Apoptosis Regulators

Reviews in Clinical and Experimental Hematology

Volumn 7, Issue 2, 2003, Pages 117-138

  Harada, Hisashi ^a   Grant, Steven ^a  

^a VIRGINIA COMMONWEALTH UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

2 AMINO 6 BROMO 4 (1 CYANO 2 ETHOXY 2 OXOETHYL) 4H CHROMENE 3 CARBOXYLIC ACID ETHYL ESTER; 7 HYDROXYSTAUROSPORINE; BORTEZIMIB; BORTEZOMIB; CASPASE; CASPASE 8; CYCLIN D1; CYTOCHROME C; CYTOTOXIC AGENT; FLAVOPIRIDOL; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE KINASE; MYC PROTEIN; OBLIMERSEN; PROTEASOME INHIBITOR; PROTEIN BCL 2; PROTEIN BID; PROTEIN INHIBITOR; PROTEIN KINASE; PROTEIN KINASE B; PROTEIN P21; PROTEIN P27; RETINOIC ACID; STAUROSPORINE DERIVATIVE; TAXANE DERIVATIVE; UNCLASSIFIED DRUG;

ACUTE LEUKEMIA; APOPTOSIS; BREAST CANCER; CANCER CELL; CANCER CELL DESTRUCTION; CHRONIC LYMPHATIC LEUKEMIA; CLINICAL TRIAL; CYTOSOL; DOWN REGULATION; DRUG EFFECT; ENZYME ACTIVATION; HUMAN; MITOCHONDRIAL MEMBRANE; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; APOPTOSIS; CELL CYCLE PROTEINS; HEMATOLOGIC NEOPLASMS; HUMANS; MITOCHONDRIA; PROTO-ONCOGENE PROTEINS; SIGNAL TRANSDUCTION;

EID: 0345276617     PISSN: 11270020     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (184)

1. Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer, 26: 239-257, 1972.
2. Thompson CB. Apoptosis in the pathogenesis and treatment of disease. Science, 267: 1456-1462, 1995.
3. Bedi A, Barber JP, Bedi GC, et al. BCR-ABL-mediated inhibition of apoptosis with delay of G2/M transition after DNA damage: a mechanism of resistance to multiple anticancer agents. Blood, 86: 1148-1158, 1995.
4. Reed JC. Apoptosis-based therapies. Nat Rev Drug Discov, 1: 111-121, 2002.
5. Brown JM and Wouters BG. Apoptosis, p53, and tumor cell sensitivity to anticancer agents. Cancer Res, 59: 1391-1399, 1999.
6. Gross A, McDonnell JM, Korsmeyer SJ. BCL-2 family members and the mitochondria in apoptosis. Genes Dev, 13: 1899-1911, 1999.
7. Vander Heiden MG and Thompson CB. BCL-2 proteins: regulators of apoptosis or of mitochondrial homeostasis? Nat Cell Biol, 1: E209-E216, 1999.
8. Green DR and Reed JC. Mitochondria and apoptosis. Science, 281: 1309-1311, 1998.
9. Adams JM and Cory S. Life-or-death decisions by the BCL-2 protein family. Trends Biochem Sci, 26: 61-66, 2001.
10. Muchmore SW, Sattler M, Liang H, et al. X-ray and NMR structure of human BCL-xL, an inhibitor of programmed cell death. Nature, 381: 335-341, 1996.
11. Sattler M, Liang H, Nettesheim D, et al. Structure of BCL-xL-BAK peptide complex: recognition between regulators of apoptosis. Science, 275: 983-986, 1997.
12. Suzuki M, Youle RJ, Tjandra N, et al. Structure of BAX: coregulation of dimer formation and intracellular localization. Cell, 103: 645-654, 2000.
13. Veis DJ, Sorenson CM, Shutter JR, et al. BCL-2-deficient mice demonstrate fulminant lymphoid apoptosis, polycystic kidneys, and hypopigmented hair. Cell, 75: 229-240, 1993.
14. Nakayama K, Nakayama K, Negishi I, et al. Targeted disruption of BCL-2 alpha beta in mice: occurrence of gray hair, polycystic kidney disease, and lymphocytopenia. Proc Natl Acad Sci USA, 91: 3700-3704, 1994.
15. Motoyama N, Wang F, Roth KA, et al. Massive cell death of immature hematopoietic cells and neurons in BCL-x-deficient mice. Science, 267: 1506-1510, 1995.
16. Rinkenberger JL, Horning S, Klocke B, et al. Mcl-1 deficiency results in peri-implantation embryonic lethality. Genes Dev, 14: 23-27, 2000.
