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Volumn 40, Issue 7, 2012, Pages

Induction of apoptosis in Eμ-myc lymphoma cells in vitro and in vivo through calpain inhibition

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CALPAIN 1; CALPAIN 2; CALPASTATIN; CASPASE 3; CASPASE 3 INHIBITOR; CASPASE 7 INHIBITOR; CASPASE 9; CASPASE 9 INHIBITOR; CASPASE INHIBITOR; CYSTEINE PROTEINASE INHIBITOR; ETOPOSIDE; MYC PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE ADENOSINE DIPHOSPHATE RIBOSYLTRANSFERASE; PD 150606; UNCLASSIFIED DRUG; [1 [(1 FORMYL 2 PHENYLETHYL)CARBAMOYL] 2 METHYLPROPYL]CARBAMIC ACID BENZYL ESTER;

EID: 84862798809     PISSN: 0301472X     EISSN: 18732399     Source Type: Journal    
DOI: 10.1016/j.exphem.2012.02.002     Document Type: Article
Times cited : (8)

References (43)
  • 1
    • 0001292985 scopus 로고
    • Translocation of the c-myc gene into the immunoglobulin heavy chain locus in human Burkitt lymphoma and murine plasmacytoma cells
    • Taub R., Kirsch I., Morton C., et al. Translocation of the c-myc gene into the immunoglobulin heavy chain locus in human Burkitt lymphoma and murine plasmacytoma cells. Proc Natl Acad Sci U S A 1982, 79:7837-7841.
    • (1982) Proc Natl Acad Sci U S A , vol.79 , pp. 7837-7841
    • Taub, R.1    Kirsch, I.2    Morton, C.3
  • 2
    • 0022405166 scopus 로고
    • Human growth hormone induces and maintains c-myc gene expression in Nb2 lymphoma cells
    • Fleming W.H., Murphy P.R., Murphy L.J., et al. Human growth hormone induces and maintains c-myc gene expression in Nb2 lymphoma cells. Endocrinology 1985, 117:2547-2549.
    • (1985) Endocrinology , vol.117 , pp. 2547-2549
    • Fleming, W.H.1    Murphy, P.R.2    Murphy, L.J.3
  • 3
    • 0027222780 scopus 로고
    • Myeloblastic leukemia cells conditionally blocked by myc-estrogen receptor chimeric transgenes for terminal differentiation coupled to growth arrest and apoptosis
    • Selvakumaran M., Liebermann D., Hoffman-Liebermann B. Myeloblastic leukemia cells conditionally blocked by myc-estrogen receptor chimeric transgenes for terminal differentiation coupled to growth arrest and apoptosis. Blood 1993, 81:2257-2262.
    • (1993) Blood , vol.81 , pp. 2257-2262
    • Selvakumaran, M.1    Liebermann, D.2    Hoffman-Liebermann, B.3
  • 4
    • 0029040537 scopus 로고
    • Apoptosis induced by c-myc overexpression is dependent on growth conditions
    • Gibson A.W., Cheng T., Johnston R.N. Apoptosis induced by c-myc overexpression is dependent on growth conditions. Exp Cell Res 1995, 218:351-358.
    • (1995) Exp Cell Res , vol.218 , pp. 351-358
    • Gibson, A.W.1    Cheng, T.2    Johnston, R.N.3
  • 6
    • 0032905924 scopus 로고    scopus 로고
    • C-Myc target genes involved in cell growth, apoptosis, and metabolism
    • Dang C.V. c-Myc target genes involved in cell growth, apoptosis, and metabolism. Mol Cell Biol 1999, 19:1-11.
    • (1999) Mol Cell Biol , vol.19 , pp. 1-11
    • Dang, C.V.1
  • 8
    • 0022380768 scopus 로고
    • The c-myc oncogene driven by immunoglobulin enhancers induces lymphoid malignancy in transgenic mice
    • Adams J.M., Harris A.W., Pinkert C.A., et al. The c-myc oncogene driven by immunoglobulin enhancers induces lymphoid malignancy in transgenic mice. Nature 1985, 318:533-538.
