Sealing one's fate: Control of cell death in neurons

Current Opinion in Neurobiology

Volumn 8, Issue 1, 1998, Pages 55-63

  Bergeron, Louise ^a   Yuan, Junying ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CASPASE; CYCLIN D1; PROTEIN BAX; PROTEIN BCL 2; UNCLASSIFIED DRUG;

APOPTOSIS; CAENORHABDITIS ELEGANS; CELL DEATH; DEGENERATIVE DISEASE; ENZYME ACTIVATION; MACROMOLECULE; NERVE CELL; ONCOGENE C JUN; PRIORITY JOURNAL; PROTEIN FAMILY; REVIEW; SYNTHESIS;

EID: 0031900347     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-4388(98)80008-1     Document Type: Article

References (59)

1. Burek MJ, Oppenheim RW. Programmed cell death in the developing nervous system. Brain Pathol. 6:1996;427-446.
2. Oppenheim RW. Neurotrophic survival molecules for motoneurons: an embarrassment of riches. Neuron. 17:1996;195-197.
3. Yuan J. Transducing signals of life and death. Curr Opin Cell Biol. 9:1997;247-251.
4. Carter BD, Lewin GR. Neutrophins live or let die: does p75NTR decide? Neuron. 18:1997;187-190.
5. Frade JM, Rodriguez-Tebar A, Barde YA. Induction of cell death by endogenous nerve growth factor through its p75 receptor. of outstanding interest Nature. 383:1996;166-168 The first description of a neuronal death receptor. The authors also propose a mechanism by which neurons are selected to die during early embryonic development, before target innervation and neurotrophin dependency take place.
6. Casaccia Bonnefil P, Carter BD, Dobrowsky RT, Chao MV. Death of oligodendrocytes mediated by the interaction of nerve growth factor with its receptor p75. Nature. 383:1996;716-719.
7. Herdegen T, Skene P, Bahr M. The c-Jun transcription factor - bipotential mediator of neuronal death, survival and regeneration. Trends Neurosci. 20:1997;227-231.
8. Deshmukh M, Johnson EM Jr. Programmed cell death in neurons: focus on the pathway of nerve growth factor deprivation-induced death of sympathetic neurons. Mol Pharmacol. 51:1997;897-906.
9. Dickens M, Rogers JS, Cavanagh J, Raitano A, Xia Z, Halpern JR, Greenberg ME, Sawyers CL, Davis RJ. A cytoplasmic inhibitor of the JNK signal transduction pathway. of outstanding interest Science. 277:1997;693-696 This study describes a novel factor that is highly effective at blocking JNK activity, as well as blocking apoptosis induced by NGF withdrawal in PC12 cells. This inhibitor may play a pivotal role in regulating the response to JNK activation in neurons.
10. Philpott KL, McCarthy MJ, Kippel A, Rubin LL. Activated phosphatidyl inositol 3-kinase and Akt kinase promote survival of superior cervical neurons. J Cell Biol. 139:1997;809-815.
11. Dudek H, Datta SR, Franke TF, Birnbaum MJ, Yao R, Cooper GM, Segal RA, Kaplan DR, Greenberg ME. Regulation of neuronal survival by the serine-threonine protein kinase Akt. Science. 275:1997;661-665.
12. Datta SR, Dudek H, Tao X, Masters S, Fu H, Gotoh Y, Greenberg ME. Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery. Cell. 91:1997;231-241.
13. Merry DE, Korsmeyer SJ. BCL-2 gene family in the nervous system. Annu Rev Neurosci. 20:1997;245-267.
14. Michaelidis TM, Sendtner M, Cooper JD, Airaksinen MS, Holtmann B, Meyer M, Thoenen H. Inactivation of bcl-2 results in progressive degeneration of motoneurons, sympathetic and sensory neurons during early postnatal development. Neuron. 17:1996;75-89.
15. Motoyama N, Wang F, Roth KA, Sawa H, Nakayama K, Nakayama K, Negishi I, Senju S, Zhang Q, Fujii S, Loh DY. Massive cell death of immature hematopoietic cells and neurons in Bcl-x-deficient mice. Science. 270:1995;96-99.
16. Deckwerth TL, Elliott JL, Knudson CM, Johnson EM Jr, Snider WD, Korsmeyer SJ. BAX is required for neuronal death after trophic factor deprivation and during development. Neuron. 17:1996;401-411.
17. Furukawa K, Estus S, Fu W, Mark RJ, Mattson MP. Neuroprotective action of cyclohexamide involves induction of bcl-2 and antioxidant pathways. J Cell Biol. 136:1997;1137-1149.
