Apoptosis

Academic Emergency Medicine

Volumn 5, Issue 10, 1998, Pages 1019-1029

  White, Blaine C ^a,b   Sullivan, Jonathon M ^a  

^a WAYNE STATE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b DETROIT RECEIVING HOSPITAL   (United States)

Author keywords

Apoptosis; Cell suicide; Programmed cell death

Indexed keywords

CALCIUM ION; CELL DNA; PROTEINASE;

APOPTOSIS; ARTICLE; CAENORHABDITIS ELEGANS; CALCIUM CELL LEVEL; CELL DEATH; DNA DEGRADATION; ENDOPLASMIC RETICULUM; ENZYME ACTIVATION; HUMAN; MOLECULAR BIOLOGY; NONHUMAN; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTO ONCOGENE; SIGNAL TRANSDUCTION;

EID: 0031711096     PISSN: 10696563     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1553-2712.1998.tb02785.x     Document Type: Article

References (105)

1. Bredesen DE. Keeping neurons alive: the molecular control of apoptosis. Neuroscientist. 1996; 2:211-6.
2. Hale AJ, Smith CA, Sutherland LC, et al. Apoptosis: molecular regulation of cell death. Eur J Biochem. 1995; 236:1-26.
3. Arends MJ, Morris RG, Wyllie AH. Apoptosis. The role of the endonuclease. Am J Pathol. 1990; 136:593-608.
4. Jacobson MD, Burne JF, Raff MC. Programmed cell death and Bcl-2 protection in the absence of a nucleus. EMBO J. 1994; 13:1899-910.
5. Ellis RE, Jacobson DM, Horvitz HR, Genes required for the engulfment of cell corpses during programmed cell death in C. elegans. Genetics. 1991; 129:79-94.
6. Nagata S, Golstein P. The Fas death factor. Science. 1995; 267:1449-56.
7. Ahmad M, Srinivasula SM, Wang L, et al. CRADD, a novel human apoptotic adaptor molecule for caspase-2 and FasL/tumor necrois factor recepor-interacting protein RIP. Cancer Res. 1997; 57:615-9.
8. Muzio M, Salvesen GS, Dixit VM. FLICE-induced apoptosis in a cell-free system. Cleavage of caspase zymogens. J Biol Chem. 1997; 272:2952-6.
9. Zhou Q, Snipas S, Orth K, Muzio M, Dixit VM, Salvesen GS. Target protease specificity of the viral serpin CrmA. Analysis of five caspases. J Biol Chem. 1997; 272:7797-800.
10. Bertin J, Armstrong RC, Ottilie S, et al. Death effector domain-containing herpesvirus and poxvirus proteins inhibit both FAS- and TNFR1-induced apoptosis. Proc Natl Acad Sci U S A. 1997; 94:1172-6.
11. Kajstura J, Cheng W, Reiss K, et al. Apoptotic and necrotic myocyte cell deaths are independent contributing variables in infarct size in rats. Lab Invest. 1996; 74:86-107.
12. Bromine HJ, Holtz J. Apoptosis in the heart: when and why? Mol Cell Biochem. 1996; 163-164:261-75.
13. Matsuyama T, Hata R, Tagaya M, et al. Fas antigen mRNA induction in postischemic murine brain. Brain Res. 1994; 657: 342-6.
14. Zhang ZG, Chopp M, Goussev A, Powers C. Tumor necrosis factor receptor expression following focal embolic cerebral ischemia in mice [abstract]. J Cereb Blood Flow Metab. 1997; 17(suppl 1):S531.
15. Bruce AJ, Boling W, Kindy MS, et al. Altered neuronal and microglial responses to excitotoxic and ischemic brain injury in mice lacking TNF receptors. Nature Med. 1996; 2:788-94.
16. Der SD, Yang YL, Weissmann C, Williams BRG. A double-stranded RNA-activated protein kinase-dependent pathway mediating stress-induced apoptosis. Proc Natl Acad Sci USA. 1997; 94:3279-83.
17. Irmler M, Hofmann K, Vaux D, Tschopp J. Direct physical interaction between the C. elegans 'death proteins' CED-3 and CED-4. FEBS Lett. 1997; 406:189-90.
18. Zou H, Henzel WJ, Liu X, Lutschg A, Wang X. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase 3. Cell. 1997; 90:405-13.
19. James C, Gschmeissner S, Fraser A, Evan GI. CED-4 induces chromatin condensation in S. pombe and is inhibited by direct physical interaction with CED-9. Curr Biol. 1997; 7: 246-52.