    • (1985) Nature , vol.318 , pp. 533-538
    • Adams, J.M.1    Harris, A.W.2    Pinkert, C.A.3
  • 9
    • 0024809147 scopus 로고
    • Oncogene cooperation and B-lymphoid tumorigenesis in Emu-myc transgenic mice
    • Alexander W.S., Bernard O., Langdon W.Y., et al. Oncogene cooperation and B-lymphoid tumorigenesis in Emu-myc transgenic mice. Haematol Blood Transfus 1989, 32:423-427.
    • (1989) Haematol Blood Transfus , vol.32 , pp. 423-427
    • Alexander, W.S.1    Bernard, O.2    Langdon, W.Y.3
  • 10
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • Huang Y., Wang K.K. The calpain family and human disease. Trends Mol Med 2001, 7:355-362.
    • (2001) Trends Mol Med , vol.7 , pp. 355-362
    • Huang, Y.1    Wang, K.K.2
  • 12
    • 0022391544 scopus 로고
    • Age-related changes of calpain II and alpha-crystallin in the lens of hereditary cataract (Nakano) mouse
    • Yoshida H., Murachi T., Tsukahara I. Age-related changes of calpain II and alpha-crystallin in the lens of hereditary cataract (Nakano) mouse. Curr Eye Res 1985, 4:983-988.
    • (1985) Curr Eye Res , vol.4 , pp. 983-988
    • Yoshida, H.1    Murachi, T.2    Tsukahara, I.3
  • 13
    • 0025157879 scopus 로고
    • Calpain and calpastatin in normal and Alzheimer-degenerated human brain tissue
    • Nilssone E., Alafuzoff I., Blennow K., et al. Calpain and calpastatin in normal and Alzheimer-degenerated human brain tissue. Neurobiol Aging 1990, 11:425-431.
    • (1990) Neurobiol Aging , vol.11 , pp. 425-431
    • Nilssone, E.1    Alafuzoff, I.2    Blennow, K.3
  • 14
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard I., Broux O., Allamand V., et al. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 1995, 81:27-40.
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3
  • 15
    • 0033772073 scopus 로고    scopus 로고
    • Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus
    • Horikawa Y., Oda N., Cox N.J., et al. Genetic variation in the gene encoding calpain-10 is associated with type 2 diabetes mellitus. Nat Genet 2000, 26:163-175.
    • (2000) Nat Genet , vol.26 , pp. 163-175
    • Horikawa, Y.1    Oda, N.2    Cox, N.J.3
  • 16
    • 0034079985 scopus 로고    scopus 로고
    • Isolation of two novel genes, down-regulated in gastric cancer
    • Yoshikawa Y., Mukai H., Hino F., Asada K., Kato I. Isolation of two novel genes, down-regulated in gastric cancer. Jpn J Cancer Res 2000, 91:459-463.
    • (2000) Jpn J Cancer Res , vol.91 , pp. 459-463
    • Yoshikawa, Y.1    Mukai, H.2    Hino, F.3    Asada, K.4    Kato, I.5
  • 18
    • 0031569532 scopus 로고    scopus 로고
    • Calpain, an upstream regulator of thymocyte apoptosis
    • Squier M.K., Cohen J.J. Calpain, an upstream regulator of thymocyte apoptosis. J Immunol 1997, 158:3690-3697.
    • (1997) J Immunol , vol.158 , pp. 3690-3697
    • Squier, M.K.1    Cohen, J.J.2
  • 19
    • 0032961233 scopus 로고    scopus 로고
    • Calpain and calpastatin regulate neutrophil apoptosis
    • Squier M.K., Sehnert A.J., Sellins K.S., et al. Calpain and calpastatin regulate neutrophil apoptosis. J Cell Physiol 1999, 178:311-319.
