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Volumn 2, Issue 2, 2003, Pages 141-152

μ-calpain activation in β-lapachone-mediated apoptosis

Author keywords

lapachone; Apoptosis; Breast cancer; Ca2+; Calpain

Indexed keywords

ANTINEOPLASTIC ANTIBIOTIC; BETA LAPACHONE; BETA-LAPACHONE; CALCIUM; CALCIUM BINDING PROTEIN; CALPAIN; CALPASTATIN; CASPASE; CYSTEINE PROTEINASE INHIBITOR; M CALPAIN; M-CALPAIN; MU CALPAIN; MU-CALPAIN; NAPHTHOQUINONE; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; NQO1 PROTEIN, HUMAN; PROTEIN P53; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE (PHOSPHATE) DEHYDROGENASE (QUINONE);

EID: 0141976410     PISSN: 15384047     EISSN: 15558576     Source Type: Journal    
DOI: 10.4161/cbt.2.2.237     Document Type: Article
Times cited : (67)

References (83)
  • 1
    • 0029927422 scopus 로고    scopus 로고
    • The role of protesases during apoptosis
    • Patel T, Gores GJ, Kaufmann SH. The role of protesases during apoptosis. Faseb J 1996; 5:587-97.
    • (1996) Faseb J , vol.5 , pp. 587-597
    • Patel, T.1    Gores, G.J.2    Kaufmann, S.H.3
  • 2
    • 0030715323 scopus 로고    scopus 로고
    • Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade
    • Li P, Nijhawan D, Budihardjo I, Srinivasula SM, Ahmad M, Alnemri ES, et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 1997; 91:479-89. (Pubitemid 27508237)
    • (1997) Cell , vol.91 , Issue.4 , pp. 479-489
    • Li, P.1    Nijhawan, D.2    Budihardjo, I.3    Srinivasula, S.M.4    Ahmad, M.5    Alnemri, E.S.6    Wang, X.7
  • 4
    • 0030892234 scopus 로고    scopus 로고
    • Apoptosis by death factor
    • DOI 10.1016/S0092-8674(00)81874-7
    • Nagata S. Apoptosis by death factor. Cell 1997; 88:355-65. (Pubitemid 27131377)
    • (1997) Cell , vol.88 , Issue.3 , pp. 355-365
    • Nagata, S.1
  • 5
    • 0031569532 scopus 로고    scopus 로고
    • Calpain, an Upstream Regulator of Thymocyte Apoptosis
    • Squier MK, Cohen JJ. Calpain, an upstream regulator of thymocyte apoptosis. J Immunol 1997; 158:3690-7. (Pubitemid 127488723)
    • (1997) Journal of Immunology , vol.158 , Issue.8 , pp. 3690-3697
    • Squier, M.K.T.1    Cohen, J.J.2
  • 8
    • 0026062980 scopus 로고
    • Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: Immunofluorescence localization and compartmentation of mu- and mCANP
    • Banik NL, DeVries GH, Neuberger T, Russell T, Chakrabarti AK, Hogan EL. Calcium-activated neutral proteinase (CANP; calpain) activity in Schwann cells: immunofluorescence localization and compartmentation of mu- and mCANP. J Neurosci Res 1991; 29:346-54.
    • (1991) J Neurosci Res , vol.29 , pp. 346-354
    • Banik, N.L.1    DeVries, G.H.2    Neuberger, T.3    Russell, T.4    Chakrabarti, A.K.5    Hogan, E.L.6
  • 10
    • 0030464946 scopus 로고    scopus 로고
    • Regulation of the calpain-calpastatin system by membranes
    • (review)
    • Kawasaki H, Kawashima S. Regulation of the calpain-calpastatin system by membranes (review). Mol Membr Biol 1996; 13:217-24.
    • (1996) Mol Membr Biol , vol.13 , pp. 217-224
    • Kawasaki, H.1    Kawashima, S.2
  • 11
    • 0027360303 scopus 로고
    • Studies of the active site of m-calpain and the interaction with calpastatin
    • Crawford C, Brown NR, Willis AC. Studies of the active site of m-calpain and the interaction with calpastatin. Biochem J 1993; 296:135-42. (Pubitemid 23344740)
    • (1993) Biochemical Journal , vol.296 , Issue.1 , pp. 135-142
    • Crawford, C.1    Brown, N.R.2    Willis, A.C.3
  • 12
    • 0019890461 scopus 로고
    • 2+-activated neutral proteinase (CaANP) and its specific inhibitor
    • 2+-activated neutral proteinase (CaANP) and its specific inhibitor. FEBS Lett 1981;136:221-4.
