메뉴 건너뛰기




Volumn 93, Issue 5, 2005, Pages 1280-1292

The critical role of calpain versus caspase activation in excitotoxic injury induced by nitric oxide

Author keywords

Apoptosis; Calpains; Caspases; Excitotoxicity; Mitochondria; Nitric oxide

Indexed keywords

3 (4 IODOPHENYL) 2 MERCAPTO 2 PROPENIC ACID; ADENOVIRUS VECTOR; APOPTOSIS INDUCING FACTOR; CALCIUM; CALPAIN; CALPASTATIN; CASPASE; CASPASE 3; CASPASE 9; CASPASE INHIBITOR; COLCHICINE; CYSTEINE PROTEINASE; CYTOCHROME C; DIZOCILPINE; GLUTAMIC ACID; HOE 33342; N ACETYL S NITROSOPENICILLAMINE; NITRIC OXIDE; PD 150606; PROCASPASE 9; PROPENIC ACID; S NITROSOGLUTATHIONE; UNCLASSIFIED DRUG;

EID: 20144368362     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1471-4159.2005.03122.x     Document Type: Article
Times cited : (51)

References (57)
  • 1
    • 0034086332 scopus 로고    scopus 로고
    • Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines
    • Atencio I. A., Ramachandra M., Shabram P. and Demers G. W. (2000) Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines. Cell Growth Differ 11, 247-253.
    • (2000) Cell Growth Differ. , vol.11 , pp. 247-253
    • Atencio, I.A.1    Ramachandra, M.2    Shabram, P.3    Demers, G.W.4
  • 3
    • 0029045611 scopus 로고
    • Induction of calpain-mediated spectrin fragments by pathogenic treatments in long-term hippocampal slices
    • Bahr B. A., Tiriveedhi S., Park G. Y. and Lynch G. (1995) Induction of calpain-mediated spectrin fragments by pathogenic treatments in long-term hippocampal slices. J. Pharmacol. Exp Ther 273, 902-908.
    • (1995) J. Pharmacol. Exp. Ther. , vol.273 , pp. 902-908
    • Bahr, B.A.1    Tiriveedhi, S.2    Park, G.Y.3    Lynch, G.4
  • 4
    • 0242384898 scopus 로고    scopus 로고
    • In vivo calpain/caspase cross-talk during 3-nitropropionic acid-induced striatal degeneration: Implication of a calpain-mediated cleavage of active caspase-3
    • Bizat N., Hermel J. M., Humbert S., Jacquard C., Creminon C., Escartin C., Saudou F., Krajewski S., Hantraye P. and Brouillet E. (2003) In vivo calpain/caspase cross-talk during 3-nitropropionic acid-induced striatal degeneration: implication of a calpain-mediated cleavage of active caspase-3. J. Biol. Chem. 278, 43 245-43 253.
    • (2003) J. Biol. Chem. , vol.278
    • Bizat, N.1    Hermel, J.M.2    Humbert, S.3    Jacquard, C.4    Creminon, C.5    Escartin, C.6    Saudou, F.7    Krajewski, S.8    Hantraye, P.9    Brouillet, E.10
  • 5
    • 0035971091 scopus 로고    scopus 로고
    • Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: A mechanism of 'pathological apoptosis'?
    • Blomgren K., Zhu C., Wang X., Karlsson J. O., Leverin A. L., Bahr B. A., Mallard C. and Hagberg H. (2001) Synergistic activation of caspase-3 by m-calpain after neonatal hypoxia-ischemia: a mechanism of 'pathological apoptosis'? J. Biol. Chem. 276, 10 191-10 198.
    • (2001) J. Biol. Chem. , vol.276
    • Blomgren, K.1    Zhu, C.2    Wang, X.3    Karlsson, J.O.4    Leverin, A.L.5    Bahr, B.A.6    Mallard, C.7    Hagberg, H.8
  • 6
    • 0035903235 scopus 로고    scopus 로고
    • Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion
    • Chen M., He H., Zhan S., Krajewski S., Reed J. C. and Gottlieb R. A. (2001) Bid is cleaved by calpain to an active fragment in vitro and during myocardial ischemia/reperfusion. J. Biol. Chem. 276, 30 724-30 728.
