메뉴 건너뛰기




Volumn 11, Issue 2, 2006, Pages 221-233

HAMLET triggers apoptosis but tumor cell death is independent of caspases, Bcl-2 and p53

Author keywords

lactalbumin; HAMLET; p53 and Bcl 2; Programmed cell death

Indexed keywords

ALPHA LACTALBUMIN; CASPASE; ETOPOSIDE; PROTEIN BCL 2; PROTEIN P53;

EID: 33344455153     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10495-006-3607-7     Document Type: Article
Times cited : (64)

References (49)
  • 1
    • 0036910734 scopus 로고    scopus 로고
    • Programmed cell death: Many ways for cells to die decently
    • Jaattela M. Programmed cell death: Many ways for cells to die decently. Ann Med 2002; 34: 480-488.
    • (2002) Ann Med , vol.34 , pp. 480-488
    • Jaattela, M.1
  • 2
    • 0015383455 scopus 로고
    • Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics
    • Kerr JFR, Wyllie AH, Currie AR. Apoptosis: A basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 1972; 26: 239-257.
    • (1972) Br J Cancer , vol.26 , pp. 239-257
    • Kerr, J.F.R.1    Wyllie, A.H.2    Currie, A.R.3
  • 3
    • 0022497852 scopus 로고
    • Genetic control of programmed cell death in the nematode C. elegans
    • Ellis HM, Horvitz HR. Genetic control of programmed cell death in the nematode C. elegans. Cell 1986; 44: 817-829.
    • (1986) Cell , vol.44 , pp. 817-829
    • Ellis, H.M.1    Horvitz, H.R.2
  • 4
    • 0035811496 scopus 로고    scopus 로고
    • Endonuclease G is an apoptotic DNase when released from mitochondria
    • Li LY, Luo X, Wang X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 2001; 412: 95-99.
    • (2001) Nature , vol.412 , pp. 95-99
    • Li, L.Y.1    Luo, X.2    Wang, X.3
  • 6
    • 0034068601 scopus 로고    scopus 로고
    • Mitochondrial control of cell death
    • Kroemer G, Reed JC. Mitochondrial control of cell death. Nat Med 2000; 6: 513-519. 1.
    • (2000) Nat Med , vol.6
    • Kroemer, G.1    Reed, J.C.2
  • 7
    • 0032575752 scopus 로고    scopus 로고
    • Mitochondria and apoptosis
    • Green DR, Reed JC. Mitochondria and apoptosis. Science 1998; 281: 1309-1312.
    • (1998) Science , vol.281 , pp. 1309-1312
    • Green, D.R.1    Reed, J.C.2
  • 8
    • 0033179760 scopus 로고    scopus 로고
    • BCL-2 family members and the mitochondria in apoptosis
    • Gross A, McDonnell JM, Korsmeyer SJ. BCL-2 family members and the mitochondria in apoptosis. Genes Dev 1999; 13: 1899-1911.
    • (1999) Genes Dev , vol.13 , pp. 1899-1911
    • Gross, A.1    McDonnell, J.M.2    Korsmeyer, S.J.3
  • 9
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis [see comments]. Science 1997; 275: 1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 10
    • 0031036872 scopus 로고    scopus 로고
    • Prevention of apoptosis by Bcl-2: Release of cytochrome c from mitochondria blocked
    • Yang J, Liu X, Bhalla K, et al. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked [see comments]. Science 1997; 275: 1129-1132.
    • (1997) Science , vol.275 , pp. 1129-1132
    • Yang, J.1    Liu, X.2    Bhalla, K.3
  • 11
    • 0032472329 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization
    • Bossy-Wetzel E, Newmeyer DD, Green DR. Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD-specific caspase activation and independently of mitochondrial transmembrane depolarization. Embo J 1998; 17: 37-49.
    • (1998) Embo J , vol.17 , pp. 37-49
    • Bossy-Wetzel, E.1    Newmeyer, D.D.2    Green, D.R.3
  • 12
    • 0032877668 scopus 로고    scopus 로고
    • Dysregulation of apoptosis in cancer
    • Reed JC. Dysregulation of apoptosis in cancer. J Clin Oncol 1999; 17: 2941-2953.
    • (1999) J Clin Oncol , vol.17 , pp. 2941-2953
    • Reed, J.C.1
  • 13
    • 7444241537 scopus 로고    scopus 로고
    • Breast cancer cells can evade apoptosis- mediated selective killing by a novel small molecule inhibitor of Bcl-2
    • Real PJ, Cao Y, Wang R, et al. Breast cancer cells can evade apoptosis- mediated selective killing by a novel small molecule inhibitor of Bcl-2. Cancer Res 2004; 64: 7947-7953.