    • (1981) FEBS Lett , vol.136 , pp. 221-224
    • Cottin, P.1    Vidalenc, P.L.2    Ducastaing, A.3
  • 13
    • 0027940509 scopus 로고
    • Domain structure of calpain: Mapping the binding site for calpastatin
    • DOI 10.1021/bi00249a008
    • Croall DE, McGrody KS. Domain structure of calpain: mapping the binding site for calpastatin. Biochemistry 1994; 33:13223-30. (Pubitemid 24373236)
    • (1994) Biochemistry , vol.33 , Issue.45 , pp. 13223-13230
    • Croall, D.E.1    McGrody, K.S.2
  • 14
    • 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, 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 1995; 270:31158-62.
    • (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
  • 15
    • 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, Hatanaka M. Inhibition of calpain by a synthetic oligopeptide corresponding to an exon of the human calpastatin gene. J Biol Chem 1989; 264:18866-9. (Pubitemid 19285783)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.32 , pp. 18866-18869
    • Maki, M.1    Bagci, H.2    Hamaguchi, K.3    Ueda, M.4    Murachi, T.5    Hatanaka, M.6
  • 16
    • 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, Hatanaka M. Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli. J Biol Chem 1988; 263:10254-61.
    • (1988) J Biol Chem , vol.263 , pp. 10254-10261
    • Maki, M.1    Takano, E.2    Osawa, T.3    Ooi, T.4    Murachi, T.5    Hatanaka, M.6
  • 17
    • 0024346641 scopus 로고
    • Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease
    • Kawasaki H, Emori Y, Imajoh-Ohmi S, Minami Y, Suzuki K. Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. J Biochem (Tokyo) 1989; 106:274-81. (Pubitemid 19203784)
    • (1989) Journal of Biochemistry , vol.106 , Issue.2 , pp. 274-281
    • Kawasaki, H.1    Emori, Y.2    Imajoh-Ohmi, S.3    Minami, Y.4    Suzuki, K.5
  • 18
    • 0028982219 scopus 로고
    • β-lapachone-mediated apoptosis in human promyelocytic leukemia (HL- 60) and human prostate cancer cells: A p53-independent response
    • Planchon SM, Wuerzberger S, Frydman B, Witiak DT, Hutson P, Church DR, et al. β-lapachone-mediated apoptosis in human promyelocytic leukemia (HL- 60) and human prostate cancer cells: a p53-independent response. Cancer Res 1995; 55:3706-11.
    • (1995) Cancer Res , vol.55 , pp. 3706-3711
    • Planchon, S.M.1    Wuerzberger, S.2    Frydman, B.3    Witiak, D.T.4    Hutson, P.5    Church, D.R.6
  • 21
    • 0033539487 scopus 로고    scopus 로고
    • Potent inhibition of tumor survival in vivo by β-lapachone plus taxol: Combining drugs imposes different artificial checkpoints
    • Li CJ, Li YZ, Pinto AV, Pardee AB. Potent inhibition of tumor survival in vivo by β-lapachone plus taxol: combining drugs imposes different artificial checkpoints. Proc Natl Acad Sci USA 1999; 96:13369-74.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13369-13374
    • Li, C.J.1    Li, Y.Z.2    Pinto, A.V.3    Pardee, A.B.4
  • 22
    • 0035056968 scopus 로고    scopus 로고
    • Induction of CDK inhibitors (p21(WAF1) and p27(Kip1)) and Bak in the β-lapachone-induced apoptosis of human prostate cancer cells
    • Don MJ, Chang YH, Chen KK, Ho LK, Chau YP. Induction of CDK inhibitors (p21(WAF1) and p27(Kip1)) and Bak in the β-lapachone-induced apoptosis of human prostate cancer cells. Mol Pharmacol 2001; 59:784-94.