18. Iwahashi H, Eguchi Y, Yasuhara N, Hanafusa T, Matsuzawa Y, Tsujimoto Y. Synergy between Bcl-2 and SMN. of special interest Nature. 1997; Using a yeast two-hybrid screen, this work identifies SMN, a protein mutated in SMA patients, as a BCL-2-binding protein. SMN and BCL-2 function synergistically to block cell death. This paper links a motor neuorn degenerative disorder to BCL-2 activity and assigns SMN a new function.
19. Fischer U, Liu Q, Dreyfuss G. The smn-sip1 complex has an essential role in spliceosomal snRNP biogenesis. Cell. 90:1997;1023-1029.
20. Liu Q, Fischer U, Wang F, Dreyfuss G. The spinal muscular atrophy disease gene product, smn, and its associated protein sip1 are in a complex with spliceosomal snRNP proteins. Cell. 90:1997;1013-1021.
21. Minn AJ, Velez P, Schendel SL, Liang H, Muchmore SW, Fesik SW, Fill M, Thompson CB. Bcl-X(L) forms an ion channel in synthetic lipid membranes. Nature. 385:1997;353-357.
22. Schendel SL, Xie ZH, Montal MO, Matsuyama S, Montal M, Reed JC. Channel formation by antiapoptotic protein Bcl-2. Proc Natl Acad Sci USA. 4:1997;5113-5118.
23. Antonsson B, Conti F, Ciavatta A, Montessuit S, Lewis S, Martinou I, Bernasconi L, Bernard A, Mermod JJ, Mazzei G, et al. Inhibition of Bax channel-forming activity by Bcl-2. Science. 277:1997;370-372.
24. Yang J, Liu X, Bhalla K, Kim CN, Ibrado AM, Cai J, Peng T-I, Jones DP, Wang X. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science. 275:1997;1129-1132.
25. Chinnaiyan AM, O'Rourke K, Lane BR, Dixit VM. Interaction of CED-4 with CED-3 and CED-9: a molecular framework for cell death. of special interest Science. 275:1997;1122-1126 See annotation [29].
26. Spector MS, Desnoyers S, Hoeppener DJ, Hengartner MO. Interaction between the C-elegans cell-death regulators Ced-9 and Ced-4. of special interest Nature. 385:1997;653-656 See annotation [29].
27. Irmler M, Hofmann K, Vaux D, Tschopp J. Direct physical interaction between the Caenorhabditis elegans 'death proteins' CED-3 and CED-4. of special interest FEBS Lett. 406:1997;189-190 See annotation [29].
28. Wu D, Wallen HD, Nunez G. Interaction and regulation of subcellular localization of CED-4 by CED-9. of special interest Science. 275:1997;1126-1129 See annotation [29].
29. Wu D, Wallen HD, Inohara N, Nunez G. Interaction and regulation of the Caenorhabditis elegans death protease CED-3 by CED-4 and CED-9. of special interest J Biol Chem. 272:1997;21449-21454 These five papers [25-29] describe physical interactions between CED-9, CED-4 and CED-3. This is the first evidence that BCL-2 proteins directly regulate caspases via CED-4.
30. Seshagiri S, Miller LK. Caenorhabditis elegans CED-4 stimulates CED-3 processing and CED-3-induced apoptosis. of outstanding interest Curr Biol. 7:1997;455-460 The authors transiently expressed ced-9, ced-4 and ced-3 to study their interactions and functions. This is the first report indicating that CED-4 stimulates CED-3 processing to generate an active caspase and induce apoptosis. This study confirms that CED-4 is regulated by interacting with CED-9.
31. Chinnaiyan AM, Chaudhary D, O'Rourke K, Koonin EV, Dixit VM. Role of Ced-4 in the activation of Ced-3. of special interest Nature. 388:1997;728-729 This paper shows that CED-4 catalyses CED-3 processing in vitro and that ATP is required for this process; thus, providing a direct functional link between CED-4 and CED-3.
32. Zou H, Henzel WJ, Liu XS, Lutschg A, Wang XD. Apaf-1, a human protein homologous to C-elegans Ced-4, participates in cytochrome C-dependent activation of caspase-3. of outstanding interest Cell. 90:1997;405-413 This group uses an elegant biochemical system to purify proteins essential for caspase-3 activation from cytosolic extracts. They identified a protein with homology to CED-4 as one of the three components necessary to mediate processing of caspase-3 in vitro.
