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Volumn 581, Issue 15, 2007, Pages 2761-2767

Protease signalling in cell death: caspases versus cysteine cathepsins

Author keywords

Apoptosis; Caspases; Cathepsins; Cell death; Necrosis; Protease signalling

Indexed keywords

CASPASE; CATHEPSIN; CYSTEINE; PROTEIN BCL 2; PROTEINASE;

EID: 34249893895     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.05.038     Document Type: Short Survey
Times cited : (189)

References (58)
  • 1
    • 0034641918 scopus 로고    scopus 로고
    • The biochemistry of apoptosis
    • Hengartner M.O. The biochemistry of apoptosis. Nature 407 (2000) 770-776
    • (2000) Nature , vol.407 , pp. 770-776
    • Hengartner, M.O.1
  • 2
    • 0034641932 scopus 로고    scopus 로고
    • From bench to clinic with apoptosis-based therapeutic agents
    • Nicholson D.W. From bench to clinic with apoptosis-based therapeutic agents. Nature 407 (2000) 810-816
    • (2000) Nature , vol.407 , pp. 810-816
    • Nicholson, D.W.1
  • 3
    • 33845977959 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization in cell death
    • Kroemer G., Galluzzi L., and Brenner C. Mitochondrial membrane permeabilization in cell death. Physiol. Rev. 87 (2007) 99-163
    • (2007) Physiol. Rev. , vol.87 , pp. 99-163
    • Kroemer, G.1    Galluzzi, L.2    Brenner, C.3
  • 4
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson D.W. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ. 6 (1999) 1028-1042
    • (1999) Cell Death Differ. , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 5
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: structure, activation, substrates, and functions during apoptosis
    • Earnshaw W.C., Martins L.M., and Kaufmann S.H. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68 (1999) 383-424
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 7
    • 33748308883 scopus 로고    scopus 로고
    • Targeting proteases: successes, failures and future prospects
    • Turk B. Targeting proteases: successes, failures and future prospects. Nat. Rev. Drug Discov. 5 (2006) 785-799
    • (2006) Nat. Rev. Drug Discov. , vol.5 , pp. 785-799
    • Turk, B.1
  • 8
    • 10644282148 scopus 로고    scopus 로고
    • The protein structures that shape caspase activity, specificity, activation and inhibition
    • Fuentes-Prior P., and Salvesen G.S. The protein structures that shape caspase activity, specificity, activation and inhibition. Biochem. J. 384 (2004) 201-232
    • (2004) Biochem. J. , vol.384 , pp. 201-232
    • Fuentes-Prior, P.1    Salvesen, G.S.2
  • 12
    • 0034616946 scopus 로고    scopus 로고
    • Apoptotic pathways: paper wraps stone blunts scissors
    • Green D.R. Apoptotic pathways: paper wraps stone blunts scissors. Cell 102 (2000) 1-4
    • (2000) Cell , vol.102 , pp. 1-4
    • Green, D.R.1
  • 14
    • 0037341354 scopus 로고    scopus 로고
    • Caspase activation by granzyme B is indirect, and caspase autoprocessing requires the release of proapoptotic mitochondrial factors
    • Sutton V.R., Wowk M.E., Cancilla M., and Trapani J.A. Caspase activation by granzyme B is indirect, and caspase autoprocessing requires the release of proapoptotic mitochondrial factors. Immunity 18 (2003) 319-329
    • (2003) Immunity , vol.18 , pp. 319-329
    • Sutton, V.R.1    Wowk, M.E.2    Cancilla, M.3    Trapani, J.A.4
  • 15
    • 0242432345 scopus 로고    scopus 로고