    • (2001) Mol Pharmacol , vol.59 , pp. 784-794
    • Don, M.J.1    Chang, Y.H.2    Chen, K.K.3    Ho, L.K.4    Chau, Y.P.5
  • 23
    • 0034570848 scopus 로고    scopus 로고
    • Potent induction of apoptosis by β-lapachone in human multiple myeloma cell lines and patient cells
    • Li Y, Li CJ, Yu D, Pardee AB. Potent induction of apoptosis by β-lapachone in human multiple myeloma cell lines and patient cells. Mol Med 2000; 6:1008-15.
    • (2000) Mol Med , vol.6 , pp. 1008-1015
    • Li, Y.1    Li, C.J.2    Yu, D.3    Pardee, A.B.4
  • 30
    • 0031014946 scopus 로고    scopus 로고
    • Proteolytic cleavage of human p53 by calpain: A potential regulator of protein stability
    • Kubbutat MH, Vousden KH. Proteolytic cleavage of human p53 by calpain: a potential regulator of protein stability. Mol Cell Biol 1997; 17:460-8. (Pubitemid 26425636)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.1 , pp. 460-468
    • Kubbutat, M.H.G.1    Vousden, K.H.2
  • 31
    • 0034698878 scopus 로고    scopus 로고
    • Cross-talk between two cysteine protease families: Activation of caspase-12 by calpain in apoptosis
    • DOI 10.1083/jcb.150.4.887
    • Nakagawa T, Yuan J. Cross-talk between two cysteine protease families. Activation of caspase- 12 by calpain in apoptosis. J Cell Biol 2000; 150:887-94. (Pubitemid 30663424)
    • (2000) Journal of Cell Biology , vol.150 , Issue.4 , pp. 887-894
    • Nakagawa, T.1    Yuan, J.2
  • 32
    • 0029844145 scopus 로고    scopus 로고
    • Irreversible loss of the oestrogen receptor in T47D breast cancer cells following prolonged oestrogen deprivation
    • Pink JJ, Bilimoria MM, Assikis J, Jordan VC. Irreversible loss of the oestrogen receptor in T47D breast cancer cells following prolonged oestrogen deprivation. Br J Cancer 1996; 74:1227-36. (Pubitemid 26360111)
    • (1996) British Journal of Cancer , vol.74 , Issue.8 , pp. 1227-1236
    • Pink, J.J.1    Bilimoria, M.M.2    Assikis, J.3    Jordan, V.C.4
  • 33
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-54.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 34
    • 0031666337 scopus 로고    scopus 로고
    • Immunohistochemical detection of NAD(P)H:Quinone oxidoreductase in human lung and lung tumors
    • Siegel D, Franklin WA, Ross D. Immunohistochemical detection of NAD(P)H:quinone oxidoreductase in human lung and lung tumors. Clin Cancer Res 1998; 4:2065-70. (Pubitemid 28415648)
    • (1998) Clinical Cancer Research , vol.4 , Issue.9 , pp. 2065-2070
    • Siegel, D.1    Franklin, W.A.2    Ross, D.3
  • 35
    • 0031027683 scopus 로고    scopus 로고
    • 1 to S-phase transition
    • Zhang W, Lu Q, Xie ZJ, Mellgren RL. Inhibition of the growth of WI-38 fibroblasts by benzyloxycarbonyl-Leu- Leu-Tyr diazomethyl ketone: evidence that cleavage of p53 by a calpain- like protease is necessary for G1 to S-phase transition. Oncogene 1997; 14:255-63. (Pubitemid 27073080)
    • (1997) Oncogene , vol.14 , Issue.3 , pp. 255-263
    • Zhang, W.1    Lu, Q.2    Xie, Z.-J.3    Mellgren, R.L.4
  • 36
    • 0032546795 scopus 로고    scopus 로고
    • Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis
    • DOI 10.1074/jbc.273.25.15540
    • Janicke RU, Ng P, Sprengart ML, Porter AG. Caspase-3 is required for alpha-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J Biol Chem 1998; 273:15540-5. (Pubitemid 28298165)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15540-15545
    • Janicke, R.U.1    Ng, P.2    Sprengart, M.L.3    Porter, A.G.4
  • 38
    • 0031029804 scopus 로고    scopus 로고
    • Isolation and identification of a proteinase from calf thymus that cleaves poly(ADP-ribose) polymerase and histone H1
    • DOI 10.1016/S0167-4838(96)00189-6, PII S0167483896001896
    • Buki KG, Bauer PI, Kun E. Isolation and identification of a proteinase from calf thymus that cleaves poly(ADP-ribose) polymerase and histone H1. Biochim Biophys Acta 1997; 1338:100-6. (Pubitemid 27107849)