33. Li P, Nijhawan D, Budihardjo I, Srinivasula S, Ahmad M, Alnemri E, Wang X. Cytochrome c and dATP-dependent formation of Apaf-1/Caspase-9 complex initiates an apoptotic protease cascade. of special interest Cell. 91:1997;479-489 This study directly links a specific caspase with the ced-4 homologue. Apaf-1. It provides a molecular mechanisms for the activation of caspases by CED-4 homologues.
34. Nicholson DW, Thornberry NA. Caspases - killer proteases. Trends Biochem Sci. 22:1997;299-306.
35. Cohen GM. Caspases - the executioners of apoptosis. Biochem J. 326:1997;1-16.
36. Kuida K, Zheng TS, Na S, Kuan C, Yang D, Karasuyama H, Rakic P, Flavell RA. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature. 384:1996;368-372.
37. Devereaux QL, Takahashi R, Salvesen GS, Reed JC. X-linked IAP is a direct inhibitor of cell-death proteases. Nature. 388:1997;300-304.
38. Roy N, Mahadevan MS, McLean M, Shutler G, Yaraghi Z, Farahani R, Baird S, Besner-Johnston A, Lefebvre C, Kang X, et al. The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy. Cell. 80:1995;167-178.
39. Srinivasan A, Foster LM, Testa MP, Ord T, Keane RW, Bredesen DE, Kayalar C. Bcl-2 expression in neural cells blocks activation of Ice/Ced-3 family proteases during apoptosis. J Neurosci. 16:1996;5654-5660.
40. Deshmukh M, Vasilakos J, Deckwerth TL, Lampe PA, Shivers BD, Johnson EM Jr. Genetic and metabolic status of NGF-deprived sympathetic neurons saved by an inhibitor of ICE family proteases. of special interest J Cell Biol. 135:1996;1341-1354 Caspases inhibitors that block sympathetic neuron apoptosis triggered by NGF withdrawal act downstream of cyclohexamide. Activation of caspases marks the death commitment point at which neurons can no longer be rescued by NGF. This well-characterized experimental paradigm of neuronal apoptosis allows the ordering of the molecular events leading to death.
41. Troy CM, Stefanis L, Prochiantz A, Greene LA, Shelanski ML. The contrasting roles of ICE family proteases are interleukin-1beta in apoptosis induced by trophic factor withdrawal and by copper/zinc superoxide dismutase down-regulation. Proc Natl Acad Sci USA. 93:1996;5635-5640.
42. Troy CM, Stefanis L, Greene LA, Shelanski ML. Nedd2 is required for apoptosis after trophic factor withdrawal, but not superoxide dismutase (SOD1) downregulation, in sympathetic neurons and PC12 cells. J Neurosci. 17:1997;1911-1918.
43. Haass C. Presenilins: genes for life and death. Neuron. 18:1997;687-690.
44. Borchelt DR, Thinakaran G, Eckman CB, Lee MK, Davenport F, Ratovitsky T, Prada CM, Kim G, Seekins S, Yager D, et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Abeta1-42/1-40 ratio in vitro and in vivo. of special interest Neuron. 17:1996;1005-1013 See annotation [47].
45. Citron M, Westaway D, Xia W, Carlson G, Diehl T, Levesque G, Johnson-Wood K, Lee M, Seubert P, Davis A, et al. Mutant presenilins of Alzheimer's disease increase production of 42-residue amyloid beta-protein in both transfected cells ad transgenic mice. of special interest Nat Med. 3:1997;67-72 See annotation [47].
46. Duff K, Eckman C, Zehr C, Yu X, Prada CM, Perez-tur J, Hutton M, Buee L, Harigaya Y, Yager D, et al. Increased amyloid-beta42(43) in brains of mice expressing mutant presenilin 1. of special interest Nature. 383:1996;710-713 See annotation [47].
47. Tomita T, Maruyama K, Saido TC, Kume H, Shinozaki K, Tokuhiro S, Capell A, Walter J, Grunberg J, Haas C, et al. The presenilin 2 mutation (N1411) linked to familial Alzheimer disease (Volga German families) increases the secretion of amyloid beta protein ending at the 42nd (or 43rd) residue. of special interest Proc Natl Acad Sci USA. 94:1997;2025-2030 These four papers [44-47] link the two known causative factors of Alzheimer's disease: amyloid and presenilins. Presenilin mutations associated with familial Alzheimer's disease increase the production of Aβ42 in transgenic animals and cells.