    • (1999) J Cell Physiol , vol.178 , pp. 311-319
    • Squier, M.K.1    Sehnert, A.J.2    Sellins, K.S.3
  • 20
    • 1542397842 scopus 로고    scopus 로고
    • Apoptosis induced by simvastatin in rat vascular smooth muscle cell through Ca2+-calpain and caspase-3 dependent pathway
    • Cheng G., Shan J., Xu G., et al. Apoptosis induced by simvastatin in rat vascular smooth muscle cell through Ca2+-calpain and caspase-3 dependent pathway. Pharmacol Res 2003, 48:571-578.
    • (2003) Pharmacol Res , vol.48 , pp. 571-578
    • Cheng, G.1    Shan, J.2    Xu, G.3
  • 21
    • 42149164851 scopus 로고    scopus 로고
    • Calpain-mediated pathway dominates cisplatin-induced apoptosis in human lung adenocarcinoma cells as determined by real-time single cell analysis
    • Liu L., Xing D., Chen W.R., et al. Calpain-mediated pathway dominates cisplatin-induced apoptosis in human lung adenocarcinoma cells as determined by real-time single cell analysis. Int J Cancer 2008, 122:2210-2222.
    • (2008) Int J Cancer , vol.122 , pp. 2210-2222
    • Liu, L.1    Xing, D.2    Chen, W.R.3
  • 22
    • 0030270612 scopus 로고    scopus 로고
    • Calpain inhibitors and serine protease inhibitors can produce apoptosis in HL-60 cells
    • Lu Q., Mellgren R.L. Calpain inhibitors and serine protease inhibitors can produce apoptosis in HL-60 cells. Arch Biochem Biophys 1996, 334:175-181.
    • (1996) Arch Biochem Biophys , vol.334 , pp. 175-181
    • Lu, Q.1    Mellgren, R.L.2
  • 23
    • 0034130450 scopus 로고    scopus 로고
    • Calpain inhibitor II induces caspase-dependent apoptosis in human acute lymphoblastic leukemia and non-Hodgkin's lymphoma cells as well as some solid tumor cells
    • Zhu D.M., Uckun F.M. Calpain inhibitor II induces caspase-dependent apoptosis in human acute lymphoblastic leukemia and non-Hodgkin's lymphoma cells as well as some solid tumor cells. Clin Cancer Res 2000, 6:2456-2463.
    • (2000) Clin Cancer Res , vol.6 , pp. 2456-2463
    • Zhu, D.M.1    Uckun, F.M.2
  • 25
    • 33747877520 scopus 로고    scopus 로고
    • Combined effect of proteasome and calpain inhibition on cisplatin-resistant human melanoma cells
    • Mlynarczuk-Bialy I., Roeckmann H., Kuckelkorn U., et al. Combined effect of proteasome and calpain inhibition on cisplatin-resistant human melanoma cells. Cancer Res 2006, 66:7598-7605.
    • (2006) Cancer Res , vol.66 , pp. 7598-7605
    • Mlynarczuk-Bialy, I.1    Roeckmann, H.2    Kuckelkorn, U.3
  • 26
    • 44949172396 scopus 로고    scopus 로고
    • Apoptosis-suppressing and autophagy-promoting effects of calpain on oridonin-induced L929 cell death
    • Cheng Y., Qiu F., Huang J., Tashiro S., Onodera S., Ikejima T. Apoptosis-suppressing and autophagy-promoting effects of calpain on oridonin-induced L929 cell death. Arch Biochem Biophys 2008, 475:148-155.