17. Ross AJ, Waymire KG, Moss JE, et al. Testicular degeneration in BCLw-deficient mice. Nat Genet, 18: 251-256, 1998.
18. Print CG, Loveland KL, Gibson L, et al. Apoptosis regulator bcl-w is essential for spermatogenesis but appears otherwise redundant. Proc Natl Acad Sci USA, 95: 12424-12431, 1998.
19. Hamasaki A, Sendo F, Nakaymna K, et al. Accelerated neutrophil apoptosis in mice lacking A1-a, a subtype of the bcl-2-related A1 gene. J Exp Med, 188: 1985-1992, 1998.
20. Xiang Z, Ahmed AA, Moller C, et al. Essential role of the prosurvival bcl-2 homologue A1 in mast cell survival after allergic activation. J Exp Med 194: 1561-1569, 2001.
21. Kelekar A and Thompson CB. BCL-2-famfly proteins: the role of the BH3 domain in apoptosis. Trends Cell Biol, 8: 324-330, 1998.
22. Puthalakath H and Strasser A. Keeping killers on a tight leash: transcriptional and post-translational control of the pro-apoptotic activity of BH3-only proteins. Cell Deatb Differ, 9: 505-512, 2002.
23. Conradt B and Horvitz HR. The TRA-1A sex determination protein of C. elegans regulates sexually dimorphic cell deaths by repressing the egl-1 cell death activator gene. Cell, 98: 317-327, 1999.
24. Metzstein MM and Horvitz HR. The C. elegans cell death specification gene ces-1 encodes a snail family zinc finger protein. Mol Cell, 4: 309-319, 1999.
25. Oda E, Ohki R, Murasawa H, et al. Noxa, a BH3-only member of the BCL-2 family and candidate mediator of p53-induced apoptosis. Science, 288: 1053-1058, 2000.
26. Yu J, Zhang L, Hwang PM, et al. PUMA induces the rapid apoptosis of colorectal cancer cells. Mol Cell 7: 673-682, 2001.
27. Nakano K and Vousden KH. PUMA, a novel proapoptotic gene, is induced by p53. Mol Cell, 7: 683-694, 2001.
28. Dijkers PF, Medema RH, Lammers JW, et al. Expression of the pro-apoptotic BCL-2 family member BIM is regulated by the forkhead transcription factor FKHR-L1. Curr Biol, 10: 1201-1204, 2000.
29. Putcha GV, Moulder KL, Golden JP, et al. Induction of BIM, a proapoptotic BH3-only BCL-2 family member, is critical for neuronal apoptosis. Neuron, 29: 615-628, 2001.
30. Shinjyo T, Kuribara R, Inukai T, et al. Down regulation of BIM, a proapoptotic relative of BCL-2 is a pivotal step in cytokine-initiated survival signaling in murine hematopoietic progenitors. Mol Cell Biol 21: 854-864, 2001.
31. Whitfield J, Neame SJ, Paquet L, et al. Dominant-negative c-Jun promotes neuronal survival by reducing BIM expression and inhibiting mitochondrial cytochrome C release. Neuron, 29: 629-643, 2001.
32. Inohara N, Ding L, Chen S, et al. Harakiri, a novel regulator of cell death, encodes a protein that activates apoptosis and interacts selectively with survival-promoting proteins BCL-2 and BCL-X(L). EMBO J, 16: 1686-1694, 1997.
33. Imaizumi K, Tsuda M, Imai Y, et al. Molecular cloning of a novel polypeptide, DP5, induced during programmed neuronal death. J Biol Chem, 272: 18842-18848, 1997.
34. Imaizumi K, Morihara T, Mori Y, et al. The cell death-promoting gene DP5, which interacts with the BCL2 family, is induced during neuronal apoptosis following exposure to amyloid beta protein. J Biol Chem, 274: 7975-7981, 1999.
35. Sanz C, Mellstrom B, Link WA, et al. Interleukin 3-dependent activation of DREAM is involved in transcriptional silencing of the apoptotic Hrk gene in hematopoietic progenitor cells. EMBO J, 20: 2286-2292, 2001.
36. Li H, Zhu H, Xu CJ, et al. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell, 94: 491-501, 1998.
37. Luo X, Budihardjo I, Zou H, et al. BID, a BCL2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell, 94: 481-490, 1998.
38. Barry M, Heibein JA, Pinkoski MJ, et al. Granzyme B short-circuits the need for caspase 8 activity during granule-mediated cytotoxic T-lymphocyte killing by directly cleaving BID. Mol Cell Biol, 20: 3781-3794, 2000.
39. Stoka V, Turk B, Schendel SL, et al. Lysosomal protease pathways to apoptosis. Cleavage of bid, not pro-caspases, is the most likely route. J Biol Chem, 276: 3149-3157, 2001.
