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Volumn 38, Issue 12, 2006, Pages 2128-2140

Detection and localization of calpain 3-like protease in a neuronal cell line: Possible regulation of apoptotic cell death through degradation of nuclear IκBα

Author keywords

Apoptosis; Calpain 3 like protease; I B ; NF B; Nucleus; PC12

Indexed keywords

CALPAIN 3; CALPAIN 3 LIKE PROTEASE; ENZYME; I KAPPA B ALPHA; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 33748692883     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biocel.2006.06.005     Document Type: Article
Times cited : (16)

References (45)
  • 1
    • 0028967819 scopus 로고
    • Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B
    • Arenzana-Seisdedos F., Thompson J., Rodriguez M.S., Bachelerie F., Thomas D., and Hay R.T. Inducible nuclear expression of newly synthesized I kappa B alpha negatively regulates DNA-binding and transcriptional activities of NF-kappa B. Mol. Cell Biol. 15 (1995) 2689-2696
    • (1995) Mol. Cell Biol. , vol.15 , pp. 2689-2696
    • Arenzana-Seisdedos, F.1    Thompson, J.2    Rodriguez, M.S.3    Bachelerie, F.4    Thomas, D.5    Hay, R.T.6
  • 2
    • 0031057644 scopus 로고    scopus 로고
    • Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm
    • Arenzana-Seisdedos F., Turpin P., Rodriguez M., Thomas D., Hay R.T., Virelizier J.L., et al. Nuclear localization of I kappa B alpha promotes active transport of NF-kappa B from the nucleus to the cytoplasm. J. Cell Sci. 110 (1997) 369-378
    • (1997) J. Cell Sci. , vol.110 , pp. 369-378
    • Arenzana-Seisdedos, F.1    Turpin, P.2    Rodriguez, M.3    Thomas, D.4    Hay, R.T.5    Virelizier, J.L.6
  • 3
    • 0023724778 scopus 로고
    • I kappa B: a specific inhibitor of the NF-kappa transcription factor
    • Baeuerle P.A., and Baltimore D. I kappa B: a specific inhibitor of the NF-kappa transcription factor. Science 242 (1988) 540-546
    • (1988) Science , vol.242 , pp. 540-546
    • Baeuerle, P.A.1    Baltimore, D.2
  • 4
    • 0030271387 scopus 로고    scopus 로고
    • NF-kappa B: ten years after
    • Baeuerle P.A., and Baltimore D. NF-kappa B: ten years after. Cell 87 (1996) 13-20
    • (1996) Cell , vol.87 , pp. 13-20
    • Baeuerle, P.A.1    Baltimore, D.2
  • 5
    • 0032941594 scopus 로고    scopus 로고
    • Calpain [3] deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A
    • Baghdiguian S., Martin M., Richard I., Pons F., Astier C., Bourg N., et al. Calpain [3] deficiency is associated with myonuclear apoptosis and profound perturbation of the IkappaB alpha/NF-kappaB pathway in limb-girdle muscular dystrophy type 2A. Nat. Med. 5 (1999) 503-511
    • (1999) Nat. Med. , vol.5 , pp. 503-511
    • Baghdiguian, S.1    Martin, M.2    Richard, I.3    Pons, F.4    Astier, C.5    Bourg, N.6
  • 6
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: roles in synaptic plasticity and cell death
    • Chan S.L., and Mattson M.P. Caspase and calpain substrates: roles in synaptic plasticity and cell death. J. Neurosci. Res. 58 (1999) 167-190
    • (1999) J. Neurosci. Res. , vol.58 , pp. 167-190
    • Chan, S.L.1    Mattson, M.P.2
  • 8
    • 0031570757 scopus 로고    scopus 로고
    • Calpain contributes to silica-induced I kappa B-alpha degradation and nuclear factor-kappa B activation
    • Chen F., Lu Y., Kuhn D.C., Maki M., Shi X., Sun S.C., et al. Calpain contributes to silica-induced I kappa B-alpha degradation and nuclear factor-kappa B activation. Arch. Biochem. Biophys. 342 (1997) 383-388
    • (1997) Arch. Biochem. Biophys. , vol.342 , pp. 383-388
    • Chen, F.1    Lu, Y.2    Kuhn, D.C.3    Maki, M.4    Shi, X.5    Sun, S.C.6
  • 10
    • 1842737533 scopus 로고    scopus 로고
    • Spatiotemporal evidence of apoptosis-mediated ischemic injury in organotypic hippocampal slice cultures