    • (2004) Cancer Res , vol.64 , pp. 7947-7953
    • Real, P.J.1    Cao, Y.2    Wang, R.3
  • 14
    • 0034722884 scopus 로고    scopus 로고
    • Bcl-2 family proteins as targets for anticancer drug design
    • Huang Z. Bcl-2 family proteins as targets for anticancer drug design. Oncogene 2000; 19: 6627-6631.
    • (2000) Oncogene , vol.19 , pp. 6627-6631
    • Huang, Z.1
  • 15
    • 0027235369 scopus 로고
    • Cancer. A death in the life of p53
    • Lane DP. Cancer. A death in the life of p53 [news; comment]. Nature 1993; 362: 786-787.
    • (1993) Nature , vol.362 , pp. 786-787
    • Lane, D.P.1
  • 16
    • 0032984992 scopus 로고    scopus 로고
    • Mechanisms of p53-mediated apoptosis
    • Bates S, Vousden KH. Mechanisms of p53-mediated apoptosis. Cell Mol Life Sci 1999; 55: 28-37.
    • (1999) Cell Mol Life Sci , vol.55 , pp. 28-37
    • Bates, S.1    Vousden, K.H.2
  • 17
    • 0025076728 scopus 로고
    • Frequent mutations in the p53 tumor suppressor gene in human leukemia T-cell lines
    • Cheng J, Haas M. Frequent mutations in the p53 tumor suppressor gene in human leukemia T-cell lines. Mol Cell Biol. 1990; 10: 5502-5509.
    • (1990) Mol Cell Biol , vol.10 , pp. 5502-5509
    • Cheng, J.1    Haas, M.2
  • 18
    • 0027944206 scopus 로고
    • p53 status and the efficacy of cancer therapy in vivo
    • Lowe SW, Bodis S, McClatchey A, et al. p53 status and the efficacy of cancer therapy in vivo. Science 1994; 266: 807-810.
    • (1994) Science , vol.266 , pp. 807-810
    • Lowe, S.W.1    Bodis, S.2    McClatchey, A.3
  • 19
    • 0032853774 scopus 로고    scopus 로고
    • Mutant p53: Gain-of-function oncoproteins and wild-type p53 inactivators
    • Roemer K. Mutant p53: Gain-of-function oncoproteins and wild-type p53 inactivators. Biol Chem 1999; 380: 879-887.
    • (1999) Biol Chem , vol.380 , pp. 879-887
    • Roemer, K.1
  • 20
    • 0037119491 scopus 로고    scopus 로고
    • Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis
    • Robertson JD, Enoksson M, Suomela M, Zhivotovsky B, Orrenius S. Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis. J Biol Chem 2002; 277: 29803-29809.
    • (2002) J Biol Chem , vol.277 , pp. 29803-29809
    • Robertson, J.D.1    Enoksson, M.2    Suomela, M.3    Zhivotovsky, B.4    Orrenius, S.5
  • 21
    • 4344663051 scopus 로고    scopus 로고
    • Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity
    • Robertson JD, Gogvadze V, Kropotov A, et al. Processed caspase-2 can induce mitochondria-mediated apoptosis independently of its enzymatic activity. EMBO Rep 2004; 5: 643-648.
    • (2004) EMBO Rep , vol.5 , pp. 643-648
    • Robertson, J.D.1    Gogvadze, V.2    Kropotov, A.3
  • 22
    • 9644307904 scopus 로고    scopus 로고
    • Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids
    • Enoksson M, Robertson JD, Gogvadze V, et al. Caspase-2 permeabilizes the outer mitochondrial membrane and disrupts the binding of cytochrome c to anionic phospholipids. J Biol Chem 2004.
    • (2004) J Biol Chem
    • Enoksson, M.1    Robertson, J.D.2    Gogvadze, V.3
  • 23
    • 0036128899 scopus 로고    scopus 로고
    • Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
    • Bykov VJ, Issaeva N, Shilov A, et al. Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound. Nat Med 2002; 8: 282-288.
    • (2002) Nat Med , vol.8 , pp. 282-288
    • Bykov, V.J.1    Issaeva, N.2    Shilov, A.3
  • 25
    • 1542405871 scopus 로고    scopus 로고
    • Human alpha-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival
    • Fischer W, Gustafsson L, Mossberg AK, et al. Human alpha-lactalbumin made lethal to tumor cells (HAMLET) kills human glioblastoma cells in brain xenografts by an apoptosis-like mechanism and prolongs survival. Cancer Res 2004; 64: 2105-2112.
    • (2004) Cancer Res , vol.64 , pp. 2105-2112
    • Fischer, W.1    Gustafsson, L.2    Mossberg, A.K.3
  • 27
