793, Issue 12, 2009, Pages 1886-1893

Calcium-dependent plasma membrane repair requires m- or μ-calpain, but not calpain-3, the proteasome, or caspases

Author keywords

Calpain; Caspase; Membrane repair; Proteasome

Indexed keywords

CALCIUM ION; CALPAIN 1; CALPAIN 2; CALPAIN 3; CASPASE; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E1; UNCLASSIFIED DRUG;

EID: 71749109832     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2009.09.013     Document Type: Article
Times cited : (59)

References (43)
  • 1
    • 0344824647 scopus 로고    scopus 로고
    • Plasma membrane disruption: repair, prevention, adaptation
    • McNeil P.L., and Steinhardt R.A. Plasma membrane disruption: repair, prevention, adaptation. Annu. Rev. Cell Dev. Biol. 19 (2003) 697-731
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 697-731
    • McNeil, P.L.1    Steinhardt, R.A.2
  • 2
    • 20344402550 scopus 로고    scopus 로고
    • An emergency response team for membrane repair
    • McNeil P.L., and Kirchhausen T. An emergency response team for membrane repair. Nat. Rev. Mol. Cell Biol. 6 (2005) 499-505
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 499-505
    • McNeil, P.L.1    Kirchhausen, T.2
  • 3
    • 34447118089 scopus 로고    scopus 로고
    • Dysferlin-mediated membrane repair protects the heart from stress-induced left ventricular injury
    • Han R., Bansal D., Miyake K., Muniz V.P., Weiss R.M., McNeil P.L., and Campbell K.P. Dysferlin-mediated membrane repair protects the heart from stress-induced left ventricular injury. J. Clin. Invest 117 (2007) 1805-1813
    • (2007) J. Clin. Invest , vol.117 , pp. 1805-1813
    • Han, R.1    Bansal, D.2    Miyake, K.3    Muniz, V.P.4    Weiss, R.M.5    McNeil, P.L.6    Campbell, K.P.7
  • 4
    • 0026729383 scopus 로고
    • Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage
    • McNeil P.L., and Khakee R. Disruptions of muscle fiber plasma membranes. Role in exercise-induced damage. Am. J. Pathol. 140 (1992) 1097-1109
    • (1992) Am. J. Pathol. , vol.140 , pp. 1097-1109
    • McNeil, P.L.1    Khakee, R.2
  • 5
    • 0030723311 scopus 로고    scopus 로고
    • Cardiac myocyte membrane wounding in the abruptly pressure-overloaded rat heart under high wall stress
    • Fischer T.A., McNeil P.L., Khakee R., Finn P., Kelly R.A., Pfeffer M.A., and Pfeffer J.M. Cardiac myocyte membrane wounding in the abruptly pressure-overloaded rat heart under high wall stress. Hypertension 30 (1997) 1041-1046
    • (1997) Hypertension , vol.30 , pp. 1041-1046
    • Fischer, T.A.1    McNeil, P.L.2    Khakee, R.3    Finn, P.4    Kelly, R.A.5    Pfeffer, M.A.6    Pfeffer, J.M.7
  • 6
    • 0029609143 scopus 로고
    • Calcium-regulated exocytosis is required for cell membrane resealing
    • Bi G.Q., Alderton J.M., and Steinhardt R.A. Calcium-regulated exocytosis is required for cell membrane resealing. J. Cell Biol. 131 (1995) 1747-1758
    • (1995) J. Cell Biol. , vol.131 , pp. 1747-1758
    • Bi, G.Q.1    Alderton, J.M.2    Steinhardt, R.A.3
  • 9
    • 33845951914 scopus 로고    scopus 로고
    • Requirement for annexin A1 in plasma membrane repair
    • McNeil A.K., Rescher U., Gerke V., and McNeil P.L. Requirement for annexin A1 in plasma membrane repair. J. Biol. Chem. 281 (2006) 35202-35207
    • (2006) J. Biol. Chem. , vol.281 , pp. 35202-35207
    • McNeil, A.K.1    Rescher, U.2    Gerke, V.3    McNeil, P.L.4
  • 10
    • 34047273570 scopus 로고    scopus 로고
    • Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane
    • Mellgren R.L., Zhang W., Miyake K., and McNeil P.L. Calpain is required for the rapid, calcium-dependent repair of wounded plasma membrane. J. Biol. Chem. 282 (2007) 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
  • 11
    • 37249053219 scopus 로고    scopus 로고
    • Fetuin A stabilizes m-calpain and facilitates plasma membrane repair
    • Mellgren R.L., and Huang X. Fetuin A stabilizes m-calpain and facilitates plasma membrane repair. J. Biol. Chem. 282 (2007) 35868-35877
    • (2007) J. Biol. Chem. , vol.282 , pp. 35868-35877
    • Mellgren, R.L.1    Huang, X.2
  • 14
  • 15
    • 0029048989 scopus 로고
    • Casein zymography: a method to study mu-calpain, m-calpain, and their inhibitory agents
    • Raser K.J., Posner A., and Wang K.K. Casein zymography: a method to study mu-calpain, m-calpain, and their inhibitory agents. Arch. Biochem. Biophys. 319 (1995) 211-216