40. Zha J, Weiler S, Oh KJ, et al. Posttranslational N-myristoylation of BID as a molecular switch for targeting mitochondria and apoptosis. Science, 290: 1761-1765, 2000.
41. Desagher S, Osen-Sand A, Montessuit S, et al. Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8. Mol Cell, 8: 601-611, 2001.
42. Yin XM, Wang K, Gross A, et al. BID-deficient mice are resistant to Fas-induced hepatocellular apoptosis. Nature, 400: 886-891, 1999.
43. Puthalakath H, Huang DC, O'Reilly LA, et al. The proapoptotic activity of the BCL-2 family member BLM is regulated by interaction with the dynein motor complex. Mol Cell, 3: 287-296, 1999.
44. Puthalakath H, Villunger A, O'Reilly LA, et al. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science, 293: 1829-1832, 2001.
45. Zha J, Harada H, Yang E, et al. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L). Cell, 87: 619-628, 1996.
46. Datta SR, Katsov A, Hu L, et al. 14-3-3 proteins and survival kinases cooperate to inactivate BAD by BH3 domain phosphorylation. Mol Cell, 6: 41-51, 2000.
47. Condorelli F, Salomoni P, Cotteret S, et al. Caspase cleavage enhances the apoptosis-inducing effects of BAD. Mol Cell Biol, 21: 3025-3036, 2001.
48. Verma S, Zhao LJ, Chinnadurai G. Phosphorylation of the pro-apoptotic protein BIK: mapping of phosphorylation sites and effect on apoptosis. J Biol Chem, 276: 4671-4676, 2001.
49. Germain M, Mathai JP, Shore GC. BH-3-only BIK functions at the endoplasmic reticulum to stimulate cytochrome c release from mitochondria. J Biol Chem, 277: 18053-18060, 2002.
50. Lindsten TA, Ross J, King A, et al. The combined functions of proapoptotic BCL-2 family members bak and bax are essential for normal development of multiple tissues. Mol Cell, 6: 1389-1399, 2000.
51. Wei MC, Zong WX, Cheng EH, et al. Proapoptotic BAX and BAK: a requisite gateway to mitochondrial dysfunction and death. Science, 292: 727-730, 2001.
52. Zong, WX, Lindsten T, Ross AJ, et al. BH3-only proteins that bind pro-survival BCL-2 family members fail to induce apoptosis in the absence of BAX and BAK. Genes Dev, 15: 1481-1486, 2001.
53. Cheng EH, Wei MC, Weiler S, et al. BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell, 8: 705-711, 2001.
54. Letai A, Bassik MC, Walensky ID, et al. Distinct BH3 domains either sensitize or activate mitochondrial apoptosis, serving as prototype cancer therapeutics. Cancer Cell, 2: 183-192, 2002.
55. Martinou, JC and Green, DR. Breaking the mitochondrial barrier. Nat Rev Mol CeU Biol, 2: 63-67, 2001.
56. Budihardjo I, Oliver H, Lutter M, et al. Biochemical pathways of caspase activation during apoptosis. Annu Rev Cell Dev Biol, 15: 269-290, 1999.
57. M.O. Hengartner, The biochemistry of apoptosis. Nature, 407: 770-776, 2000.
58. Strasser A, O'Connor L, Dixit VM. Apoptosis signaling. Annu Rev Biochem, 69: 217-245, 2000.
59. McDonnell TJ, Deane N, Platt FM, et al. Bcl-2-immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation. Cell 57: 79-88, 1989.
60. Zinkel SS, Ong CC, Ferguson DO, et al. Proapoptotic BID is required for myeloid homeostasis and tumor suppression. Genes Dev, 17: 229-239, 2003.
61. Bouillet P, Metcalf D, Huang DC, et al. Proapoptotic BCL-2 relative BIM required for certain apoptotic responses, leukocyte homeostasis, and to preclude autoimmunity. Science, 286: 1735-1738, 1999.
62. Bouillet P, Purton JF, Godfrey DI, et al. BH3-only BCL-2 family member BIM is required for apoptosis of autoreactive thymocytes. Nature, 415: 922-926, 2002.
63. Hildeman DA, Zhu Y, Mitchell TC, et al. Activated T cell death in vivo mediated by proapoptotic bcl-2 family member bim. Immunity, 16: 759-767, 2002.
64. Ashkenazi A and Dixit VM. Death receptors: Signaling and modulation. Science, 281: 1305-1308, 1998.
65. Wallach D, Varfolomeev EE, Malinin NL, et al. Tumor necrosis factor receptor and Fas signaling mechanisms. Annu Rev Immunol 17: 331-367, 1999.