    • (2001) J. Biol. Chem. , vol.276
    • Chen, M.1    He, H.2    Zhan, S.3    Krajewski, S.4    Reed, J.C.5    Gottlieb, R.A.6
  • 7
    • 0037047326 scopus 로고    scopus 로고
    • Calpain and mitochondria in ischemia/reperfusion injury
    • Chen M., Won D. J., Krajewski S. and Gottlieb R. A. (2002) Calpain and mitochondria in ischemia/reperfusion injury. J. Biol. Chem. 277, 29 181-29 186.
    • (2002) J. Biol. Chem. , vol.277
    • Chen, M.1    Won, D.J.2    Krajewski, S.3    Gottlieb, R.A.4
  • 8
    • 0034967241 scopus 로고    scopus 로고
    • Cleavage of Bax is mediated by caspase-dependent or-independent calpain activation in dopaminergic neuronal cells: Protective role of Bcl-2
    • Choi W. S., Lee E. H., Chung C. W., Jung Y. K., Jin B. K., Kim S. U., Oh T. H., Saido T. C. and Oh Y. J. (2001) Cleavage of Bax is mediated by caspase-dependent or-independent calpain activation in dopaminergic neuronal cells: protective role of Bcl-2. J. Neurochem. 77, 1531-1541.
    • (2001) J. Neurochem. , vol.77 , pp. 1531-1541
    • Choi, W.S.1    Lee, E.H.2    Chung, C.W.3    Jung, Y.K.4    Jin, B.K.5    Kim, S.U.6    Oh, T.H.7    Saido, T.C.8    Oh, Y.J.9
  • 9
    • 0025265926 scopus 로고
    • The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death
    • Choi D. W. and Rothman S. M. (1990) The role of glutamate neurotoxicity in hypoxic-ischemic neuronal death. Annu. Rev. Neurosci. 13, 171-182.
    • (1990) Annu. Rev. Neurosci. , vol.13 , pp. 171-182
    • Choi, D.W.1    Rothman, S.M.2
  • 10
    • 0001110114 scopus 로고    scopus 로고
    • Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases
    • Chua B. T., Guo K. and Li P. (2000) Direct cleavage by the calcium-activated protease calpain can lead to inactivation of caspases. J. Biol. Chem. 275, 5131-5135.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5131-5135
    • Chua, B.T.1    Guo, K.2    Li, P.3
  • 11
    • 0032560572 scopus 로고    scopus 로고
    • Persistent inhibition of cell respiration by nitric oxide: Crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione
    • Clementi E., Brown G. C., Feelisch M. and Moncada S. (1998) Persistent inhibition of cell respiration by nitric oxide: crucial role of S-nitrosylation of mitochondrial complex I and protective action of glutathione. Proc. Natl Acad. Sci. USA 95, 7631-7636.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 7631-7636
    • Clementi, E.1    Brown, G.C.2    Feelisch, M.3    Moncada, S.4
  • 12
    • 0027940509 scopus 로고
    • Domain structure of calpain: Mapping the binding site for calpastatin
    • Croall D. E. and McGrody K. S. (1994) Domain structure of calpain: mapping the binding site for calpastatin. Biochemistry 33, 13 223-13 230.
    • (1994) Biochemistry , vol.33
    • Croall, D.E.1    McGrody, K.S.2
  • 13
    • 0023835174 scopus 로고
    • All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli
    • Emori Y., Kawasaki H., Imajoh S., Minami Y. and Suzuki K. (1988) All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. J. Biol. Chem. 263, 2364-2370.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2364-2370
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Minami, Y.4    Suzuki, K.5
  • 14
    • 0031888955 scopus 로고    scopus 로고
    • A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
    • Enari M., Sakahira H., Yokoyama H., Okawa K., Iwamatsu A. and Nagata S. (1998) A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391, 43-50.
    • (1998) Nature , vol.391 , pp. 43-50
    • Enari, M.1    Sakahira, H.2    Yokoyama, H.3    Okawa, K.4    Iwamatsu, A.5    Nagata, S.6
  • 15
    • 0028880026 scopus 로고
    • The role of the calpain-calpastatin system in thyrotropin-releasing hormone-induced selective down-regulation of a protein kinase C isozyme, nPKC epsilon, in rat pituitary GH4C1 cells
    • Eto A., Akita Y., Saido T. C., Suzuki K. and Kawashima S. (1995) The role of the calpain-calpastatin system in thyrotropin-releasing hormone-induced selective down-regulation of a protein kinase C isozyme, nPKC epsilon, in rat pituitary GH4C1 cells. J. Biol. Chem. 270, 25 115-25 120.