    • (2008) Arch Biochem Biophys , vol.475 , pp. 148-155
    • Cheng, Y.1    Qiu, F.2    Huang, J.3    Tashiro, S.4    Onodera, S.5    Ikejima, T.6
  • 27
    • 52049113458 scopus 로고    scopus 로고
    • Regulation of calpain activity by c-Myc through calpastatin and promotion of transformation in c-Myc-negative cells by calpastatin suppression
    • Niapour M., Yu Y., Berger S.A. Regulation of calpain activity by c-Myc through calpastatin and promotion of transformation in c-Myc-negative cells by calpastatin suppression. J Biol Chem 2008, 283:21371-21381.
    • (2008) J Biol Chem , vol.283 , pp. 21371-21381
    • Niapour, M.1    Yu, Y.2    Berger, S.A.3
  • 28
    • 59649101299 scopus 로고    scopus 로고
    • Calpain small-1 modulates Akt/FoxO3A signaling and apoptosis through PP2A
    • Bertoli C., Copetti T., Lam E.W., Demarchi F., Schneider C. Calpain small-1 modulates Akt/FoxO3A signaling and apoptosis through PP2A. Oncogene 2009, 28:721-733.
    • (2009) Oncogene , vol.28 , pp. 721-733
    • Bertoli, C.1    Copetti, T.2    Lam, E.W.3    Demarchi, F.4    Schneider, C.5
  • 29
    • 1642349839 scopus 로고    scopus 로고
    • Calpain activity is generally elevated during transformation but has oncogene-specific biological functions
    • Carragher N.O., Fonseca B.D., Frame M.C. Calpain activity is generally elevated during transformation but has oncogene-specific biological functions. Neoplasia 2004, 6:53-73.
    • (2004) Neoplasia , vol.6 , pp. 53-73
    • Carragher, N.O.1    Fonseca, B.D.2    Frame, M.C.3
  • 30
    • 49149108257 scopus 로고    scopus 로고
    • AID and RAG1 do not contribute to lymphomagenesis in Emu c-myc transgenic mice
    • Nepal R.M., Zaheen A., Basit W., Li L., Berger S.A., Martin A. AID and RAG1 do not contribute to lymphomagenesis in Emu c-myc transgenic mice. Oncogene 2008, 27:4752-4756.
    • (2008) Oncogene , vol.27 , pp. 4752-4756
    • Nepal, R.M.1    Zaheen, A.2    Basit, W.3    Li, L.4    Berger, S.A.5    Martin, A.6
  • 31
    • 34447115066 scopus 로고    scopus 로고
    • Flow cytometric measurement of calpain activity in living cells
    • Niapour M., Berger S. Flow cytometric measurement of calpain activity in living cells. Cytometry A 2007, 71:475-485.
    • (2007) Cytometry A , vol.71 , pp. 475-485
    • Niapour, M.1    Berger, S.2
  • 32
    • 80055102740 scopus 로고    scopus 로고
    • Measuring calpain activity in fixed and living cells by flow cytometry
    • Farr C., Berger S. Measuring calpain activity in fixed and living cells by flow cytometry. J Vis Exp 2010, 8(41).
    • (2010) J Vis Exp , vol.8 , Issue.41
    • Farr, C.1    Berger, S.2
  • 33
    • 0029987453 scopus 로고    scopus 로고
    • An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective
    • Wang K.K., Nath R., Posner A., et al. An alpha-mercaptoacrylic acid derivative is a selective nonpeptide cell-permeable calpain inhibitor and is neuroprotective. Proc Natl Acad Sci U S A 1996, 93:6687-6692.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 6687-6692
    • Wang, K.K.1    Nath, R.2    Posner, A.3
  • 34
    • 0022000391 scopus 로고
    • Elimination of malignant clonogenic cells from human bone marrow using multiple monoclonal antibodies and complement
    • Bast R.C.J., De Fabritiis P., Lipton J., et al. Elimination of malignant clonogenic cells from human bone marrow using multiple monoclonal antibodies and complement. Cancer Res 1985, 45:499-503.