66. Locksley RM, Killeen N, Lenardo MJ. The TNF and TNF receptor superfamilies: integrating mammalian biology. Cell 104: 487-501, 2001.
67. Thome M and Tschopp J. Regulation of lymphocyte proliferation and death by FLIP. Nat Rev Immunol, 1: 50-58, 2001.
68. Zou H, Li Y, Liu X, et al. An APAF-1.cytochrome C multimeric complex is a functional apoptosome that activates procaspase-9. J Biol Chem, 274: 11549-11556, 1999.
69. Du C, Fang M, Li Y, et al. SMAC, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell, 102: 33-42, 2000.
70. Verhagen AM, Ekert PG, Pakusch M, et al. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins. Cell, 102: 43-53, 2000.
71. Chai J, Du C, Wu JW, et al. Structural and biochemical basis of apoptotic activation by SMAC/DIABLO. Nature, 406: 855-862, 2000.
72. Liu Z, Sun C, Olejniczak ET, et al. Structural basis for binding of SMAC/DIABLO to the XIAP BIR3 domain. Nature, 408: 1004-1008, 2000.
73. Wu G, Chai J, Suber TL, et al. Structural basis of IAP recognition by SMAC/DIABLO. Nature, 408: 1008-1012, 2000.
74. Srinivasula SM, Hegde R, Saleh A, et al. A conserved XIAP-interaction motif in caspase-9 and SMAC/DIABLO regulates caspase activity and apoptosis. Nature, 410: 112-116, 2001.
75. Altieri DC. Validating survivinas a cancer therapeutic target. Nat Rev Cancer, 3: 46-54, 2003.
76. Suzuki Y, Imai Y, Nakayama H, et al. A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell, 8: 613-621, 2001.
77. Hegde R, Srinivasula SM, Zhang Z, et al. Identification of Omi/HtrA2 as a mitochondrial apoptotic serine protease that disrupts inhibitor of apoptosis protein-caspase interaction. J Biol Chem, 277: 432-438, 2002.
78. Susin SA, Lorenzo HK, Zamzaini N, et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature, 397: 441-446, 1999.
79. Li LY, Luo X, Wang X. Endonuclease G (EndoG) is an apoptotic DNAse when released from mitochondria. Nature, 412: 95-99, 2001.
80. Enari M, Sakahira H, Yokoyama H, et al. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature, 391: 43-50, 1998.
81. Zamzami N and Kroemer G. The mitochondrion in apoptosis: how Pandora's box opens. Nat Rev Mol Cell Biol, 2: 67-71, 2001.
82. Lemasters JJ, Nieminen AL, Qian T, et al. The mitochondrial permeability transition in cell death: a common mechanism in necrosis, apoptosis and autophagy. Biochem Biophys Acta 1366: 177-196, 1998.
83. Schwerzmann K and Pedersen PL. Regulation of the mitochondrial ATP synthase/ATPase complex. Arch Biochem Biophys, 250: 1-18, 1986.
84. Belzacq AS, Vieira HL, Kroemer G, et al. The adenine nucleotide translocator in apoptosis. Biochimie, 84: 167-176, 2002.
85. Wang X. The expanding role of mitochondria in apoptosis. Genes Dev, 15: 2922-2933, 2001.
86. Li X, Du L, Darzynkiewicz Z. During apoptosis of HL-60 and U-937 cells caspases are activated independently of dissipation of mitochondrial electrocheimcal potential. Exp Cell Res, 257: 290-297, 2000.
87. Tsujimoto Y and Shimizu S. The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84: 187-193, 2002.
88. Antonsson B, Montessuit S, Lauper S, et al. BAX oligomerization is required for channel-forming activity in liposomes and to trigger cytochrome C release from mitochondria. Biochem J, 345: 271-278, 2000.
89. Sun XM, MacFarlane M, Zhuang J, et al. Distinct caspase cascades are initiated in receptor-mediated and chemical-induced apoptosis. J Biol Chem, 274: 5053-5060, 1999.
90. Green DR and Reed JC. Mitochondria and apoptosis. Science, 281: 1309-1312, 1998
91. Robertson JD, Enoksson M, Suomela M, et al. Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis. J Biol Chem, 277: 29803-29809, 2002.
92. Lassus P, Opitz-Araya X, Lazebnik Y. Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization. Science, 297: 1352-1354, 2002.
93. Lundberg AS and Weinberg RA. Control of the cell cycle and apoptosis. Eur J Cancer, 35: 1886-1894, 1999.
94. Chang F, Steelman LS, Shelton JG, et al. Regulation of cell cycle progression and apoptosis by the Ras/Raf/MEK/ERK pathway. Int J Oncol, 22: 469-480, 2003.