    • (1995) Arch. Biochem. Biophys. , vol.319 , pp. 211-216
    • Raser, K.J.1    Posner, A.2    Wang, K.K.3
  • 17
    • 0025800039 scopus 로고
    • Proteolysis of nuclear proteins by mu-calpain and m-calpain
    • Mellgren R.L. Proteolysis of nuclear proteins by mu-calpain and m-calpain. J. Biol. Chem. 266 (1991) 13920-13924
    • (1991) J. Biol. Chem. , vol.266 , pp. 13920-13924
    • Mellgren, R.L.1
  • 18
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays
    • Mosmann T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays. J. Immunol. Meth. 65 (1983) 55-63
    • (1983) J. Immunol. Meth. , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 20
    • 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 J.G., and Spencer M.J. Null mutation of calpain 3 (p94) in mice causes abnormal sarcomere formation in vivo and in vitro. Hum. Mol. Genet. 13 (2004) 1373-1388
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 1373-1388
    • Kramerova, I.1    Kudryashova, E.2    Tidball, J.G.3    Spencer, M.J.4
  • 21
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin N., Bhatt A.K., Dutt P., Greer P.A., Arthur J.S., Elce J.S., and Huttenlocher A. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J. Biol. Chem. 276 (2001) 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    Huttenlocher, A.7
  • 22
    • 4043077024 scopus 로고    scopus 로고
    • Isoform specific function of calpain 2 in regulating membrane protrusion
    • Franco S., Perrin B., and Huttenlocher A. Isoform specific function of calpain 2 in regulating membrane protrusion. Exp. Cell Res. 299 (2004) 179-187
    • (2004) Exp. Cell Res. , vol.299 , pp. 179-187
    • Franco, S.1    Perrin, B.2    Huttenlocher, A.3
  • 23
    • 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., Kinbara K., Kimura S., Takahashi M., Ishiura S., Sasagawa N., Sorimachi N., Shimada H., Tagawa K., Maruyama K., 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. 270 (1995) 31158-31162
    • (1995) J. Biol. Chem. , vol.270 , pp. 31158-31162
    • Sorimachi, H.1    Kinbara, K.2    Kimura, S.3    Takahashi, M.4    Ishiura, S.5    Sasagawa, N.6    Sorimachi, N.7    Shimada, H.8    Tagawa, K.9    Maruyama, K.10
  • 25
    • 34250838745 scopus 로고    scopus 로고
    • Dysferlin in membrane trafficking and patch repair
    • Glover L., and Brown Jr. R.H. Dysferlin in membrane trafficking and patch repair. Traffic 8 (2007) 785-794
    • (2007) Traffic , vol.8 , pp. 785-794
    • Glover, L.1    Brown Jr., R.H.2
  • 26
    • 65549087562 scopus 로고    scopus 로고
    • Endogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent of stretch
    • Murphy R.M., and Lamb G.D. Endogenous calpain-3 activation is primarily governed by small increases in resting cytoplasmic [Ca2+] and is not dependent of stretch. J. Biol. Chem. 284 (2009) 7811-7819
    • (2009) J. Biol. Chem. , vol.284 , pp. 7811-7819
    • Murphy, R.M.1    Lamb, G.D.2
  • 27
    • 0344629442 scopus 로고    scopus 로고
    • Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components
    • Taveau M., Bourg N., Sillon G., Roudaut C., Bartoli M., and Richard I. Calpain 3 is activated through autolysis within the active site and lyses sarcomeric and sarcolemmal components. Mol. Cell Biol. 23 (2003) 9127-9135
    • (2003) Mol. Cell Biol. , vol.23 , pp. 9127-9135
    • Taveau, M.1    Bourg, N.2    Sillon, G.3    Roudaut, C.4    Bartoli, M.5    Richard, I.6
  • 29
    • 33751012118 scopus 로고    scopus 로고
    • Regulation of the M-cadherin-beta-catenin complex by calpain 3 during terminal stages of myogenic differentiation
    • Kramerova I., Kudryashova E., Wu B., and Spencer M.J. Regulation of the M-cadherin-beta-catenin complex by calpain 3 during terminal stages of myogenic differentiation. Mol. Cell Biol. 26 (2006) 8437-8447
    • (2006) Mol. Cell Biol. , vol.26 , pp. 8437-8447
    • Kramerova, I.1    Kudryashova, E.2    Wu, B.3    Spencer, M.J.4
  • 30
    • 12944283204 scopus 로고    scopus 로고
    • Increased proteasome degradation of cyclin-dependent kinase inhibitor p27 is associated with a decreased overall survival in mantle cell lymphoma
    • Chiarle R., Budel L.M., Skolnik J., Frizzera G., Chilosi M., Corato A., Pizzolo G., Magidson J., Montagnoli A., Pagano M., et al. Increased proteasome degradation of cyclin-dependent kinase inhibitor p27 is associated with a decreased overall survival in mantle cell lymphoma. Blood 95 (2000) 619-626