20. Spector MS, Desnoyers S, Hoeppner DJ, Hengartner MO. Interaction between the C. elegans cell-death regulators CED-9 and CED-4. Nature. 1997; 385:653-6.
21. Gillardon F, Botiger BW, Schmitz B, Hossmann KA. Activation of CPP-32, an ICE-related protease, in hippocampal neurons following ischemia and epilepsy [abstract]. J Cereb Blood Flow Metab. 1997; 17(suppl 1):S445.
22. Hara H, Friedlander RM, Gagliardini V, et al. Inhibition of interleukin 1β converting enzyme family proteases reduces ischemic and excitotoxic neuronal damage. Proc Natl Acad Sci U S A. 1997; 94:2007-12.
23. Martins LM, Kottke T, Mesner PW, et al. Activation of multiple interleukin-1β converting enzyme homologues in cytosol and nuclei of HL-60 cells during etoposide-induced apoptosis. J Biol Chem. 1997; 272:7421-30.
24. Margolin N, Raybuck SA, Wilson KP, et al. Substrate and inhibitor specificity of interleukin-1 beta-converting enzyme and related caspases. J Biol Chem. 1997; 272:7223-8.
25. Van de Craen M, Vandenabeele P, Declercq W, et al. Characterization of seven murine caspase family members. FEBS Lett. 1997; 403:61-9.
26. Le Romancer M, Cosulich SC, Jackson SP, Clarke PR. Cleavage and inactivation of DNA-dependent protein kinase catalytic subunit during apoptosis in Xenopus egg extracts. J Cell Sci. 1996; 109(pt 13):3121-7.
27. Rosenthal DS, Ding R, Simbulan-Rosenthal CMG, Cherney B, Vanek P, Smulson M. Detection of DNA breaks in apoptotic cells utilizing the DNA binding domain of poly(ADP-ribose) polymerase with fluorescence microscopy. Nucleic Acids Res. 1997; 15:1437-41.
28. Shah GM, Poirer D, Desnoyers S, et al. Complete inhibition of poly(ADP-ribose) polymerase activity prevents the recovery of C3H10T1/2 cells from oxidative stress. Biochim Biophys Acta. 1996; 1312:1-1317.
29. Whitacre CM, Hashimoto H, Tsai ML, Chatterjee S, Berger SJ, Berger NA. Involvement of NAD-poly(ADP-ribose) metabolism in p53-regulation and its consequences. Cancer Res. 1995; 55:3697-701.
30. Gaken JA, Tavassoli M, Gan SU, et al. Efficient retroviral infection of mammalian cells is blocked by inhibition of poly(ADP-ribose) polymerase activity. J Virol. 1996; 70:3992-4000.
31. Uchida K, Uchida M, Hanai S, et al. Isolation of the poly(ADP-ribose) polymerase-encoding cDNA from Xenopus laevis: phylogenetic conservation of the functional domain. Gene. 1993; 137:293-7.
32. Mashima T, Naito M, Noguchi K, Miller DK, Nicholson DW, Tsuruo T. Actin cleavage by CPP-32/apopain during the development of apoptosis. Oncogene. 1997; 14:1007-12.
33. Kuida K, Zheng TS, Na S, et al. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature. 1996; 384:368-72.
34. Ni B, Wu X, Du Y, et al. Cloning and expression of a rat brain interleukin-1β-converting enzyme (ICE)-related protease (IRP) and its possible role in apoptosis of cultured cerebellar granule neurons. J Neurosci. 1997; 17:1561-9.
35. Allet B, Hochmann A, Martinou I, et al. Dissecting processing and apoptotic activity of a cysteine protease by mutant analysis. J Cell Biol. 1996; 135:479-86.
36. Gu Y, Sarnecki C, Aldape RA, Livingston DJ, Su MS. Cleavage of poly(ADP-ribose) polymerase by interleukin-1 beta converting enzyme and its homologs TX and Nedd-2. J Biol Chem. 1995; 270:18715-8.
37. Srinivasan A, Foster LM, Testa MP, et al. Bcl-2 expression in neural cells blocks activation of ICE/CED-3 family proteases during apoptosis. J Neurosci. 1996; 16:5654-60.
38. Troy CM, Stefanis L, Greene LA, Shelanski ML. Nedd2 is required for apoptosis after trophic factor withdrawal, but not Superoxide dismutase (SOD1) down-regulation, in sympathetic neurons and PC12 cells. J Neurosci. 1997; 17:1911-8.