95. Ruvolo PP, Deng X, May WS. Phosphorylation of BCL2 and regulation of apoptosis. Leukemia, 15: 515-522, 2001
96. Blagosklonny MV, Giannakakou P, el-Deiry WS, et al. Raf-1/bd-2 phosphorylation: a step from microtubule damage to cell death. Cancer Res. 57: 130-135, 1997.
97. Scatena CD, Stewart ZA, Mays D, et al. Mitotic phosphorylation of BCL-2 during normal cell cycle progression and Taxol-induced growth arrest. J Biol Chem, 273: 30777-30784, 1998.
98. Chadebech P, Truchet I, Brichese L, et al. Upregulation of cdc2 protein during paclitaxel-induced apoptosis. Int J Cancer, 87: 779-786, 2000.
99. Wahl GM and Carr AM. The evolution of diverse biological responses to DNA damage: insights from yeast and p53. Nat Cell Biol, 3: E277-E286, 2001.
100. Schuler M, Bossy-Wetzel E, Goldstein JC, et al. p53 induces apoptosis by caspase activation through mitochondrial cytochrome C release. J Biol Chem, 275: 7337-7342, 2000.
101. Miyashita T and Reed JC. Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell, 80: 293-299, 1995.
102. Sheikh MS and Fornace AJ Jr. Death and decoy receptors and p53-mediated apoptosis. Leukemia, 14: 1509-1513, 2000.
103. Burns TF, Bernhard EJ, El-Deiry WS. Tissue specific expression of p53 target genes suggests a key role for KILLER/DR5 in p53-dependent apoptosis in vivo. Oncogene, 20: 4601-4612, 2001.
104. Polyak K, Xia Y, Zweier JL, et al. A model for p53-induced apoptosis. Nature, 389: 300-305, 1997.
105. Lowe SW, Bodis S, McClatchey A, et al. p53 status and the efficacy of cancer therapy in vivo. Science, 266: 807-810, 1994.
106. Perkins ND. Not just a CDK inhibitor: regulation of transcription by p21 (WAF1/CIP1/SDI1). Cell Cycle, 1: 39-41, 2002.
107. Asada M, Yamada T, Ichijo H, et al. Apoptosis inhibitory activity of cytoplasmic p21 (Cip1/WAF1) in monocytic differentiation. EMBO J, 18: 1223-1234, 1999.
108. Shim J, Lee H, Park J, et al. A non-enzymatic p21 protein inhibitor of stress-activated protein kinases. Nature, 381: 804-806, 1996.
109. Wang Z, Su ZZ, Fisher PB, et al. Evidence of a functional role for the cyclin-dependent kinase inhibitor p21(WAF1/CIP1/MDA6) in the reciprocal regulation of PKC activator-induced apoptosis and differentiation in human myelomonocytic leukemia cells. Exp Cell Res, 244: 105-116, 1998.
110. Wang Z, Van Tuyle G, Conrad D, et al. Dysregulation of the cyclin-dependent kinase inhibitor p21WAF1/CIP1/MDA6 increases the susceptibility of human leukemia cells (U937) to 1-beta-D-arabinofuranosylcytosine-mediated mitochondrial dysfunction and apoptosis. Cancer Res, 59: 1259-1267, 1999.
111. Moller MB. P27 in cell cycle control and cancer. Leuk Lymphoma, 39: 19-27, 2000.
112. KiP1 on resistance of tumor cells to anticancer agents. Nat Med, 2: 1204-1210, 1996.
113. KIP1 expression. Blood, 101: 1439-1445, 2003.
114. Castedo M, Perfettini JL, Roumier T, et al. Cyclin-dependent kinase-1: linking apoptosis to cell cycle and mitotic catastrophe. Cell Death Differ, 9: 1287-1293, 2003.
115. McIntosh JR. Cell biology. Microtubule catastrophe. Nature, 312: 196-197, 1984.
116. Ling YH, Tornos C, Perez-Soler R. Phosphorylation of BCL-2 is a marker of M phase events and not a determinant of apoptosis. J Biol Chem 273: 18984-18991, 1998.
117. Wang Q, Worland PJ, Clark JL, et al. Apoptosis in 7-hydroxystaurosporine-treated T lymphoblasts correlates with activation of cyclin-dependent kinases 1 and 2. Cell Growth Differ, 6: 927-936, 1995.
118. Morris EJ and Dyson NJ. Retinoblastoma protein partners. Adv Cancer Res, 82: 1-54, 2001.
119. Hatakeyama M and Weinberg RA. The role of RB in cell cycle control. Prog Cell Cycle Res, 1: 9-19, 1995.
120. Almasan A, Yin Y, Kelly RE, et al. Deficiency of retinoblastoma protein leads to inappropriate S-phase entry, activation of E2F-responsive genes, and apoptosis. Proc Natl Acad Sci USA, 92: 5436-5440, 1995.