    • (2000) Blood , vol.95 , pp. 619-626
    • Chiarle, R.1    Budel, L.M.2    Skolnik, J.3    Frizzera, G.4    Chilosi, M.5    Corato, A.6    Pizzolo, G.7    Magidson, J.8    Montagnoli, A.9    Pagano, M.10
  • 31
    • 30344460668 scopus 로고    scopus 로고
    • Recognition and delivery of ERAD substrates to the proteasome and alternative paths for cell survival
    • McCracken A.A., and Brodsky J.L. Recognition and delivery of ERAD substrates to the proteasome and alternative paths for cell survival. Curr. Top Microbiol. Immunol. 300 (2005) 17-40
    • (2005) Curr. Top Microbiol. Immunol. , vol.300 , pp. 17-40
    • McCracken, A.A.1    Brodsky, J.L.2
  • 32
    • 34948845308 scopus 로고    scopus 로고
    • Proteasome activator enhances survival of Huntington's disease neuronal model cells
    • Seo H., Sonntag K.C., Kim W., Cattaneo E., and Isacson O. Proteasome activator enhances survival of Huntington's disease neuronal model cells. PLoS ONE 2 (2007) e238
    • (2007) PLoS ONE , vol.2
    • Seo, H.1    Sonntag, K.C.2    Kim, W.3    Cattaneo, E.4    Isacson, O.5
  • 33
    • 39749084641 scopus 로고    scopus 로고
    • Active caspase-1 is a regulator of unconventional protein secretion
    • Keller M., Ruegg A., Werner S., and Beer H.D. Active caspase-1 is a regulator of unconventional protein secretion. Cell 132 (2008) 818-831
    • (2008) Cell , vol.132 , pp. 818-831
    • Keller, M.1    Ruegg, A.2    Werner, S.3    Beer, H.D.4
  • 34
    • 33748598700 scopus 로고    scopus 로고
    • Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival
    • Gurcel L., Abrami L., Girardin S., Tschopp J., and van der Goot F.G. Caspase-1 activation of lipid metabolic pathways in response to bacterial pore-forming toxins promotes cell survival. Cell 126 (2006) 1135-1145
    • (2006) Cell , vol.126 , pp. 1135-1145
    • Gurcel, L.1    Abrami, L.2    Girardin, S.3    Tschopp, J.4    van der Goot, F.G.5
  • 35
    • 0028205667 scopus 로고
    • Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway
    • Chowdary D.R., Dermody J.J., Jha K.K., and Ozer H.L. Accumulation of p53 in a mutant cell line defective in the ubiquitin pathway. Mol. Cell Biol. 14 (1994) 1997-2003
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1997-2003
    • Chowdary, D.R.1    Dermody, J.J.2    Jha, K.K.3    Ozer, H.L.4
  • 38
    • 0031044857 scopus 로고    scopus 로고
    • Calpain II expression is increased by changes in mechanical loading of muscle in vivo
    • Spencer M.J., Lu B., and Tidball J.G. Calpain II expression is increased by changes in mechanical loading of muscle in vivo. J. Cell Biochem. 64 (1997) 55-66
    • (1997) J. Cell Biochem. , vol.64 , pp. 55-66
    • Spencer, M.J.1    Lu, B.2    Tidball, J.G.3
  • 39
  • 40
    • 34347221228 scopus 로고    scopus 로고
    • Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain
    • Ojima K., Ono Y., Doi N., Yoshioka K., Kawabata Y., Labeit S., and Sorimachi H. Myogenic stage, sarcomere length, and protease activity modulate localization of muscle-specific calpain. J. Biol. Chem. 282 (2007) 14493-14504
    • (2007) J. Biol. Chem. , vol.282 , pp. 14493-14504
    • Ojima, K.1    Ono, Y.2    Doi, N.3    Yoshioka, K.4    Kawabata, Y.5    Labeit, S.6    Sorimachi, H.7
  • 41
    • 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 R.M., Goodman C.A., McKenna M.J., Bennie J., Leikis M., and Lamb G.D. Calpain-3 is autolyzed and hence activated in human skeletal muscle 24 h following a single bout of eccentric exercise. J. Appl. Physiol. 103 (2007) 926-931
    • (2007) J. Appl. Physiol. , vol.103 , 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
  • 43
    • 0037101928 scopus 로고    scopus 로고
    • Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle
    • Feasson L., Stockholm D., Freyssenet D., Richard I., Duguez S., Beckmann J.S., and Denis C. Molecular adaptations of neuromuscular disease-associated proteins in response to eccentric exercise in human skeletal muscle. J. Physiol. 543 (2002) 297-306
    • (2002) J. Physiol. , vol.543 , pp. 297-306
    • Feasson, L.1    Stockholm, D.2    Freyssenet, D.3    Richard, I.4    Duguez, S.5    Beckmann, J.S.6    Denis, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.