48. Weidemann A, Paliga K, Durrwang U, Czech C, Evin G, Masters CL, Beyreuther K. Formation of stable complexes between two Alzheimer's disease gene products: presenilin-2 and beta-amyloid precursor protein. Nat Med. 3:1997;328-332.
49. Wolozin B, Iwasaki K, Vito P, Ganjei JK, Lacana E, Sunderland T, Zhao BY, Kusiak JW, Wasco V, Dadamio L. Participation of presenilin 2 in apoptosis - enhanced basal activity conferred by an Alzheimer mutation. of outstanding interest Science. 274:1996;1710-1713 PS2 antisense conferred protection against neuronal apoptosis induced by NGF deprivation of or βAPP expression. PS2 mutations linked to FAD generated a protein with apoptotic activity.
50. Vito P, Wolozin B, Ganjei JK, Iwasaki K, Lacana E, Dadamio L. Requirement of the familial Alzheimer's disease gene PS2 for apoptosis - opposing effect of ALG-3. of outstanding interest J Biol Chem. 271:1996;31025-31028 This work identifies a truncated 10 kDa PS2 carboxy-terminal fragment that acts as a dominant-negative of PS2 to protect T cells from Fas-induced apoptosis and PC12 cells from NGF-deprivation-induced death.
51. Kim TW, Pettingell WH, Yung YK, Kovacs DM, Tanzi RE. Alternative cleavage of Alzheimer-associated presenilins during apoptosis by a caspase-3 family protease. of outstanding interest Science. 277:1997;373-376 This study links caspases to Alzheimer's disease by describing how presenilin-bearing FAD mutations are cleaved by caspase-3. Alternative processing generates a carboxy-terminal fragment that is able to elevate Aβ42 release as well as apoptosis.
52. Golberg YP, Nicholson DW, Rasper DM, Kalchman MA, Koide HB, Graham RK, Bromm M, Kazemi-Esfarjani P, Thornberry NA, Vaillancourt JP, Hayden MR. Cleavage of huntingtin by apopain, a proapoptotic cysteine protease, is modulated by the polyglutamine tract. Nat Gen. 13:1996;442-449.
53. Martinou J-C, Dubois-Dauphin M, Staple JK, Rodriguez I, Frankowski M, Missotten M, Albertini P, Talabot D, Catsicas S, Pietra C, Juarte J. Overexpression of Bcl-2 in transgenic mice protects neurons from naturally occurring cell death and experimental ischemia. Neuron. 13:1994;1017-1030.
54. Friedlander RM, Gagliardini V, Hara H, Fink KB, Li W, MacDonald G, Fishman MC, Greenberg AH, Moskowitz MA, Yuan J. Expression of a dominant negative mutant of interleukin-1 beta converting enzyme in transgenic mice prevents neuronal cell death induced by trophic factor withdrawal and ischemic brain injury. J Exp Med. 185:1997;933-940.
55. Hara H, Friedlander RM, Gangliardini V, Ayata C, Fink K, Huang Z, Shimizu-Sasamata M, Yuan J, Moskowitz MA. Inhibition of interleukin 1beta converting enzyme family proteases reduces ischemic and excitotoxic neuronal damage. Proc Natl Acad Sci USA. 94:1997;2007-2012.
56. Coulpier M, Junier MP, Peschanski M, Dreyfus PA. Bcl-2 sensitivity differentiates two pathways for motoneuronal death in the wobbler mutant mouse. J Neurosci. 16:1996;5897-5904.
57. Bruijn LI, Becher MW, Lee MK, Anderson KL, Jenkins NA, Copeland NG, Sisodia SS, Rothstein JD, Borchelt DR, Price DL, Cleveland DW. ALS-linked SOD1 mutant G85R mediates damage to astrocytes and promotes rapidly progressive disease with SOD1-containing inclusions. Neuron. 18:1997;327-338.
58. Kostic V, Jackson-Lewis V, de Bilbao F, Dubois-Dauphin M, Przedborski S. Bcl-2: prolonging life in transgenic mouse model of familial amyotrophic lateral sclerosis. of special interest Science. 277:1997;559-562 This is the first successful attempt at using BCL-2 to delay symptoms of motor neuron degeneration caused by a neurological disorder. This work also indicates that BCL-2 acts early in the apoptotic pathway, before c-Jun expression increases.
59. Friedlander RM, Brown RH, Gangliardini V, Wang J, Yuan JY. Inhibition of ICE slows ALS in mice. Nature. 388:1997;31.