    • Cho S., Liu D., Fairman D., Li P., Jenkins L., McGonigle P., et al. Spatiotemporal evidence of apoptosis-mediated ischemic injury in organotypic hippocampal slice cultures. Neurochem. Int. 45 (2004) 117-127
    • (2004) Neurochem. Int. , vol.45 , pp. 117-127
    • Cho, S.1    Liu, D.2    Fairman, D.3    Li, P.4    Jenkins, L.5    McGonigle, P.6
  • 12
    • 3042597817 scopus 로고    scopus 로고
    • Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide
    • Diaz B.G., Moldoveanu T., Kuiper M.J., Campbell R.L., and Davies P.L. Insertion sequence 1 of muscle-specific calpain, p94, acts as an internal propeptide. J. Biol. Chem. 279 (2004) 27656-27666
    • (2004) J. Biol. Chem. , vol.279 , pp. 27656-27666
    • Diaz, B.G.1    Moldoveanu, T.2    Kuiper, M.J.3    Campbell, R.L.4    Davies, P.L.5
  • 13
    • 2442631459 scopus 로고    scopus 로고
    • Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus
    • Gafni J., Hermel E., Young J.E., Wellington C.L., Hayden M.R., and Ellerby L.M. Inhibition of calpain cleavage of huntingtin reduces toxicity: accumulation of calpain/caspase fragments in the nucleus. J. Biol. Chem. 279 (2004) 20211-20220
    • (2004) J. Biol. Chem. , vol.279 , pp. 20211-20220
    • Gafni, J.1    Hermel, E.2    Young, J.E.3    Wellington, C.L.4    Hayden, M.R.5    Ellerby, L.M.6
  • 14
    • 0036168356 scopus 로고    scopus 로고
    • Cutting to the chase: calpain proteases in cell motility
    • Glading A., Lauffenburger D.A., and Wells A. Cutting to the chase: calpain proteases in cell motility. Trends Cell Biol. 12 (2002) 46-54
    • (2002) Trends Cell Biol. , vol.12 , pp. 46-54
    • Glading, A.1    Lauffenburger, D.A.2    Wells, A.3
  • 15
    • 0032903191 scopus 로고    scopus 로고
    • Calcium ionophores can induce either apoptosis or necrosis in cultured cortical neurons
    • Gwag B.J., Canzoniero L.M., Sensi S.L., Demaro J.A., Koh J.Y., Goldberg M.P., et al. Calcium ionophores can induce either apoptosis or necrosis in cultured cortical neurons. Neuroscience 90 (1999) 1339-1348
    • (1999) Neuroscience , vol.90 , pp. 1339-1348
    • Gwag, B.J.1    Canzoniero, L.M.2    Sensi, S.L.3    Demaro, J.A.4    Koh, J.Y.5    Goldberg, M.P.6
  • 16
    • 0023196746 scopus 로고
    • Regulatory domains of erythrocyte ankyrin
    • Hall T.G., and Bennett V. Regulatory domains of erythrocyte ankyrin. J. Biol. Chem. 262 (1987) 10537-10545
    • (1987) J. Biol. Chem. , vol.262 , pp. 10537-10545
    • Hall, T.G.1    Bennett, V.2
  • 17
    • 0033534475 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain: A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation
    • Han Y., Weinman S., Boldogh I., Walker R.K., and Brasier A.R. Tumor necrosis factor-alpha-inducible IkappaBalpha proteolysis mediated by cytosolic m-calpain: A mechanism parallel to the ubiquitin-proteasome pathway for nuclear factor-kappab activation. J. Biol. Chem. 274 (1999) 787-794
    • (1999) J. Biol. Chem. , vol.274 , pp. 787-794
    • Han, Y.1    Weinman, S.2    Boldogh, I.3    Walker, R.K.4    Brasier, A.R.5
  • 18
    • 0033050067 scopus 로고    scopus 로고
    • Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events
    • Herasse M., Ono Y., Fougerousse F., Kimura E., Stockholm D., Beley C., et al. Expression and functional characteristics of calpain 3 isoforms generated through tissue-specific transcriptional and posttranscriptional events. Mol. Cell Biol. 19 (1999) 4047-4055
    • (1999) Mol. Cell Biol. , vol.19 , pp. 4047-4055
    • Herasse, M.1    Ono, Y.2    Fougerousse, F.3    Kimura, E.4    Stockholm, D.5    Beley, C.6
  • 19
    • 0030893610 scopus 로고    scopus 로고
    • Role of calpain- and interleukin-1 beta converting enzyme-like proteases in the beta-amyloid-induced death of rat hippocampal neurons in culture