39. Henderson S, Huen D, Rowe M, Dawson C, Johnson G, Rickinson A. Epstein-Barr virus-encoded BHRF1 protein, a viral homologue of Bcl-2, protects human B cells from programmed cell death. Proc Natl Acad Sci USA. 1993; 90: 8479-83.
40. 2+ fluxes. Proc Natl Acad Sci USA. 1994; 91:6569-73.
41. Antonsson B, Conti F, Ciavatta AM, et al. Inhibition of Bax channel-forming activity by Bcl-2. Science. 1997; 277:370-2.
42. Merrick WC. Mechanism and regulation of eukaryotic protein synthesis. Microbiol Rev. 1992; 56:291-315.
43. Rowlands AG, Panniers R, Henshaw E. The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J Biol Chem. 1988; 263:5526-33.
44. Samuel CE. The eIF-2α protein kinases, regulators of translation in eukaryotes from yeasts to humans. J Biol Chem. 1993; 268:7603-6.
45. Wek RC. eIF-2 kinases: regulators of general and gene-specific translation initiation. Trends Biol Sci. 1994; 19:491-6.
46. Haines GK, Ghadge G, Radosevich JA. Expression of p68 protein kinase as recognized by the monoclonal antibody TJ4C4 during human fetal development. Tumor Biol. 1993; 14: 95-104.
47. Schwemmle M, Clemens MJ, Hilse K, et al. Localization of Epstein-Barr virus-encoded RNAs EBER-1 and EBER-2 in interphase and mitotic burkitt lymphoma cells. Proc Natl Acad Sci U S A. 1992; 89:10292-6.
48. Jeffrey IW, Kadereit S, Meurs EF, et al. Nuclear localization of the interferon-inducible protein kinase PKR in human cells and transfected mouse cells. Exp Cell Res. 1995; 218: 17-27.
49. Thomas DC, Samuel CE. Mechanism of interferon action: characterization of the intermolecular autophosphorylation of PKR, the interferon-inducible, RNA-dependent protein kinase. J Virol. 1995; 69:5195-8.
50. Proud CG. PKR: a new name and new roles. Trends Biol Sci. 1995; 20:241-6.
51. Jagus R, Gray MM. Proteins that interact with PKR. Biochimie. 1994; 76:779-91.
52. Petryshyn RA, Li J, Judware R. Activation of the dsRNA-dependent kinase. Prog Mol Subcell Biol. 1994; 14:1-14.
53. Mundschau LJ, Faller DV. Endogenous inhibitors of the dsRNA-dependent eIF-2α protein kinase PKR in normal and ras-transformed cells. Biochimie. 1994; 76:792-800.
54. Bandyopadhyhay SK, Sen GC. Role of protein phosphorylation in activation of interferon-stimulated gene factors. J Biol Chem. 1992; 267:6389-95.
55. Takizawa T, Fukuda, R, Miyawaki T, Ohashi K, Nakanishi Y. Activation of the apoptotic FAS antigen-encoding gene upon influenza virus infection involving spontaneously produced β-interferon. Virology. 1995; 209:288-96.
56. Kaufman RJ, Srivastava SP. PKR: a general transducer of the cellular stress response leading to apoptosis [abstract]. In: Translational Control. New York: Cold Spring Harbor, 1996, p 127.
57. 2+ requirement for protein synthesis in eukaryotic cells. J Biol Chem. 1983; 258:14390-9.
58. Brostrom CO, Bocckino SB, Brostrom MA, Galuska EM. Regulation of protein synthesis in isolated hepatocyctes by calcium-mobilizing hormones. Mol Pharmacol. 1985; 29:104-11.
59. Chin KV, Cade C, Brostrom CO, Galuska EM, Brostrom MA. Calcium-dependent regulation of protein synthesis at translational initiation in eukaryotic cells. J Biol Chem. 1987; 262:16509-14.
60. Brostrom CO, Chin KV, Wong WL, Cade C, Brostrom MA. Inhibition of translation initition in eukaryotic cells by calcium ionophore. J Biol Chem. 1989; 264:1644-9.
61. Kumar RV, Wolfman A, Panniers R, Henshaw EC. Mechanism of inhibition of polypeptide chain initiation in calcium-depleted Erlich ascites tumor cells. J Cell Biol. 1989; 108: 2107-15.
62. Kimball SR, Jefferson LS. Regulation of protein sythesis by modulation of intracellular calcium in rat liver. Endocrinol Metab. 1992; 26:E958-E964.