  • 30
    • 0028356434 scopus 로고
    • Adenovirus infection enhances in vitro adherence of Streptococcus pneumoniae
    • Håkansson A, Kidd A, Wadell G, Sabharwal H, Svanborg C. Adenovirus infection enhances in vitro adherence of Streptococcus pneumoniae. Infect Immun 1994; 62: 2707-2714.
    • (1994) Infect Immun , vol.62 , pp. 2707-2714
    • Håkansson, A.1    Kidd, A.2    Wadell, G.3    Sabharwal, H.4    Svanborg, C.5
  • 32
    • 8944230656 scopus 로고    scopus 로고
    • Fas-induced activation of the cell death-related protease CPP32 Is inhibited by Bcl-2 and by ICE family protease inhibitors
    • Armstrong RC, Aja T, Xiang J, et al. Fas-induced activation of the cell death-related protease CPP32 Is inhibited by Bcl-2 and by ICE family protease inhibitors. J Biol Chem 1996; 271: 16850-16855.
    • (1996) J Biol Chem , vol.271 , pp. 16850-16855
    • Armstrong, R.C.1    Aja, T.2    Xiang, J.3
  • 33
    • 0027282044 scopus 로고
    • bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
    • Boise LH, Gonzalez-Garcia M, Postema CE, et al. bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death. Cell 1993; 74: 597-608.
    • (1993) Cell , vol.74 , pp. 597-608
    • Boise, L.H.1    Gonzalez-Garcia, M.2    Postema, C.E.3
  • 34
    • 0037063173 scopus 로고    scopus 로고
    • Novel gain of function activity of p53 mutants: Activation of the dUTPase gene expression leading to resistance to 5-fluorouracil
    • Pugacheva EN, Ivanov AV, Kravchenko JE, et al. Novel gain of function activity of p53 mutants: activation of the dUTPase gene expression leading to resistance to 5-fluorouracil. Oncogene 2002; 21: 4595-4600.
    • (2002) Oncogene , vol.21 , pp. 4595-4600
    • Pugacheva, E.N.1    Ivanov, A.V.2    Kravchenko, J.E.3
  • 35
    • 0032553485 scopus 로고    scopus 로고
    • Requirement for p53 and p21 to sustain G2 arrest after DNA damage
    • Bunz F, Dutriaux A, Lengauer C, et al. Requirement for p53 and p21 to sustain G2 arrest after DNA damage. Science 1998; 282: 1497-1501.
    • (1998) Science , vol.282 , pp. 1497-1501
    • Bunz, F.1    Dutriaux, A.2    Lengauer, C.3
  • 36
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • Nicholson DW, Ali A, Thornberry NA, 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
  • 37
    • 0037584357 scopus 로고    scopus 로고
    • Multimeric alpha-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei
    • Håkansson A, Andreasson J, Zhivotovsky B, et al. Multimeric alpha-lactalbumin from human milk induces apoptosis through a direct effect on cell nuclei. Exp Cell Res 1999; 246: 451-460.
    • (1999) Exp Cell Res , vol.246 , pp. 451-460
    • Håkansson, A.1    Andreasson, J.2    Zhivotovsky, B.3
  • 38
    • 0035954427 scopus 로고    scopus 로고
    • Kinetics of core histones in living human cells: Little exchange of H3 and H4 and some rapid exchange of H2B
    • Kimura H, Cook PR. Kinetics of core histones in living human cells: little exchange of H3 and H4 and some rapid exchange of H2B. J Cell Biol 2001; 153: 1341-1353.
    • (2001) J Cell Biol , vol.153 , pp. 1341-1353
    • Kimura, H.1    Cook, P.R.2
  • 39
    • 0033552948 scopus 로고    scopus 로고
    • Mutant p53 gain of function: Differential effects of different p53 mutants on resistance of cultured cells to chemotherapy
    • Blandino G, Levine AJ, Oren M. Mutant p53 gain of function: Differential effects of different p53 mutants on resistance of cultured cells to chemotherapy. Oncogene 1999; 18: 477-485.
    • (1999) Oncogene , vol.18 , pp. 477-485
    • Blandino, G.1    Levine, A.J.2    Oren, M.3
  • 40
    • 0035433420 scopus 로고    scopus 로고
    • Four deaths and a funeral: From caspases to alternative mechanisms
    • Leist M, Jaattela M. Four deaths and a funeral: From caspases to alternative mechanisms. Nat Rev Mol Cell Biol 2001; 2: 589-598.
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 589-598
    • Leist, M.1    Jaattela, M.2
  • 41