    • (1997) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1338 , Issue.1 , pp. 100-106
    • Buki, K.G.1    Bauer, P.I.2    Kun, E.3
  • 39
    • 0030612795 scopus 로고    scopus 로고
    • Restriction of microM-calcium-requiring calpain activation to the plasma membrane in human neuroblastoma cells: Evidence for regionalized influence of a calpain activator protein
    • DOI 10.1002/(SICI)1097-4547(19970615)48:6<543::AID-JNR7>3.0.CO;2-A
    • Shea TB. Restriction of microM-calcium-requiring calpain activation to the plasma membrane in human neuroblastoma cells: evidence for regionalized influence of a calpain activator protein. J Neurosci Res 1997; 48:543-50. (Pubitemid 27276684)
    • (1997) Journal of Neuroscience Research , vol.48 , Issue.6 , pp. 543-550
    • Shea, T.B.1
  • 41
    • 0023658410 scopus 로고
    • Calcium-activated neutral protease and its endogenous inhibitor. Activation at the cell membrane and biological function
    • Suzuki K, Imajoh S, Emori Y, Kawasaki H, Minami Y, Ohno S. Calcium-activated neutral protease and its endogenous inhibitor. Activation at the cell membrane and biological function. FEBS Lett 1987; 220:271-7.
    • (1987) FEBS Lett , vol.220 , pp. 271-277
    • Suzuki, K.1    Imajoh, S.2    Emori, Y.3    Kawasaki, H.4    Minami, Y.5    Ohno, S.6
  • 42
    • 0028868307 scopus 로고
    • Purification and properties of high molecular weight calpastatin from bovine brain
    • Mohan PS, Nixon RA. Purification and properties of high molecular weight calpastatin from bovine brain. J Neurochem 1995; 64:859-66.
    • (1995) J Neurochem , vol.64 , pp. 859-866
    • Mohan, P.S.1    Nixon, R.A.2
  • 43
    • 0023659729 scopus 로고
    • All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II
    • Maki M, Takano E, Mori H, Sato A, Murachi T, Hatanaka M. All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II. FEBS Lett 1987; 223:174-80.
    • (1987) FEBS Lett , vol.223 , pp. 174-180
    • Maki, M.1    Takano, E.2    Mori, H.3    Sato, A.4    Murachi, T.5    Hatanaka, M.6
  • 44
    • 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, Suzuki K. 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 1988; 263:2364-70. (Pubitemid 18060298)
    • (1988) Journal of Biological Chemistry , vol.263 , Issue.5 , pp. 2364-2370
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Minami, Y.4    Suzuki, K.5
  • 45
    • 0033931805 scopus 로고    scopus 로고
    • Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues
    • Takano J, Watanabe M, Hitomi K, Maki M. Four types of calpastatin isoforms with distinct amino-terminal sequences are specified by alternative first exons and differentially expressed in mouse tissues. J Biochem (Tokyo) 2000; 128:83-92. (Pubitemid 30485372)
    • (2000) Journal of Biochemistry , vol.128 , Issue.1 , pp. 83-92
    • Takano, J.1    Watanabe, M.2    Hitomi, K.3    Maki, M.4
  • 47
    • 0027980319 scopus 로고
    • Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules
    • DOI 10.1016/S0092-8674(94)90462-6
    • Rock KL, Gramm C, Rothstein L, Clark K, Stein R, Dick L, et al. Inhibitors of the proteasome block the degradation of most cell proteins and the generation of peptides presented on MHC class I molecules. Cell 1994; 78:761-71. (Pubitemid 24294452)
    • (1994) Cell , vol.78 , Issue.5 , pp. 761-771
    • Rock, K.L.1    Gramm, C.2    Rothstein, L.3    Clark, K.4    Stein, R.5    Dick, L.6    Hwang, D.7    Goldberg, A.L.8
  • 48
    • 0033553428 scopus 로고    scopus 로고
    • Evidence for a calpeptin-sensitive protein-tyrosine phosphatase upstream of the small GTPase Rho. A novel role for the calpain inhibitor calpeptin in the inhibition of protein-tyrosine phosphatases
    • Schoenwaelder SM, Burridge K. Evidence for a calpeptin-sensitive protein-tyrosine phosphatase upstream of the small GTPase Rho. A novel role for the calpain inhibitor calpeptin in the inhibition of protein-tyrosine phosphatases. J Biol Chem 1999; 274:14359-67.