    • (1995) J. Biol. Chem. , vol.270
    • Eto, A.1    Akita, Y.2    Saido, T.C.3    Suzuki, K.4    Kawashima, S.5
  • 16
    • 0031038495 scopus 로고    scopus 로고
    • Calpain activation contributes to dendritic remodeling after brief excitotoxic injury in vitro
    • Faddis B. T., Hasbani M. J. and Goldberg M. P. (1997) Calpain activation contributes to dendritic remodeling after brief excitotoxic injury in vitro. J. Neurosci. 17, 951-959.
    • (1997) J. Neurosci. , vol.17 , pp. 951-959
    • Faddis, B.T.1    Hasbani, M.J.2    Goldberg, M.P.3
  • 17
    • 0033758751 scopus 로고    scopus 로고
    • N-terminal cleavage of Bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes Bcl-2-independent cytochrome C release and apoptotic cell death
    • Gao G. and Dou Q. P. (2000) N-terminal cleavage of Bax by calpain generates a potent proapoptotic 18-kDa fragment that promotes Bcl-2-independent cytochrome C release and apoptotic cell death. J. Cell Biochem. 80, 53-72.
    • (2000) J. Cell Biochem. , vol.80 , pp. 53-72
    • Gao, G.1    Dou, Q.P.2
  • 21
    • 0024953850 scopus 로고
    • Neurotoxicity at the N-methyl-D-aspartate receptor in energy-compromised neurons. An hypothesis for cell death in aging and disease
    • Henneberry R. C., Novelli A., Cox J. A. and Lysko P. G. (1989) Neurotoxicity at the N-methyl-D-aspartate receptor in energy-compromised neurons. An hypothesis for cell death in aging and disease. Ann. N Y Acad. Sci. 568, 225-233.
    • (1989) Ann. N Y Acad. Sci. , vol.568 , pp. 225-233
    • Henneberry, R.C.1    Novelli, A.2    Cox, J.A.3    Lysko, P.G.4
  • 22
    • 0032514704 scopus 로고    scopus 로고
    • Role of calpain in skeletal-muscle protein degradation
    • Huang J. and Forsberg N. E. (1998) Role of calpain in skeletal-muscle protein degradation. Proc. Natl Acad. Sci. USA 95, 12 100-12 105.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95
    • Huang, J.1    Forsberg, N.E.2
  • 23
    • 0040298568 scopus 로고    scopus 로고
    • Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis
    • Jänicke R. U., Sprengart M. L., Wati M. R. and Porter A. G. (1998) Caspase-3 is required for DNA fragmentation and morphological changes associated with apoptosis. J. Biol. Chem. 273, 9357-9360.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9357-9360
    • Jänicke, R.U.1    Sprengart, M.L.2    Wati, M.R.3    Porter, A.G.4
  • 24
    • 0034595834 scopus 로고    scopus 로고
    • Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25
    • Kusakawa G., Saito T., Onuki R., Ishiguro K., Kishimoto T. and Hisanaga S. (2000) Calpain-dependent proteolytic cleavage of the p35 cyclin-dependent kinase 5 activator to p25. J. Biol. Chem. 275, 17 166-17 172.
    • (2000) J. Biol. Chem. , vol.275
    • Kusakawa, G.1    Saito, T.2    Onuki, R.3    Ishiguro, K.4    Kishimoto, T.5    Hisanaga, S.6
  • 26
    • 0030860241 scopus 로고    scopus 로고
    • Peroxynitrite and nitric oxide donors induce neuronal apoptosis by eliciting autocrine excitotoxicity
    • Leist M., Fava E., Montecucco C. and Nicotera P. (1997a) Peroxynitrite and nitric oxide donors induce neuronal apoptosis by eliciting autocrine excitotoxicity. Eur J. Neurosci. 9, 1488-1498.
    • (1997) Eur. J. Neurosci. , vol.9 , pp. 1488-1498
    • Leist, M.1    Fava, E.2    Montecucco, C.3    Nicotera, P.4
  • 27
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M. and Jäättelä M. (2001) Four deaths and a funeral: from caspases to alternative mechanisms. Nat Rev. Mol Cell Biol. 2, 589-598.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 589-598
    • Leist, M.1    Jäättelä, M.2
  • 28
    • 0031442999 scopus 로고    scopus 로고
    • Caspase-mediated apoptosis in neuronal excitotoxicity triggered by nitric oxide
    • Leist M., Volbracht C., Kühnle S., Fava E., Ferrando-May E. and Nicotera P. (1997b) Caspase-mediated apoptosis in neuronal excitotoxicity triggered by nitric oxide. Mol Med. 3, 750-764.