121. Nahle Z, Polakoff J, Davulurl RV, et al. Direct coupling of the cell cycle and cell death machinery by E2F. Nat Cell Biol, 4: 859-864, 2002.
122. Pelengaris S, Khan M, Evan G. c-MYC: more than just a matter of life and death. Nat Rev Cancer, 2: 764-776, 2002.
123. Harrington EA, Bennett MR, Fanidi A, et al. c-Myc-induced apoptosis in fibroblasts is inhibited by specific cytokines. EMBO J, 13: 3286-3295, 1994.
124. Bissonnette RP, Echeverri F, Mahboubi A, et al. Apoptotic cell death induced by c-myc is inhibited by bcl-2. Nature, 359: 552-554, 1992.
125. Juin P, Hueber AO, Littlewood T, et al. c-Myc-induced sensitization to apoptosis is mediated through cytochrome c release. Genes Dev, 13: 1367-1381, 1999.
126. Packham G and Cleveland JL. Ornithine decarboxylase is a mediator of c-Myc-induced apoptosis. Mol Cell Biol, 14: 5741-5747, 1994.
127. Morgan DO. Principles of CDK regulation. Nature, 374: 131-134, 1995.
128. 1 by transcriptional repression in MCF-7 human breast carcinoma cells induced by flavopiridol. Cancer Res, 59: 4634-4641, 1999.
129. Carlson BA, Dubay MM, Sausville EA, et al. Flavopiridol induces G1 arrest with inhibition of cyclin-dependent kinase (CDK) 2 and CDK4 in human breast carcinoma cells. Cancer Res, 56: 2973-2978, 1996.
130. 1 in transformation by ErbB2 predicts synergy between herceptin and flavopiridol. Cancer Res, 62: 2267-2271, 2002.
131. Xia Z, Dickens M, Raingeaud J, et al. Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis. Science, 270: 1326-1331, 1995.
132. Yamamoto K, Ichijo H, Korsmeyer SJ. BCL-2 is phosphorylated and inactivated by an ASK1/Jun N-terminal protein kinase pathway normally activated at G(2)/M. Mol Cell Biol, 19: 8469-8478, 1999.
133. Tournier C, Hess P, Yang DD, et al. Requirement of JNK for stress-induced activation of the cytochrome c-mediated death pathway. Science, 288: 870-874, 2000.
134. Lei K, Davis RJ. JNK phosphorylation of BIM-related members of the BCL2 family induces BAX-dependent apoptosis. Proc Natl Acad Sci USA, 100: 2432-2437, 2003.
135. 2-terminal kinase. J Exp Med, 191: 1017-10130, 2000.
136. 2-terminal kinase/stress-activated protein kinase (JNK/SAPK) is critical for hypoxia-induced apoptosis of human malignant melanoma. Cell Growth Differ, 12: 137-145, 2001.
137. Jin K, Mao XO, Zhu Y, et al. MEK and ERK protect hypoxic cortical neurons via phosphorylation of Bad. J Neurochem, 80: 119-125, 2002.
138. Deng X, Ruvolo P, Carr B, et al. Survival function of ERK1/2 as IL-3-activated, staurosporine-resistant BCL2 kinases. Proc Natl Acad Sci USA, 97: 1578-1583, 2000.
139. Liu Y, Martindale JL, Gorospe M, et al. Regulation of p21WAF1/CIP1 expression through mitogen-activated protein kinase signaling pathway. Cancer Res, 56: 31-35, 1996
140. Datta SR, Dudek H, Tao X, et al. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell, 91: 231-241, 1997.
141. Scheid MP, Woodgett JR. PKB/AKT: functional insights from genetic models. Nat Rev Mol Cell Biol, 2: 760-768, 2001.
142. Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells. Nat Cell Biol, 3: 245-252, 2001.
143. Kim AH, Khursigara G, Sun X, et al. Akt phosphorylates and negatively regulates apoptosis signal-regulating kinase 1. Mol Cell Biol, 21: 893-901, 2001.
144. Hohmann HP, Remy R, Poschl B, et al. Tumor necrosis factors-alpha and -beta bind to the same two types of tumor necrosis factor receptors and maximally activate the transcription factor NF-kappa B at low receptor occupancy and within minutes after receptor binding. J Biol Chem, 265: 15183-15188, 1990.
145. Bowie A and O'Neill LA. Oxidative stress and nuclear factor-kappaB activation: a reassessment of the evidence in the light of recent discoveries. Biochem Pharmacol, 59: 13-23, 2000.