    • (1999) J Biol Chem , vol.274 , pp. 14359-14367
    • Schoenwaelder, S.M.1    Burridge, K.2
  • 49
    • 0031770307 scopus 로고    scopus 로고
    • Calpain involvement in calphostin C-induced apoptosis
    • DOI 10.1016/S0006-2952(98)00169-5, PII S0006295298001695
    • Spinedi A, Oliverio S, Di Sano F, Piacentini M. Calpain involvement in calphostin C-induced apoptosis. Biochem Pharmacol 1998; 56:1489-92. (Pubitemid 28529427)
    • (1998) Biochemical Pharmacology , vol.56 , Issue.11 , pp. 1489-1492
    • Spinedi, A.1    Oliverio, S.2    Di, S.F.3    Piacentini, M.4
  • 50
    • 0024473080 scopus 로고
    • 2+ on binding of the calpains to calpastatin
    • Kapprell HP, Goll DE. Effect of Ca2+ on binding of the calpains to calpastatin. J Biol Chem 1989; 264:17888-96. (Pubitemid 19279255)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.30 , pp. 17888-17896
    • Kapprell, H.-P.1    Goll, D.E.2
  • 51
    • 0026458245 scopus 로고
    • A comparison of the intracellular distribution of mu-calpain, m- calpain, and calpastatin in proliferating human A431 cells
    • Lane RD, Allan DM, Mellgren RL. A comparison of the intracellular distribution of mu-calpain, m- calpain, and calpastatin in proliferating human A431 cells. Exp Cell Res 1992; 203:5-16.
    • (1992) Exp Cell Res , vol.203 , pp. 5-16
    • Lane, R.D.1    Allan, D.M.2    Mellgren, R.L.3
  • 53
    • 0027397094 scopus 로고
    • A protein kinase inhibitor, staurosporine, enhances the expression of phorbol dibutyrate binding sites in human polymorphonuclear leucocytes
    • Combadiere C, Pedruzzi E, Hakim J, Perianin A. A protein kinase inhibitor, staurosporine, enhances the expression of phorbol dibutyrate binding sites in human polymorphonuclear leucocytes. Biochem J 1993; 289:695-701. (Pubitemid 23074951)
    • (1993) Biochemical Journal , vol.289 , Issue.3 , pp. 695-701
    • Combadiere, C.1    Pedruzzi, E.2    Hakim, J.3    Perianin, A.4
  • 54
    • 0034737736 scopus 로고    scopus 로고
    • Caspase-8 activation and Bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis
    • DOI 10.1074/jbc.275.13.9303
    • Tang D, Lahti JM, Kidd VJ. Caspase-8 activation and bid cleavage contribute to MCF7 cellular execution in a caspase-3-dependent manner during staurosporine-mediated apoptosis. J Biol Chem 2000; 275:9303-7. (Pubitemid 30185152)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.13 , pp. 9303-9307
    • Tang, D.1    Lahti, J.M.2    Kidd, V.J.3
  • 57
    • 0035072535 scopus 로고    scopus 로고
    • Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors
    • DOI 10.1038/sj.cdd.4400808
    • Tenev T, Marani M, McNeish I, Lemoine NR. Pro-caspase-3 overexpression sensitises ovarian cancer cells to proteasome inhibitors. Cell Death Differ 2001; 8:256-264. (Pubitemid 32288171)
    • (2001) Cell Death and Differentiation , vol.8 , Issue.3 , pp. 256-264
    • Tenev, T.1    Marani, M.2    McNeish, I.3    Lemoine, N.R.4
  • 58
    • 0019948262 scopus 로고
    • L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins, B, H and L
    • Barrett AJ, Kembhavi AA, Brown MA, Kirschke H, Knight CG, Tamai M, et al. L-trans-Epoxysuccinyl-leucylamido(4-guanidino)butane (E-64) and its analogues as inhibitors of cysteine proteinases including cathepsins B, H and L. Biochem J 1982; 201:189-98. (Pubitemid 12038477)
    • (1982) Biochemical Journal , vol.201 , Issue.1 , pp. 189-198
    • Barrett, A.J.1    Kembhavi, A.A.2    Brown, M.A.3
  • 59
    • 0032575750 scopus 로고    scopus 로고
    • Caspases: Enemies within
    • Thornberry NA, Lazebnik Y. Caspases: enemies within. Science 1998;281(5381):1312-6. (Pubitemid 28406817)
    • (1998) Science , vol.281 , Issue.5381 , pp. 1312-1316
    • Thornberry, N.A.1    Lazebnik, Y.2
  • 60
    • 0032785021 scopus 로고    scopus 로고
    • Caspase structure, proteolytic substrates, and function during apoptotic cell death
    • Nicholson DW. Caspase structure, proteolytic substrates, and function during apoptotic cell death. Cell Death Differ 1999; 6:1028-42.