    • (1997) Mol. Med. , vol.3 , pp. 750-764
    • Leist, M.1    Volbracht, C.2    Kühnle, S.3    Fava, E.4    Ferrando-May, E.5    Nicotera, P.6
  • 29
    • 0030581151 scopus 로고    scopus 로고
    • Induction of apoptotic program in cell-free extracts: Requirement for dATP and cytochrome c
    • Liu X., Kim C. N., Yang J., Jemmerson R. and Wang X. (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86, 147-157.
    • (1996) Cell , vol.86 , pp. 147-157
    • Liu, X.1    Kim, C.N.2    Yang, J.3    Jemmerson, R.4    Wang, X.5
  • 30
    • 0024844775 scopus 로고
    • Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene
    • Maki M., Bagci H., Hamaguchi K., Ueda M., Murachi T. and Hatanaka M. (1989) Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. J. Biol. Chem. 264, 18 866-18 869.
    • (1989) J. Biol. Chem. , vol.264
    • Maki, M.1    Bagci, H.2    Hamaguchi, K.3    Ueda, M.4    Murachi, T.5    Hatanaka, M.6
  • 31
    • 0023677846 scopus 로고
    • Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli
    • Maki M., Takano E., Osawa T., Ooi T., Murachi T. and Hatanaka M. (1988) Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli. J. Biol. Chem. 263, 10 254-10 261.
    • (1988) J. Biol. Chem. , vol.263
    • Maki, M.1    Takano, E.2    Osawa, T.3    Ooi, T.4    Murachi, T.5    Hatanaka, M.6
  • 32
    • 0036236471 scopus 로고    scopus 로고
    • Calpain-mediated Bid cleavage and calpain-independent Bak modulation: Two separate pathways in cisplatin-induced apoptosis
    • Mandic A., Viktorsson K., Strandberg L., Heiden T., Hansson J., Linder S. and Shoshan M. C. (2002) Calpain-mediated Bid cleavage and calpain-independent Bak modulation: two separate pathways in cisplatin-induced apoptosis. Mol Cell Biol. 22, 3003-3013.
    • (2002) Mol. Cell Biol. , vol.22 , pp. 3003-3013
    • Mandic, A.1    Viktorsson, K.2    Strandberg, L.3    Heiden, T.4    Hansson, J.5    Linder, S.6    Shoshan, M.C.7
  • 34
    • 0028229610 scopus 로고
    • Nitric oxide stimulates Ca (2+)-independent synaptic vesicle release
    • Meffert M. K., Premack B. A. and Schulman H. (1994) Nitric oxide stimulates Ca (2+)-independent synaptic vesicle release. Neuron 12, 1235-1244.
    • (1994) Neuron , vol.12 , pp. 1235-1244
    • Meffert, M.K.1    Premack, B.A.2    Schulman, H.3
  • 35
    • 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., Talanian R. V., Yuen P., Gilbertsen R. B. and Wang K. K. (1996) 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, 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    Talanian, R.V.7    Yuen, P.8    Gilbertsen, R.B.9    Wang, K.K.10
  • 36
    • 0033083559 scopus 로고    scopus 로고
    • Neuronal cell death: A demise with different shapes
    • Nicotera P., Leist M. and Manzo L. (1999) Neuronal cell death: a demise with different shapes. Trends Pharmacol. Sci. 20, 46-51.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 46-51
    • Nicotera, P.1    Leist, M.2    Manzo, L.3
  • 37
    • 0014682523 scopus 로고
    • Brain lesions in an infant rhesus monkey treated with monsodium glutamate
    • Olney J. W. and Sharpe L. G. (1969) Brain lesions in an infant rhesus monkey treated with monsodium glutamate. Science 166, 386-388.
    • (1969) Science , vol.166 , pp. 386-388
    • Olney, J.W.1    Sharpe, L.G.2
  • 40
    • 0034812501 scopus 로고    scopus 로고
    • Ca(2+)-induced inhibition of apoptosis in human SH-SY5Y neuroblastoma cells: Degradation of apoptotic protease activating factor-1 (APAF-1)
    • Reimertz C., Kogel D., Lankiewicz S., Poppe M. and Prehn J. H. (2001) Ca(2+)-induced inhibition of apoptosis in human SH-SY5Y neuroblastoma cells: degradation of apoptotic protease activating factor-1 (APAF-1). J. Neurochem. 78, 1256-1266.