    • 0038731167 scopus 로고    scopus 로고
    • Caspase-independent cell death in T lymphocytes
    • Jaattela M, Tschopp J. Caspase-independent cell death in T lymphocytes. Nat Immunol 2003; 4: 416-423.
    • (2003) Nat Immunol , vol.4 , pp. 416-423
    • Jaattela, M.1    Tschopp, J.2
  • 42
    • 0035160316 scopus 로고    scopus 로고
    • A folding variant of human alpha-lactalbumin induces mitochondrial permeability transition in isolated mitochondria
    • Kohler C, Gogvadze V, Hakansson A, et al. A folding variant of human alpha-lactalbumin induces mitochondrial permeability transition in isolated mitochondria. Eur J Biochem 2001; 268: 186-191.
    • (2001) Eur J Biochem , vol.268 , pp. 186-191
    • Kohler, C.1    Gogvadze, V.2    Hakansson, A.3
  • 43
    • 15244342640 scopus 로고    scopus 로고
    • A novel celecoxib derivative, OSU03012, induces cytotoxicity in primary CLL cells and transformed B-cell lymphoma cell line via a caspase- and Bcl-2-independent mechanism
    • Johnson AJ, Smith LL, Zhu J, et al. A novel celecoxib derivative, OSU03012, induces cytotoxicity in primary CLL cells and transformed B-cell lymphoma cell line via a caspase- and Bcl-2-independent mechanism. Blood 2005; 105: 2504-2509.
    • (2005) Blood , vol.105 , pp. 2504-2509
    • Johnson, A.J.1    Smith, L.L.2    Zhu, J.3
  • 44
    • 0041703017 scopus 로고    scopus 로고
    • Celecoxib activates a novel mitochondrial apoptosis signaling pathway
    • Jendrossek V, Handrick R, Belka C. Celecoxib activates a novel mitochondrial apoptosis signaling pathway. Faseb J 2003; 17: 1547-1549.
    • (2003) Faseb J , vol.17 , pp. 1547-1549
    • Jendrossek, V.1    Handrick, R.2    Belka, C.3
  • 45
    • 0034726959 scopus 로고    scopus 로고
    • The c-Myc-interacting adaptor protein Bin1 activates a caspase-independent cell death program
    • Elliott K, Ge K, Du W, Prendergast GC. The c-Myc-interacting adaptor protein Bin1 activates a caspase-independent cell death program. Oncogene 2000; 19: 4669-4684.
    • (2000) Oncogene , vol.19 , pp. 4669-4684
    • Elliott, K.1    Ge, K.2    Du, W.3    Prendergast, G.C.4
  • 46
    • 0033118229 scopus 로고    scopus 로고
    • Oncogenic Ras triggers cell suicide through the activation of a caspase-independent cell death program in human cancer cells
    • Chi S, Kitanaka C, Noguchi K, et al. Oncogenic Ras triggers cell suicide through the activation of a caspase-independent cell death program in human cancer cells. Oncogene 1999; 18: 2281-2290.
    • (1999) Oncogene , vol.18 , pp. 2281-2290
    • Chi, S.1    Kitanaka, C.2    Noguchi, K.3
  • 47
    • 0035206962 scopus 로고    scopus 로고
    • Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1
    • Yamaki M, Umehara T, Chimura T, Horikoshi M. Cell death with predominant apoptotic features in Saccharomyces cerevisiae mediated by deletion of the histone chaperone ASF1/CIA1. Genes Cells 2001; 6: 1043-1054.
    • (2001) Genes Cells , vol.6 , pp. 1043-1054
    • Yamaki, M.1    Umehara, T.2    Chimura, T.3    Horikoshi, M.4
  • 48
    • 0032513291 scopus 로고    scopus 로고
    • Defects in the ubiquitin pathway induce caspase-independent apoptosis blocked by Bcl-2
    • Monney L, Otter I, Olivier R, et al. Defects in the ubiquitin pathway induce caspase-independent apoptosis blocked by Bcl-2. J Biol Chem 1998; 273: 6121-6131.
    • (1998) J Biol Chem , vol.273 , pp. 6121-6131
    • Monney, L.1    Otter, I.2    Olivier, R.3
  • 49
    • 0037163133 scopus 로고    scopus 로고
    • Calcium and calpain as key mediators of apoptosis-like death induced by vitamin D compounds in breast cancer cells
    • Mathiasen IS, Sergeev IN, Bastholm L, et al. Calcium and calpain as key mediators of apoptosis-like death induced by vitamin D compounds in breast cancer cells. J Biol Chem 2002; 277: 30738-30745.
    • (2002) J Biol Chem , vol.277 , pp. 30738-30745
    • Mathiasen, I.S.1    Sergeev, I.N.2    Bastholm, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.