    • Many cuts to ruin: a comprehensive update of caspase substrates
    • Fischer U., Janicke R.U., and Schulze-Osthoff K. Many cuts to ruin: a comprehensive update of caspase substrates. Cell Death Differ. 10 (2003) 76-100
    • (2003) Cell Death Differ. , vol.10 , pp. 76-100
    • Fischer, U.1    Janicke, R.U.2    Schulze-Osthoff, K.3
  • 17
    • 0033539067 scopus 로고    scopus 로고
    • Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation
    • Sahara S., Aoto M., Eguchi Y., Imamoto N., Yoneda Y., and Tsujimoto Y. Acinus is a caspase-3-activated protein required for apoptotic chromatin condensation. Nature 401 (1999) 168-173
    • (1999) Nature , vol.401 , pp. 168-173
    • Sahara, S.1    Aoto, M.2    Eguchi, Y.3    Imamoto, N.4    Yoneda, Y.5    Tsujimoto, Y.6
  • 18
    • 0035478060 scopus 로고    scopus 로고
    • Differential expression of apoptotic protease-activating factor-1 and caspase-3 genes and susceptibility to apoptosis during brain development and after traumatic brain injury
    • Yakovlev A.G., Ota K., Wang G., Movsesyan V., Bao W.L., Yoshihara K., and Faden A.I. Differential expression of apoptotic protease-activating factor-1 and caspase-3 genes and susceptibility to apoptosis during brain development and after traumatic brain injury. J. Neurosci. 21 (2001) 7439-7446
    • (2001) J. Neurosci. , vol.21 , pp. 7439-7446
    • Yakovlev, A.G.1    Ota, K.2    Wang, G.3    Movsesyan, V.4    Bao, W.L.5    Yoshihara, K.6    Faden, A.I.7
  • 19
    • 33745122159 scopus 로고    scopus 로고
    • Differential regulation of the intrinsic pathway of apoptosis in brain and liver during ageing
    • Stoka V., Turk V., and Bredesen D.E. Differential regulation of the intrinsic pathway of apoptosis in brain and liver during ageing. FEBS Lett. 580 (2006) 3739-3745
    • (2006) FEBS Lett. , vol.580 , pp. 3739-3745
    • Stoka, V.1    Turk, V.2    Bredesen, D.E.3
  • 20
    • 19544382901 scopus 로고    scopus 로고
    • The caspase-8 modulator c-FLIP
    • Kataoka T. The caspase-8 modulator c-FLIP. Crit. Rev. Immunol. 25 (2005) 31-58
    • (2005) Crit. Rev. Immunol. , vol.25 , pp. 31-58
    • Kataoka, T.1
  • 22
    • 0033082995 scopus 로고    scopus 로고
    • IAP family proteins-suppressors of apoptosis
    • Deveraux Q.L., and Reed J.C. IAP family proteins-suppressors of apoptosis. Genes Dev. 13 (1999) 239-252
    • (1999) Genes Dev. , vol.13 , pp. 239-252
    • Deveraux, Q.L.1    Reed, J.C.2
  • 23
    • 33749252583 scopus 로고    scopus 로고
    • Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family
    • Eckelman B.P., Salvesen G.S., and Scott F.L. Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family. EMBO Rep. 7 (2006) 988-994
    • (2006) EMBO Rep. , vol.7 , pp. 988-994
    • Eckelman, B.P.1    Salvesen, G.S.2    Scott, F.L.3
  • 24
    • 0035986219 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators
    • Turk B., Turk D., and Salvesen G.S. Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Curr. Pharm. Des. 8 (2002) 1623-1637
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 1623-1637
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 25
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: more than scavengers
    • Turk B., Turk D., and Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim. Biophys. Acta 1477 (2000) 98-111
    • (2000) Biochim. Biophys. Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 26