    • Jordan J., Galindo M.F., and Miller R.J. Role of calpain- and interleukin-1 beta converting enzyme-like proteases in the beta-amyloid-induced death of rat hippocampal neurons in culture. J. Neurochem. 68 (1997) 1612-1621
    • (1997) J. Neurochem. , vol.68 , pp. 1612-1621
    • Jordan, J.1    Galindo, M.F.2    Miller, R.J.3
  • 20
    • 0034757949 scopus 로고    scopus 로고
    • Sequential degradation of proteins from the nuclear envelope during apoptosis
    • Kihlmark M., Imreh G., and Hallberg E. Sequential degradation of proteins from the nuclear envelope during apoptosis. J. Cell Sci. 114 (2001) 3643-3653
    • (2001) J. Cell Sci. , vol.114 , pp. 3643-3653
    • Kihlmark, M.1    Imreh, G.2    Hallberg, E.3
  • 21
    • 18144445733 scopus 로고    scopus 로고
    • Purification of native p94, a muscle-specific calpain, and characterization of its autolysis
    • Kinbara K., Ishiura S., Tomioka S., Sorimachi H., Jeong S.Y., Amano S., et al. Purification of native p94, a muscle-specific calpain, and characterization of its autolysis. Biochem. J. 335 (1998) 589-596
    • (1998) Biochem. J. , vol.335 , pp. 589-596
    • Kinbara, K.1    Ishiura, S.2    Tomioka, S.3    Sorimachi, H.4    Jeong, S.Y.5    Amano, S.6
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • Mattson M.P. Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1 (2000) 120-129
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 25
    • 0033979815 scopus 로고    scopus 로고
    • Roles of nuclear factor kappaB in neuronal survival and plasticity
    • Mattson M.P., Culmsee C., Yu Z., and Camandola S. Roles of nuclear factor kappaB in neuronal survival and plasticity. J. Neurochem. 74 (2000) 443-456
    • (2000) J. Neurochem. , vol.74 , pp. 443-456
    • Mattson, M.P.1    Culmsee, C.2    Yu, Z.3    Camandola, S.4
  • 26
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Nath R., Raser K.J., Stafford D., Hajimohammadreza I., Posner A., Allen H., et al. Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1 beta-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis. Biochem. J. 319 (1996) 683-690
    • (1996) Biochem. J. , vol.319 , pp. 683-690
    • Nath, R.1    Raser, K.J.2    Stafford, D.3    Hajimohammadreza, I.4    Posner, A.5    Allen, H.6
  • 27
    • 0141762744 scopus 로고    scopus 로고
    • The calpains in aging and aging-related diseases
    • Nixon R.A. The calpains in aging and aging-related diseases. Ageing Res. Rev. 2 (2003) 407-418
    • (2003) Ageing Res. Rev. , vol.2 , pp. 407-418
    • Nixon, R.A.1
  • 28
    • 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 T.C., Beckmann J.S., et al. Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J. Biol. Chem. 273 (1998) 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
  • 31
    • 0037375291 scopus 로고    scopus 로고
    • Protein expression patterns for ubiquitous and tissue specific calpains in the developing mouse lens
    • Reed N.A., Castellini M.A., Ma H., Shearer T.R., and Duncan M.K. Protein expression patterns for ubiquitous and tissue specific calpains in the developing mouse lens. Exp. Eye Res. 76 (2003) 433-443
    • (2003) Exp. Eye Res. , vol.76 , pp. 433-443
    • Reed, N.A.1    Castellini, M.A.2    Ma, H.3    Shearer, T.R.4    Duncan, M.K.5
  • 33
    • 0037132543 scopus 로고    scopus 로고
    • 2+-dependent intramolecular autolysis
    • 2+-dependent intramolecular autolysis. FEBS Lett. 532 (2002) 401-406
    • (2002) FEBS Lett. , vol.532 , pp. 401-406
    • Rey, M.A.1    Davies, P.L.2
  • 34
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types, Specific expression of the mRNA in skeletal muscle