    • (1985) Cancer Res , vol.45 , pp. 499-503
    • Bast, R.C.J.1    De Fabritiis, P.2    Lipton, J.3
  • 35
    • 0029894733 scopus 로고    scopus 로고
    • Alpha-mercaptoacrylic acid derivatives as novel selective calpain inhibitors
    • Wang K.K., Posner A., Raser K.J., et al. Alpha-mercaptoacrylic acid derivatives as novel selective calpain inhibitors. Adv Exp Med Biol 1996, 389:95-101.
    • (1996) Adv Exp Med Biol , vol.389 , pp. 95-101
    • Wang, K.K.1    Posner, A.2    Raser, K.J.3
  • 36
    • 77949268266 scopus 로고    scopus 로고
    • Cellular responses to etoposide: cell death despite cell cycle arrest and repair of DNA damage
    • Schonn I., Hennesen J., Dartsch D.C. Cellular responses to etoposide: cell death despite cell cycle arrest and repair of DNA damage. Apoptosis 2010, 15:162-172.
    • (2010) Apoptosis , vol.15 , pp. 162-172
    • Schonn, I.1    Hennesen, J.2    Dartsch, D.C.3
  • 37
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson D.W., Ali A., Thornberry N.A., et al. Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis. Nature 1995, 376:37-43.
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1    Ali, A.2    Thornberry, N.A.3
  • 38
    • 14344272939 scopus 로고    scopus 로고
    • Maintenance of caspase-3 proenzyme dormancy by an intrinsic "safety catch" regulatory tripeptide
    • Roy S., Bayly C.I., Gareau Y., et al. Maintenance of caspase-3 proenzyme dormancy by an intrinsic "safety catch" regulatory tripeptide. Proc Natl Acad Sci U S A 2001, 98:6132-6137.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 6132-6137
    • Roy, S.1    Bayly, C.I.2    Gareau, Y.3
  • 39
    • 33845891045 scopus 로고    scopus 로고
    • Aspartic protease and caspase 3/7 activation are central for macrophage apoptosis following infection with Escherichia coli
    • Albee L., Shi B., Perlman H. Aspartic protease and caspase 3/7 activation are central for macrophage apoptosis following infection with Escherichia coli. J Leukoc Biol 2007, 81:229-237.
    • (2007) J Leukoc Biol , vol.81 , pp. 229-237
    • Albee, L.1    Shi, B.2    Perlman, H.3
  • 40
    • 0030976895 scopus 로고    scopus 로고
    • A sequential two-step mechanism for the production of the mature p17:p12 form of caspase-3 in vitro
    • Han Z., Hendrickson E.A., Bremner T.A., Wyche J.H. A sequential two-step mechanism for the production of the mature p17:p12 form of caspase-3 in vitro. J Biol Chem 1997, 272:13432-13436.
    • (1997) J Biol Chem , vol.272 , pp. 13432-13436
    • Han, Z.1    Hendrickson, E.A.2    Bremner, T.A.3    Wyche, J.H.4
  • 42
    • 0034086332 scopus 로고    scopus 로고
    • Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines
    • Atencio I.A., Ramachandra M., Shabram P., Demers G.W. Calpain inhibitor 1 activates p53-dependent apoptosis in tumor cell lines. Cell Growth Differ 2000, 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
  • 43
    • 34250788040 scopus 로고    scopus 로고
    • Bone marrow stromal cells prevent apoptosis of lymphoma cells by upregulation of anti-apoptotic proteins associated with activation of NF-kappaB (RelB/p52) in non-Hodgkin's lymphoma cells
    • Lwin T., Hazlehurst L.A., Li Z., et al. Bone marrow stromal cells prevent apoptosis of lymphoma cells by upregulation of anti-apoptotic proteins associated with activation of NF-kappaB (RelB/p52) in non-Hodgkin's lymphoma cells. Leukemia 2007, 21:1521-1531.
    • (2007) Leukemia , vol.21 , pp. 1521-1531
    • Lwin, T.1    Hazlehurst, L.A.2    Li, Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.