    • 0035801514 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: facts and opportunities
    • Turk V., Turk B., and Turk D. Lysosomal cysteine proteases: facts and opportunities. EMBO J. 20 (2001) 4629-4633
    • (2001) EMBO J. , vol.20 , pp. 4629-4633
    • Turk, V.1    Turk, B.2    Turk, D.3
  • 27
    • 0016198057 scopus 로고
    • Cathepsin D: rapid isolation by affinity chromatography on haemoglobin-agarose resin
    • Smith R., and Turk V. Cathepsin D: rapid isolation by affinity chromatography on haemoglobin-agarose resin. Eur. J. Biochem. 48 (1974) 245-254
    • (1974) Eur. J. Biochem. , vol.48 , pp. 245-254
    • Smith, R.1    Turk, V.2
  • 28
    • 33846164404 scopus 로고    scopus 로고
    • Emerging roles of cysteine cathepsins in disease and their potential as drug targets
    • Vasiljeva O., Reinheckel T., Peters C., Turk D., Turk V., and Turk B. Emerging roles of cysteine cathepsins in disease and their potential as drug targets. Curr. Pharm. Des. 13 (2007) 387-403
    • (2007) Curr. Pharm. Des. , vol.13 , pp. 387-403
    • Vasiljeva, O.1    Reinheckel, T.2    Peters, C.3    Turk, D.4    Turk, V.5    Turk, B.6
  • 30
    • 28544435485 scopus 로고    scopus 로고
    • Lysosomes and autophagy in cell death control
    • Kroemer G., and Jaattela M. Lysosomes and autophagy in cell death control. Nat. Rev. Cancer 5 (2005) 886-897
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 886-897
    • Kroemer, G.1    Jaattela, M.2
  • 31
    • 0034948738 scopus 로고    scopus 로고
    • The autophagosomal-lysosomal compartment in programmed cell death
    • Bursch W. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ. 8 (2001) 569-581
    • (2001) Cell Death Differ. , vol.8 , pp. 569-581
    • Bursch, W.1
  • 32
    • 0029782494 scopus 로고    scopus 로고
    • Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha
    • Deiss L.P., Galinka H., Berissi H., Cohen O., and Kimchi A. Cathepsin D protease mediates programmed cell death induced by interferon-gamma, Fas/APO-1 and TNF-alpha. EMBO J. 15 (1996) 3861-3870
    • (1996) EMBO J. , vol.15 , pp. 3861-3870
    • Deiss, L.P.1    Galinka, H.2    Berissi, H.3    Cohen, O.4    Kimchi, A.5
  • 36
    • 21344455498 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: structural features and their role in apoptosis
    • Stoka V., Turk B., and Turk V. Lysosomal cysteine proteases: structural features and their role in apoptosis. IUBMB Life 57 (2006) 347-353
    • (2006) IUBMB Life , vol.57 , pp. 347-353
    • Stoka, V.1    Turk, B.2    Turk, V.3
  • 37
    • 0242609099 scopus 로고    scopus 로고
    • Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine
    • Johansson A.C., Steen H., Ollinger K., and Roberg K. Cathepsin D mediates cytochrome c release and caspase activation in human fibroblast apoptosis induced by staurosporine. Cell Death Differ. 10 (2003) 1253-1259
    • (2003) Cell Death Differ. , vol.10 , pp. 1253-1259
    • Johansson, A.C.1    Steen, H.2    Ollinger, K.3    Roberg, K.4
  • 38
    • 84944051604 scopus 로고    scopus 로고
    • Cathepsin D
    • Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds), Elsevier Academic Press, Amsterdam
    • Conner G.E. Cathepsin D. In: Barrett A.J., Rawlings N.D., and Woessner J.F. (Eds). Handbook of Proteolytic Enzymes. second ed. (2004), Elsevier Academic Press, Amsterdam 43-52
    • (2004) Handbook of Proteolytic Enzymes. second ed. , pp. 43-52
    • Conner, G.E.1
  • 39