63. Prostko CR, Brostrom MA, Malara EM, Brostrom CO. Phosphorylation of eukaryotic initiation factor (eIF) 2 alpha and inhibition of eIF-2B in GH3 pituitary cells by perturbation of early protein processing that induces GRP78. J Biol Chem. 1992; 267:16751-4.
64. Prostko CR, Brostrom MA, Brostrom CO. Reversible phosphorylation of eukaryotic initiation factor 2 alpha in response to endoplasmic reticular signaling. Mol Cell Biochem. 1993; 127/128:255-65.
65. Prostko CR, Dholakia JN, Brostrom MA, Brostrum CO. Activation of the double-stranded RNA-regulated protein kinase by depletion of endoplasmic reticulum calcium stores. J Biol Chem. 1995; 270:6211-5.
66. Srivatava SP, Davies MV, Kaufman RJ. Calcium deletion from the endoplasmic reticulum activates the double-stranded RNA-dependent protein kinase (PKR) to inhibit protein synthesis. J Biol Chem. 1995; 28:16619-24.
67. Petryshyn RA, Li J. Activation of the double-stranded RNA-dependent eIF-2α kinase by cellular RNA from 3T3-F442A cells. Eur J Biochem. 1991; 195:41-8.
68. Ito T, Jagus R. Interleukin 3 stimulates protein synthesis by regulating double-stranded RNA-dependent protein kinase. Proc Natl Acad Sci U S A. 1994; 91:7455-9.
69. 2+ in the epidermal growth factor-induced inhibition of protein tyrosine phosphatase activity in a breast cancer cell line. Biochem Biophys Res Commun. 1993; 191:1066-72.
70. Frangioni JV, Beahm PH, Shifrin V, Jos CA, Neel BG. Non-transmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. Cell. 1992; 68:545-60.
71. Rotman EI, Brostrom MA, Brostrom CO. Inhibition of protein synthesis in intact mammalian cells by arachidonic acid. Biochem J. 1992; 282:487-94.
72. Fleming N, Mellow L. Arachidonic acid stimulates intracellular calcium mobilization and regulates protein synthesis, ATP levels, and mucin secretion in submandibular gland cells. J Dent Res. 1995; 74:1295-302.
73. Abe K, Yoshidomi M, Kogure K. Arachidonic acid metabolism in ischemic neuronal damage. Ann N Y Acad Sci. 1989; 559:259-68.
74. DeGracia DJ, Neumar RW, White BC, Krause GS. Global brain ischemia and reperfusion: modifications in eukaryotic initiation factors are associated with inhibition of translation initiation. J Neurochem. 1996; 67:2005-12.
75. DeGracia DJ, Sullivan JM, Neumar RW, et al. Effect of brain ischemia and reperfusion on the localization of phosphorylated eukaryotic initiation factor 2α. J Cereb Blood Flow Metab. 1997; 17:1291-302.
76. 2+ release channels in rat brain. J Neurosci. 1993; 13:3051-63.
77. 2+ release channel by arachidonic acid. J Mol Cell Cardiol. 1996; 18:43-51.
78. Marks AM. Intracellular calcium-release channels: regulators of cell life and death. Am J Physiol. 1997; 272:H597-H605.
79. Marks AR. Cellular functions of immunophilins. Physiol Rev. 1996; 76:631-49.
80. Cameron AM, Steiner JP, Sabatini DM, Kaplin AL, Walensky LD, Snyder SH. Immunophilin FK506 binding protein associated with inositol 1,4,5-triphosphate receptor modulates calcium flux. Proc Natl Acad Sci USA. 1995; 92:1784-8.
81. Timermann AP, Wiederrecht G, Marcy A, Fleischer S. Characterization of an exchange reaction between soluble FKBP-12 and the FKBP-ryanodine receptor complex. Modulation by FKBP mutants deficient in peptidyl-prolyl isomerase activity. J Biol Chem. 1995; 270:2451-9.
82. Sharkey J, Butcher SP. Immunophilins mediate the neuroprotective effects of FK506 in focal cerebral ischemia. Nature. 1994; 371:336-9.
83. Katayama Y, Kamlya T, Muramatsu H, Abe H, Terashi A. Immunosuppressant FK506 enhances immediate - early gene expression and prevents delayed neuronal death in the gerbil hippocampus [abstract]. J Cereb Blood Flow Metab. 1997; 17(suppl 1):S492.