    • (2001) J. Neurochem. , vol.78 , pp. 1256-1266
    • Reimertz, C.1    Kogel, D.2    Lankiewicz, S.3    Poppe, M.4    Prehn, J.H.5
  • 42
    • 0024363137 scopus 로고
    • Calpain I activation is specifically related to excitatory amino acid induction of hippocampal damage
    • Siman R., Noszek J. C. and Kegerise C. (1989) Calpain I activation is specifically related to excitatory amino acid induction of hippocampal damage. J. Neurosci. 9, 1579-1590.
    • (1989) J. Neurosci. , vol.9 , pp. 1579-1590
    • Siman, R.1    Noszek, J.C.2    Kegerise, C.3
  • 46
    • 0028024908 scopus 로고
    • Triggering and execution of neuronal death in brain ischaemia: Two phases of glutamate release by different mechanisms
    • Szatkowski M. and Attwell D. (1994) Triggering and execution of neuronal death in brain ischaemia: two phases of glutamate release by different mechanisms. Trends Neurosci. 17, 359-365.
    • (1994) Trends Neurosci. , vol.17 , pp. 359-365
    • Szatkowski, M.1    Attwell, D.2
  • 47
    • 0028965234 scopus 로고
    • Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains
    • Takano E., Ma H., Yang H. Q., Maki M. and Hatanaka M. (1995) Preference of calcium-dependent interactions between calmodulin-like domains of calpain and calpastatin subdomains. FEBS Lett. 362, 93-97.
    • (1995) FEBS Lett. , vol.362 , pp. 93-97
    • Takano, E.1    Ma, H.2    Yang, H.Q.3    Maki, M.4    Hatanaka, M.5
  • 48
    • 0035807940 scopus 로고    scopus 로고
    • Calpain inhibitors prevent nitric oxide-triggered excitotoxic apoptosis
    • Volbracht C., Fava E., Leist M. and Nicotera P. (2001a) Calpain inhibitors prevent nitric oxide-triggered excitotoxic apoptosis. Neuroreport 12, 3645-3648.
    • (2001) Neuroreport , vol.12 , pp. 3645-3648
    • Volbracht, C.1    Fava, E.2    Leist, M.3    Nicotera, P.4
  • 50
    • 0032810012 scopus 로고    scopus 로고
    • ATP controls neuronal apoptosis triggered by microtubule breakdown or potassium deprivation
    • Volbracht C., Leist M. and Nicotera P. (1999) ATP controls neuronal apoptosis triggered by microtubule breakdown or potassium deprivation. Mol Med. 5, 477-49.
    • (1999) Mol. Med. , vol.5 , pp. 477-489
    • Volbracht, C.1    Leist, M.2    Nicotera, P.3
  • 53
    • 0033199115 scopus 로고    scopus 로고
    • Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation
    • Wolf B. B., Goldstein J. C., Stennicke H. R., Beere H., Amarante-Mendes G. P., Salvesen G. S. and Green D. R. (1999) Calpain functions in a caspase-independent manner to promote apoptosis-like events during platelet activation. Blood 94, 1683-1692.
    • (1999) Blood , vol.94 , pp. 1683-1692
    • Wolf, B.B.1    Goldstein, J.C.2    Stennicke, H.R.3    Beere, H.4    Amarante-Mendes, G.P.5    Salvesen, G.S.6    Green, D.R.7
  • 55
    • 0034193138 scopus 로고    scopus 로고
    • Cleavage of Bax enhances its cell death function
    • Wood D. E. and Newcomb E. W. (2000) Cleavage of Bax enhances its cell death function. Exp Cell Res. 256, 375-382.
    • (2000) Exp. Cell Res. , vol.256 , pp. 375-382
    • Wood, D.E.1    Newcomb, E.W.2
  • 57
    • 0025768972 scopus 로고
    • Mechanisms underlying initiation of excitotoxicity associated with metabolic inhibition
    • Zeevalk G. D. and Nicklas W. J. (1991) Mechanisms underlying initiation of excitotoxicity associated with metabolic inhibition. J. Pharmacol. Exp Ther 257, 870-878.
    • (1991) J. Pharmacol. Exp. Ther. , vol.257 , pp. 870-878
    • Zeevalk, G.D.1    Nicklas, W.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.