    • Sorimachi H., Imajoh-Ohmi S., Emori Y., Kawasaki H., Ohno S., Minami Y., et al. Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and mu-types, Specific expression of the mRNA in skeletal muscle. J. Biol. Chem. 264 (1989) 20106-20111
    • (1989) J. Biol. Chem. , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3    Kawasaki, H.4    Ohno, S.5    Minami, Y.6
  • 35
    • 0028959934 scopus 로고
    • Identification of a third ubiquitous calpain species-chicken muscle expresses four distinct calpains
    • Sorimachi H., Tsukahara T., Okada-Ban M., Sugita H., Ishiura S., and Suzuki K. Identification of a third ubiquitous calpain species-chicken muscle expresses four distinct calpains. Biochim. Biophys. Acta 1261 (1995) 381-393
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 381-393
    • Sorimachi, H.1    Tsukahara, T.2    Okada-Ban, M.3    Sugita, H.4    Ishiura, S.5    Suzuki, K.6
  • 37
    • 3442884545 scopus 로고    scopus 로고
    • The effects of calpain inhibition on IkB-alpha degradation after activation of PBMCs: Identification of the calpain cleavage sites
    • Schaecher K., Goust J.M., and Banik N.L. The effects of calpain inhibition on IkB-alpha degradation after activation of PBMCs: Identification of the calpain cleavage sites. Neurochem. Res. 29 (2004) 1443-1451
    • (2004) Neurochem. Res. , vol.29 , pp. 1443-1451
    • Schaecher, K.1    Goust, J.M.2    Banik, N.L.3
  • 39
    • 0033595636 scopus 로고    scopus 로고
    • The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain
    • Shumway S.D., Maki M., and Miyamoto S. The PEST domain of IkappaBalpha is necessary and sufficient for in vitro degradation by mu-calpain. J. Biol. Chem. 274 (1999) 30874-30881
    • (1999) J. Biol. Chem. , vol.274 , pp. 30874-30881
    • Shumway, S.D.1    Maki, M.2    Miyamoto, S.3
  • 40
    • 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
  • 41
    • 0037469097 scopus 로고    scopus 로고
    • Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax
    • Toyota H., Yanase N., Yoshimoto T., Moriyama M., Sudo T., and Mizuguchi J. Calpain-induced Bax-cleavage product is a more potent inducer of apoptotic cell death than wild-type Bax. Cancer Lett. 189 (2003) 221-230
    • (2003) Cancer Lett. , vol.189 , pp. 221-230
    • Toyota, H.1    Yanase, N.2    Yoshimoto, T.3    Moriyama, M.4    Sudo, T.5    Mizuguchi, J.6
  • 42
    • 10544238107 scopus 로고    scopus 로고
    • Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis
    • Vanags D.M., Porn-Ares M.I., Coppola S., Burgess D.H., and Orrenius S. Protease involvement in fodrin cleavage and phosphatidylserine exposure in apoptosis. J. Biol. Chem. 271 (1996) 31075-31085
    • (1996) J. Biol. Chem. , vol.271 , pp. 31075-31085
    • Vanags, D.M.1    Porn-Ares, M.I.2    Coppola, S.3    Burgess, D.H.4    Orrenius, S.5
  • 43
    • 0034641936 scopus 로고    scopus 로고
    • Apoptosis in the nervous system
    • Yuan J., and Yankner B.A. Apoptosis in the nervous system. Nature 407 (2000) 802-809
    • (2000) Nature , vol.407 , pp. 802-809
    • Yuan, J.1    Yankner, B.A.2
  • 44
    • 0025304791 scopus 로고
    • Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA
    • Zabel U., and Baeuerle P.A. Purified human I kappa B can rapidly dissociate the complex of the NF-kappa B transcription factor with its cognate DNA. Cell 61 (1990) 255-265
    • (1990) Cell , vol.61 , pp. 255-265
    • Zabel, U.1    Baeuerle, P.A.2
  • 45
    • 0031714410 scopus 로고    scopus 로고
    • Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells
    • Zhang J., Patel J.M., and Block E.R. Hypoxia-specific upregulation of calpain activity and gene expression in pulmonary artery endothelial cells. Am. J. Physiol. 275 (1998) 461-465
    • (1998) Am. J. Physiol. , vol.275 , pp. 461-465
    • Zhang, J.1    Patel, J.M.2    Block, E.R.3


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