146. Mayo MW and Baldwin AS. The transcription factor NF-kappaB: control of oncogenesis and cancer therapy resistance. Biochim Biophys Acta, 1470: M55-62, 2000.
147. Khoshnan A, Tindell C, Laux I, et al. The NF-kappa B cascade is important in BCL-xL expression and for the anti-apoptotic effects of the CD28 receptor in primary human CD4+ lymphocytes. J Immunol, 165: 1743-1754, 2000.
148. Stehlik C, de Martin R, Kumabashiri I, et al. Nuclear factor (NF)-kappaB-regulated X-chromosome-linked iap gene expression protects endothelial cells from tumor necrosis factor alpha-induced apoptosis. J Exp Med, 188: 211-216, 1998.
149. Ravi R, Bedi GC, Engstrom LW, et al. Regulation of death receptor expression and TRAIL/Apo2L-induced apoptosis by NF-kappaB. Nat Cell Biol, 3: 409-416, 2001.
150. Mitsiades N, Mitsiades CS, Poulaki V, et al. Molecular sequelae of proteasome inhibition in human multiple myeloma cells. Proc Natl Acad Sci USA, 99: 14374-14379, 2002.
151. Wang CY, Cusack JC Jr, Liu R, et al. Control of inducible chemoresistance: enhanced antitumor therapy through increased apoptosis by inhibition of NF-kappaB. Nat Med, 5: 412-417, 1999.
152. Jarvis WD, Fomari FA Jr, Browning JL, et al. Attenuation of ceramide-induced apoptosis by diglyceride in human myeloid leukemia cells. J Biol Chem, 269: 31685-31692, 1994.
153. Lotem J, Cragoe EJ Jr, Sachs L. Rescue from programmed cell death in leukemic and normal myeloid cells. Blood, 78: 953-960, 1991.
154. Bertrand R, Solary E, O'Connor P, et al. Induction of a common pathway of apoptosis by staurosporine. Exp Cell Res, 211: 314-321, 1994.
155. Jarvis WD, Turner AJ, Povirk LF, et al. Induction of apoptotic DNA fragmentation and cell death in HL-60 human promyelocytic leukemia cells by pharmacological inhibitors of protein kinase C. Cancer Res, 54: 1707-1714, 1994.
156. Wang S, Vrana JA, Bartimole TM, et al. Agents that down-regulate or inhibit protein kinase C circumvent resistance to 1-beta-D-arabinofuranosylcytosine-induced apoptosis in human leukemia cells that overexpress BCL-2. Mol Pharmacol, 52: 1000-1009, 1997.
157. Wang Z, Wang S, Dai Y, et al. Bryostatin 1 increases 1-beta-D-arabinofuranosylcytosine-induced cytochrome c release and apoptosis in human leukemia cells ectopically expressing BCL-x(L). J Pharmacol Exp Ther, 301: 568-77, 2002.
158. Wang S, Wang Z, Grant S. Bryostatin 1 and UCN-01 potentiate 1-beta-D-arabinofuranoylcytosine-induced apoptosis in human myeloid leukemia cells through disparate mechanisms. Mol Pharmacol, 63: 232-242, 2003.
159. Jarvis WD, Kolesnick RN, Fomari FA, et al. Induction of apoptotic DNA damage and cell death by activation of the sphingomyelin pathway. Proc Natl Acad Sci USA, 91: 73-77, 1994.
160. Cuvillier O, Pirianov G, Kleuser B, et al. Suppression of ceramide-mediated programmed cell death by sphingosine-1-phosphate. Nature, 381: 800-803, 1996.
161. Majumder PK, Pandey P, Sun X, et al. Mitochondrial translocation of protein kinase C delta in phorbol ester-induced cytochrome C release and apoptosis. J Biol Chem, 275: 21793-21796, 2000.
162. Campos L, Rouault JP, Sabido O, et al. High expression of bcl-2 protein in acute myeloid leukemia cells is associated with poor response to chemotherapy. Blood, 81: 3091-3096, 1993.
163. Konopleva M, Tari AM, Estrov Z, et al. Liposomal BCL-2 antisense oligonucleotides enhance proliferation, sensitize acute myeloid leukemia to cytosine-arabinoside, and induce apoptosis independent of other antiapoptotic proteins. Blood, 95: 3929-3938, 2000.
164. Rudin CM, Otterson GA, Mauer AM, et al. A pilot trial of G3139, a bcl-2 antisense oligonucleotide, and paclitaxel in patients with chemorefractory small-cell lung cancer. Ann Oncol, 13: 539-545, 2002.
165. Wang JL, Liu D, Zhang ZJ, et al. Structure-based discovery of an organic compound that binds BCL-2 protein and induces apoptosis of tumor cells. Proc Natl Acad Sci USA, 97: 7124-7129, 2000.