    • (1999) Cell Death Differ , vol.6 , pp. 1028-1042
    • Nicholson, D.W.1
  • 61
    • 0035862189 scopus 로고    scopus 로고
    • P53-independent upregulation of KILLER/DR5 TRAIL receptor expression by glucocorticoids and interferon-gamma
    • DOI 10.1006/excr.2000.5073
    • Meng RD, El-Deiry WS. p53-independent upregulation of KILLER/DR5 TRAIL receptor expression by glucocorticoids and interferon-gamma. Exp Cell Res 2001; 262:154-69. (Pubitemid 32980255)
    • (2001) Experimental Cell Research , vol.262 , Issue.2 , pp. 154-169
    • Meng, R.D.1    El-Deiry, W.S.2
  • 63
    • 0033568430 scopus 로고    scopus 로고
    • Implication of calpain in caspase activation during B cell clonal deletion
    • Ruiz-Vela A, Gonzalez de Buitrago G, Martinez AC. Implication of calpain in caspase activation during B cell clonal deletion. Embo J 1999; 18:4988-98.
    • (1999) Embo J , vol.18 , pp. 4988-4998
    • Ruiz-Vela, A.1    Gonzalez De Buitrago, G.2    Martinez, A.C.3
  • 64
    • 0033583313 scopus 로고    scopus 로고
    • Caspase-dependent activation of calpain during drug-induced apoptosis
    • Wood DE, Newcomb EW. Caspase-dependent activation of calpain during drug-induced apoptosis. J Biol Chem 1999; 274:8309-15.
    • (1999) J Biol Chem , vol.274 , pp. 8309-8315
    • Wood, D.E.1    Newcomb, E.W.2
  • 67
    • 0033553481 scopus 로고    scopus 로고
    • Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1
    • Liu X, Zou H, Widlak P, Garrard W, Wang X. Activation of the apoptotic endonuclease DFF40 (caspase-activated DNase or nuclease). Oligomerization and direct interaction with histone H1. J Biol Chem 1999; 274:13836-40.
    • (1999) J Biol Chem , vol.274 , pp. 13836-13840
    • Liu, X.1    Zou, H.2    Widlak, P.3    Garrard, W.4    Wang, X.5
  • 68
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid alpha-spectrin breakdown by calpain and interleukin 1beta-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Nath R, Raser KJ, 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 1996; 319:683-90. (Pubitemid 26386177)
    • (1996) Biochemical Journal , vol.319 , Issue.3 , 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.-W.8    Gilbertsen, R.B.9    Wang, K.K.W.10
  • 69
    • 0032493743 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis
    • DOI 10.1074/jbc.273.32.19993
    • McGinnis KM, Whitton MM, Gnegy ME, Wang KK. Calcium/calmodulin-dependent protein kinase IV is cleaved by caspase-3 and calpain in SH-SY5Y human neuroblastoma cells undergoing apoptosis. J Biol Chem 1998; 273:19993-20000. (Pubitemid 28377549)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.32 , pp. 19993-20000
    • McGinnis, K.M.1    Whitton, M.M.2    Gnegy, M.E.3    Wang, K.K.W.4
  • 70
    • 0022456376 scopus 로고
    • Limited proteolysis of the erythrocyte membrane skeleton by calcium- dependent proteinases
    • Croall DE, Morrow JS, DeMartino GN. Limited proteolysis of the erythrocyte membrane skeleton by calcium- dependent proteinases. Biochim Biophys Acta 1986; 882:287-96.