    • 0041912315 scopus 로고    scopus 로고
    • Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D
    • Tardy C., Tyynela J., Hasilik A., Levade T., and Andrieu-Abadie N. Stress-induced apoptosis is impaired in cells with a lysosomal targeting defect but is not affected in cells synthesizing a catalytically inactive cathepsin D. Cell Death Differ. 10 (2003) 1090-1100
    • (2003) Cell Death Differ. , vol.10 , pp. 1090-1100
    • Tardy, C.1    Tyynela, J.2    Hasilik, A.3    Levade, T.4    Andrieu-Abadie, N.5
  • 40
    • 0029284365 scopus 로고
    • Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins
    • Turk B., Bieth J.G., Bjork I., Dolenc I., Turk D., Cimerman N., Kos J., Colic A., Stoka V., and Turk V. Regulation of the activity of lysosomal cysteine proteinases by pH-induced inactivation and/or endogenous protein inhibitors, cystatins. Biol. Chem. Hoppe Seyler 376 (1995) 225-230
    • (1995) Biol. Chem. Hoppe Seyler , vol.376 , pp. 225-230
    • Turk, B.1    Bieth, J.G.2    Bjork, I.3    Dolenc, I.4    Turk, D.5    Cimerman, N.6    Kos, J.7    Colic, A.8    Stoka, V.9    Turk, V.10
  • 41
    • 4544246352 scopus 로고    scopus 로고
    • Alterations of intracellular pH homeostasis in apoptosis: origins and roles
    • Lagadic-Gossmann D., Huc L., and Lecureur V. Alterations of intracellular pH homeostasis in apoptosis: origins and roles. Cell Death Differ. 11 (2004) 953-961
    • (2004) Cell Death Differ. , vol.11 , pp. 953-961
    • Lagadic-Gossmann, D.1    Huc, L.2    Lecureur, V.3
  • 43
    • 0036671894 scopus 로고    scopus 로고
    • The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta
    • Martinon F., Burns K., and Tschopp J. The inflammasome: a molecular platform triggering activation of inflammatory caspases and processing of proIL-beta. Mol Cell. 10 (2002) 417-426
    • (2002) Mol Cell. , vol.10 , pp. 417-426
    • Martinon, F.1    Burns, K.2    Tschopp, J.3
  • 44
    • 0942265544 scopus 로고    scopus 로고
    • Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins
    • Cirman T., Oresic K., Mazovec G.D., Turk V., Reed J.C., Myers R.M., Salvesen G.S., and Turk B. Selective disruption of lysosomes in HeLa cells triggers apoptosis mediated by cleavage of Bid by multiple papain-like lysosomal cathepsins. J. Biol. Chem. 279 (2004) 3578-3587
    • (2004) J. Biol. Chem. , vol.279 , pp. 3578-3587
    • Cirman, T.1    Oresic, K.2    Mazovec, G.D.3    Turk, V.4    Reed, J.C.5    Myers, R.M.6    Salvesen, G.S.7    Turk, B.8
  • 45
    • 34247849157 scopus 로고    scopus 로고
    • Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization
    • Blomgran R., Zheng L., and Stendahl O. Cathepsin-cleaved Bid promotes apoptosis in human neutrophils via oxidative stress-induced lysosomal membrane permeabilization. J. Leukoc. Biol. 81 (2007) 1213-1223
    • (2007) J. Leukoc. Biol. , vol.81 , pp. 1213-1223
    • Blomgran, R.1    Zheng, L.2    Stendahl, O.3
  • 46
    • 0348038755 scopus 로고    scopus 로고
    • Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1)
    • Houseweart M.K., Vilaythong A., Yin X.M., Turk B., Noebels J.L., and Myers R.M. Apoptosis caused by cathepsins does not require Bid signaling in an in vivo model of progressive myoclonus epilepsy (EPM1). Cell Death Differ. 10 (2003) 1329-1335
    • (2003) Cell Death Differ. , vol.10 , pp. 1329-1335
    • Houseweart, M.K.1    Vilaythong, A.2    Yin, X.M.3    Turk, B.4    Noebels, J.L.5    Myers, R.M.6