166. Liu D, Huang Z. Synthetic peptides and non-peptidic molecules as probes of structure and function of BCL-2 family proteins and modulators of apoptosis. Apoptosis, 6: 453-462, 2001
167. Amt CR, Chiorean MV, Heldebrant MP, et al. Synthetic SMAC/DIABLO peptides enhance the effects of chemotherapeutic agents by binding XIAP and cIAP1 in situ. J Biol Chem, 277: 44236-44243, 2002.
168. Olie RA, Simoes-Wust AP, Baumann B, et al. A novel antisense oligonucleotide targeting survivin expression induces apoptosis and sensitizes lung cancer cells to chemotherapy. Cancer Res, 60: 2805-2809, 2000.
169. Sasaki H, Sheng Y, Kotsuji F, et al. Down-regulation of X-linked inhibitor of apoptosis protein induces apoptosis in chemoresistant human ovarian cancer cells. Cancer Res, 60: 5659-5666, 2000.
170. Reed JC. Apoptosis-targeted therapies for cancer. Cancer Cell, 3: 17-22, 2003
171. Scaffidi C, Fulda S, Srinivasan A, et al. Two CD95 (APO-1/Fas) signaling pathways. EMBO J, 17: 1675-1687, 1998.
172. Altucci L, Rossin A, Raffelsberger W, et al. Retinoic acid-induced apoptosis in leukemia cells is mediated by paracrine action of tumor-selective death ligand TRAIL. Nat Med, 7: 680-686, 2001.
173. Lacour S, Hammann A, Wotawa A, et al. Anticancer agents sensitize tumor cells to tumor necrosis factor-related apoptosis-inducing ligand-mediated caspase-8 activation and apoptosis. Cancer Res, 61: 1645-1651, 2001.
174. Ito Y, Pandey P, Place A, et al. The novel triterpenoid 2-cyano-3, 12-dioxoolean-1, 9-dien-28-oic acid induces apoptosis of human myeloid leukemia cells by a caspase-8-dependent mechanism. Cell Growth Differ, 11: 261-267, 2000.
175. Kitada S, Zapata JM, Andreeff M, et al. Protein kinase inhibitors flavopiridol and 7-hydroxy-staurosporine down-regulate antiapoptosis proteins in B-cell chronic lymphocytic leukemia. Blood, 96: 393-397, 2000.
176. Gojo I, Zhang B, Fenton RG. The Cyclin-dependent Kinase Inhibitor Flavopiridol Induces Apoptosis in Multiple Myeloma Cells through Transcriptional Repression and Down-Regulation of Mcl-1. Clin Cancer Res, 8: 3527-3538, 2002.
177. Chao SH, Fujinaga K, Marion JE, et al. Flavopiridol inhibits P-TEFb and blocks HIV-1 replication. J Biol Chem, 275: 28345-28348, 2000.
178. Achenbach TV, Muller R, Slater EP. BCL-2 independence of flavopiridol-induced apoptosis. Mitochondrial depolarization in the absence of cytochrome c release. J Biol Chem, 275: 32089-32097, 2000.
179. An B, Goldfarb RH, Siman R, et al. Novel dipeptidyl proteasome inhibitors overcome BCL-2 protective function and selectively accumulate the cyclin-dependent kinase inhibitor p27 and induce apoptosis in transformed, but not normal, human fibroblasts. Cell Death Differ, 5: 1062-1075, 1998.
180. Adams J. Proteasome inhibitors as new anticancer drugs. Curr Opin Oncol, 14: 628-634, 2002.
181. Milella M, Estrov Z, Kornblau SM, et al. Synergistic induction of apoptosis by simultaneous disruption of the BCL-2 and MEK/MAPK pathways in acute myelogenous leukemia. Blood, 99: 3461-3464, 2002.
182. Orlowski RZ, Small GW, Shi YY. Evidence that inhibition of p44/42 mitogen-activated protein kinase signaling is a factor in proteasome inhibitor-mediated apoptosis. J Biol Chem, 277: 2786427871, 2002.
183. Cartee L, Wang Z, Decker RH et al. The cyclin-dependent kinase inhibitor (CDKI) flavopiridol disrupts phorbol 12-myristate 13-acetate-induced dfferentiation and CDKI expression while enhancing apoptosis in human myeloid leukemia cells. Cancer Res, 61: 2583-2591, 2001.
184. Cartee L, Smith R, Dai Y, et al. Synergistic induction of apoptosis in human myeloid leukemia cells by phorbol 12-myristate 13-acetate and flavopiridol proceeds via activation of both the intrinsic and tumor necrosis factor-mediated extrinsic cell death pathways. Mol Pharmacol, 61: 1313-1321, 2002.