84. Kamlya T, Katayama Y, Aoyama S, Muramatsu H, Abe H, Terashi A. Neuroprotective effects of immunosuppressant FK506 in focal cerebral ischemia in the rat: the effect on cerebral infarction, brain edema, immediate - early genes, and heat shock protein hsp72 [abstract]. J Cereb Blood Flow Metab. 1997; 17(suppl 1):S372.
85. Thomson AW, Bonham CA, Zeevi A. Mode of action of tacrolimus (FK506): molecular and cellular mechanisms. Ther Drug Monit. 1995; 17:584-91.
86. Bierer BE, Schreiber SL, Burakoff SJ. The effect of the immunosuppressant FK-506 on alternate pathways of T cell activation. Eur J Immunol. 1991; 21:439-45.
87. Odom A, Del Poeta M, Perfect J, Jeitman J. The immunosuppressant FK506 and its non-immunosuppressive analog L-685,818 are toxic to Cryptococcus neoformans by inhibition of a common target protein. Antimicrob Agents Chemother. 1997; 41:156-61.
88. Fischer S, Michnick S, Karplus M. A mechanism for rotamase catalysis by the FK506 binding protein (FKBP). Biochemistry. 1993; 32:13830-7.
89. Galat A. Peptidylproline cis-trans-isomerases: immunophilins. Eur J Biochem. 1993; 216:689-707.
90. Montague JW, Hughes FM, Cidlowski JA. Native recombinant cyclophilins A, B, and C degrade DNA independently of peptidylprolyl cis-trans-isomerase activity. Potential roles of cyclophilins in apoptosis. J Biol Chem. 1997; 272:6677-84.
91. Montague JW, Gaido ML, Frye C, Cidlowski JA. The calcium-dependent nuclease from apoptotic rat thymocytes is homologous with cyclophilin. Recombinant cyclophilins A, B, and C have nuclease activity. J Biol Chem. 1994; 169:18877-80.
92. Wine RN, Ku WW, Li LH, Chapin RE. Cyclophilin A is present in rat germ cells and is associated with spermatocyte apoptosis. Biol Reprod. 1997; 56:439-46.
93. Fraser MJ, Tynan SJ, Papaioannou A, Ireland CM, Pittman SM. Endo-exonuclease of human leukaemic cells: evidence for a role in apoptosis. J Cell Sci. 1996; 109:2343-60.
94. 2+ and oxidant stress. Eur J Biochem. 1996; 238:166-72.
95. 2+-activated inner membrane pore of heart mitochondria. Eur J Biochem. 1995; 230:1125-32.
96. 2+ release to cyclosporin A and related compounds. Biochem Pharmacol. 1993; 45:641-6.
97. Golstein P. Controlling cell death. Science. 1997; 275: 1081-2.
98. Liu J, Albers MW, Wandless TJ, et al. Inhibition of T cell signaling by immunophilin-ligand complexes correlates with loss of calcineurin phosphatase activity. Biochem. 1992; 31: 3896-901.
99. Dawson TM, Steiner JP, Dawson VL, Dinerman JL, Uhl GR, Snyder SH. Immunosuppressant FK506 enhances phosphorylation of nitric oxide synthase and protects against glutamate neurotoxicity. Proc Natl Acad Sci U S A. 1993; 90: 9808-12.
100. Wiederrecht G, Hong S, Chan HK, et al. Characterization of high molecular weight FK-506 binding activities reveals a novel FK-506 binding protein as well as a protein complex. J Biol Chem. 1992; 267:21753-60.
101. Steiner JP, Connolly MA, Valentine HL, et al. Neurotrophic actions of non-immunosuppressive analogues of immunosuppressive drugs FK506, rapamycin and cyclosporin A. Nature Med. 1997; 3:421-8.
102. + T cells from human immunodificiency virus-infected persons: differential in vitro preventive effect of cytokines and protease antagonists. Blood. 1996; 87:4959-66.
103. Neumar RW, Hagle SM, DeGracia DJ, Krause GS, White BC. Brain μ-calpain autolysis during global cerebral ischemia. J Neurochem. 1996; 66:421-4.
104. Squier MK, Cohen JJ. Calpain, an upstream regulator of thymocyte apoptosis. J Immunol. 1997; 158:3690-7.
105. Jordan J, Galindo MF, Miller RJ. Role of calpain- and ICE-like proteases in the beta-amyloid-induced death of rat hippocampal neurons in culture. J Neurochem. 1997; 68: 1612-21.