  • 48
    • 0032891626 scopus 로고    scopus 로고
    • The fate of E- and P-cadherin during the early stages of apoptosis
    • Schmeiser K., and Grand R.J. The fate of E- and P-cadherin during the early stages of apoptosis. Cell Death Differ. 6 (1999) 377-386
    • (1999) Cell Death Differ. , vol.6 , pp. 377-386
    • Schmeiser, K.1    Grand, R.J.2
  • 50
    • 0043234207 scopus 로고    scopus 로고
    • Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis
    • Bidere N., Lorenzo H.K., Carmona S., Laforge M., Harper F., Dumont C., and Senik A. Cathepsin D triggers Bax activation, resulting in selective apoptosis-inducing factor (AIF) relocation in T lymphocytes entering the early commitment phase to apoptosis. J. Biol. Chem. 278 (2003) 31401-31411
    • (2003) J. Biol. Chem. , vol.278 , pp. 31401-31411
    • Bidere, N.1    Lorenzo, H.K.2    Carmona, S.3    Laforge, M.4    Harper, F.5    Dumont, C.6    Senik, A.7
  • 52
    • 0038677510 scopus 로고    scopus 로고
    • Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine
    • Boya P., Gonzalez-Polo R.A., Poncet D., Andreau K., Vieira H.L., Roumier T., Perfettini J.L., and Kroemer G. Mitochondrial membrane permeabilization is a critical step of lysosome-initiated apoptosis induced by hydroxychloroquine. Oncogene 22 (2003) 3927-3936
    • (2003) Oncogene , vol.22 , pp. 3927-3936
    • Boya, P.1    Gonzalez-Polo, R.A.2    Poncet, D.3    Andreau, K.4    Vieira, H.L.5    Roumier, T.6    Perfettini, J.L.7    Kroemer, G.8
  • 53
    • 0141447370 scopus 로고    scopus 로고
    • Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis
    • Zhao M., Antunes F., Eaton J.W., and Brunk U.T. Lysosomal enzymes promote mitochondrial oxidant production, cytochrome c release and apoptosis. Eur. J. Biochem. 270 (2003) 3778-3786
    • (2003) Eur. J. Biochem. , vol.270 , pp. 3778-3786
    • Zhao, M.1    Antunes, F.2    Eaton, J.W.3    Brunk, U.T.4
  • 55
    • 23944522127 scopus 로고    scopus 로고
    • Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators
    • Turk B., Turk D., and Salvesen G.S. Regulating cysteine protease activity: essential role of protease inhibitors as guardians and regulators. Med. Chem. Rev. 2 (2005) 283-297
    • (2005) Med. Chem. Rev. , vol.2 , pp. 283-297
    • Turk, B.1    Turk, D.2    Salvesen, G.S.3
  • 56
    • 0031764610 scopus 로고    scopus 로고
    • Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice
    • Pennacchio L.A., Bouley D.M., Higgins K.M., Scott M.P., Noebels J.L., and Myers R.M. Progressive ataxia, myoclonic epilepsy and cerebellar apoptosis in cystatin B-deficient mice. Nat. Genet. 20 (1998) 251-258
    • (1998) Nat. Genet. , vol.20 , pp. 251-258
    • Pennacchio, L.A.1    Bouley, D.M.2    Higgins, K.M.3    Scott, M.P.4    Noebels, J.L.5    Myers, R.M.6
  • 57
    • 0036463649 scopus 로고    scopus 로고
    • Apoptosis-based therapies
    • Reed J.C. Apoptosis-based therapies. Nat. Rev. Drug Disc. 1 (2002) 111-121
    • (2002) Nat. Rev. Drug Disc. , vol.1 , pp. 111-121
    • Reed, J.C.1
  • 58
    • 22944473652 scopus 로고    scopus 로고
    • New approaches and therapeutics in targeting apoptosis in disease
    • Fischer U., and Schulze-Osthoff K. New approaches and therapeutics in targeting apoptosis in disease. Pharmacol. Rev. 57 (2006) 187-215
    • (2006) Pharmacol. Rev. , vol.57 , pp. 187-215
    • Fischer, U.1    Schulze-Osthoff, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.