    • (1986) Biochim Biophys Acta , vol.882 , pp. 287-296
    • Croall, D.E.1    Morrow, J.S.2    DeMartino, G.N.3
  • 71
    • 0023323994 scopus 로고
    • A unique specificity of a calcium activated neutral protease indicated in histone hydrolysis
    • (Tokyo)
    • Sakai K, Akanuma H, Imahori K, Kawashima S. A unique specificity of a calcium activated neutral protease indicated in histone hydrolysis. J Biochem (Tokyo) 1987;101(4):911-8.
    • (1987) J Biochem , vol.101 , Issue.4 , pp. 911-918
    • Sakai, K.1    Akanuma, H.2    Imahori, K.3    Kawashima, S.4
  • 72
  • 73
    • 0019234255 scopus 로고
    • 2+-dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin)
    • 2+-dependent protease (calpain) and its high-molecular-weight endogenous inhibitor (calpastatin). Adv Enzyme Regul 1980; 19:407-24.
    • (1980) Adv Enzyme Regul , vol.19 , pp. 407-424
    • Murachi, T.1    Tanaka, K.2    Hatanaka, M.3    Murakami, T.4
  • 75
    • 0021639220 scopus 로고
    • Calcium-dependent proteinases and specific inhibitors: Calpain and calpastatin
    • Murachi T. Calcium-dependent proteinases and specific inhibitors: calpain and calpastatin. Biochem Soc Symp 1984; 49:149-67. (Pubitemid 15174605)
    • (1984) Biochemical Society Symposia , vol.NO. 49 , pp. 149-167
    • Murachi, T.1
  • 76
    • 0024285560 scopus 로고
    • Calpain II involvement in mitosis
    • Schollmeyer JE. Calpain II involvement in mitosis. Science 1988; 240:911-3.
    • (1988) Science , vol.240 , pp. 911-913
    • Schollmeyer, J.E.1
  • 77
    • 0023661249 scopus 로고
    • Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion
    • Beckerle MC, Burridge K, DeMartino GN, Croall DE. Colocalization of calcium-dependent protease II and one of its substrates at sites of cell adhesion. Cell 1987; 51:569-77.
    • (1987) Cell , vol.51 , pp. 569-577
    • Beckerle, M.C.1    Burridge, K.2    DeMartino, G.N.3    Croall, D.E.4
  • 78
    • 0022509727 scopus 로고
    • Immunogold electron-microscopic localisation of calpain I in skeletal muscle of rats
    • Yoshimura N, Murachi T, Heath R, Kay J, Jasani B, Newman GR. Immunogold electron- microscopic localisation of calpain I in skeletal muscle of rats. Cell Tissue Res 1986; 244:265-70. (Pubitemid 16053376)
    • (1986) Cell and Tissue Research , vol.244 , Issue.2 , pp. 265-270
    • Yoshimura, N.1    Murachi, T.2    Heath, R.3
  • 79
    • 0033567878 scopus 로고    scopus 로고
    • 2+-dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts
    • DOI 10.1002/(SICI)1097-4644(19990915)74:4<522::AID-JCB2>3.0.CO;2-I
    • Barnoy S, Zipser Y, Glaser T, Grimberg Y, Kosower NS. Association of calpain (Ca(2+)-dependent thiol protease) with its endogenous inhibitor calpastatin in myoblasts. J Cell Biochem 1999; 74:522-31. (Pubitemid 29372492)
    • (1999) Journal of Cellular Biochemistry , vol.74 , Issue.4 , pp. 522-531
    • Barnoy, S.1    Zipser, Y.2    Glaser, T.3    Grimberg, Y.4    Kosower, N.S.5
  • 80
    • 0028104428 scopus 로고
    • Selective nuclear transport of mu-calpain
    • Mellgren RL, Lu Q. Selective nuclear transport of mu-calpain. Biochem Biophys Res Commun 1994; 204:544-50.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 544-550
    • Mellgren, R.L.1    Lu, Q.2
  • 82
    • 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; 20:4474-81.
    • (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
  • 83


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.