A caspase-3-like protease is involved in NF-κB activation induced by stimulation of N-methyl-d-aspartate receptors in rat striatum

Molecular Brain Research

Volumn 80, Issue 2, 2000, Pages 111-122

  Qin, Zheng Hong ^a   Wang, Yumei ^a   Chasea, Thomas N ^a  

^a NATIONAL INSTITUTE OF NEUROLOGICAL DISORDERS AND STROKE   (United States)

Author keywords

Ac DEVD CHO; Apoptosis; Caspase 3; I B ; MG 132; NF B; Proteasome

Indexed keywords

CASPASE 3; EXCITATORY AMINO ACID RECEPTOR; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; N METHYL DEXTRO ASPARTIC ACID RECEPTOR; PROTEINASE;

ANIMAL TISSUE; APOPTOSIS; ARTICLE; CORPUS STRIATUM; ENZYME ACTIVATION; ENZYME ACTIVITY; NEUROTOXICITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT; RECEPTOR BINDING;

ANIMALS; APOPTOSIS; CASPASE 3; CASPASES; CORPUS STRIATUM; CYSTEINE ENDOPEPTIDASES; CYSTEINE PROTEINASE INHIBITORS; DNA FRAGMENTATION; DNA-BINDING PROTEINS; ENZYME ACTIVATION; I-KAPPA B PROTEINS; LEUPEPTINS; MALE; MULTIENZYME COMPLEXES; NEURONS; NF-KAPPA B; NUCLEOSOMES; OLIGOPEPTIDES; PROTEASOME ENDOPEPTIDASE COMPLEX; QUINOLINIC ACID; RATS; RATS, SPRAGUE-DAWLEY; RECEPTORS, N-METHYL-D-ASPARTATE; TRANSCRIPTION FACTOR AP-1;

ANIMALIA;

EID: 0034665797     PISSN: 0169328X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-328X(00)00147-9     Document Type: Article

References (64)

1. Alkalay I., Yaron A., Hatzubai A., Orian A., Ciechanover A., Ben-Neriah Y. Stimulation dependent IκBα phosphorylation marks the NF-κB inhibitor for degradation via the ubiquitin proteasome pathway. Proc. Natl. Acad. Sci. USA. 92:1995;10599-10603.
2. Ankarcrona M., Dypbukt J.M., Bonfoco E., Zhivotovsky B., Orrenius S., Lipton S.A., Nicotera P. Glutamate-induced neuronal death: A succession of necrosis or apoptosis dependent on mitochondrial function. Neuron. 15:1995;961-973.
3. Baeuerle P.A. The inducible transcription activator NF-κB: regulation by distinct protein subunits. Biochem. Biophy. Acta. 107:1991;63-80.
4. Baeuerle P.A., Henkel T. Function and activation of NF-κB in the immune system. Ann. Rev. Immunol. 12:1994;141-179.
5. Baeuerle P.A., Baltimore D. NF-κB: ten years after. Cell. 87:1996;13-20.
6. Barkett M., Xue D., Horvitz H.R., Gilmore T.D. Phosphorylation of IκB-α inhibits its cleavage by caspase CPP32 in vitro. J. Biol. Chem. 272:1997;29419-29422.
7. Barnes J.M., Henley J.M. Molecular characteristics of excitatory amino acid receptors. Prog. Neurobiol. 39:1992;113-133.
8. Beg A.A., Finco T.S., Nantermet P.V., Baldwin A.S. Jr. Tumor necrosis factor and interleukin-1 lead to phosphorylation and loss of IκBα: a mechanism for NF-κB activation. Mol. Cell. Biol. 13:1993;3301-3310.
9. Boland M.P., O'Neil L.A.J. Ceramide activates NFêB by inducing the processing of p105. J. Biol. Chem. 273:1998;15494-15500.
10. Bonfoco E., Krainc D., Ankarcrona M., Nicotera P., Lipton S.A. Apoptosis and necrosis: Two distinct events induced, respectively, by mild and intense insults with N-methyl-D-aspartate or nitric oxide/superoxide in cortical cell cultures. Proc. Natl. Acad. Sci. USA. 92:1995;7162-7166.
11. Brown K., Gerstberger S., Carlson L., Franzoso G., Siebenlist U. Control of IκB-α proteolysis by site-specific, signal-induced phosphorylation. Science. 267:1995;1485-1488.
12. Canty T.G., Boyle E.M., Farr A., Morgan E.N., Verrier E.D., Pohlman T.H. Oxidative stress induces NF-kappaB nuclear translocation without degradation of Ikappaalpha. Circulation. 100 (suppl):1999;II361-II364.
13. Chen F., Lu Y., Kukn D.C., Maki M., Shi X., Sun S-C., Demers L.M. Calpain contributes to silica-induced IκB-α degradation and nuclear factor êB activation. Archives Biochem. Biophy. 342:1997;383-388.
14. Cheng E.H-Y., Kirsch D.G., Clem R.J., Ravi R., Kastan M.B., Bedi A., Ueno K., Hardwick J.M. Conversion of Bcl-2 to a Bax-like death effector by caspases. Science. 278:1997;1966-1968.
15. Choi D.W. Excitotoxic cell death, J. Neurobiol. 23:1992;1261-1276.
16. Dai R-W., Chen E., Longgo D.L., Gorbea C.M., Li C-CH. Involvement of Valosin-containing protein, an ATPase co-purified with IκB and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IκBα J. Biol. Chem. 273:1998;3562-3573.
17. Darmon A.J., Ley T.J., Nicholson D.W., Bleackley R.C. Cleavage of CPP32 by granzyme B represents a critical role of granzyme B in the induction of target cell DNA fragmentation. J. Biol. Chem. 271:1996;21709-21712.
18. Datta R., Kojima H., Yoshida K., Kufe D. Caspase-3-mediated cleavage of protein kinase Cq in induction of apoptosis. J. Biol. Chem. 272:1997;20317-20320.
19. DiDonato J.A., Mercurio F., Karin M. Phosphorylation of IκBα precedes but not sufficient for its dissociation from NF-κB. Mol. Cell. Biol. 15:1995;1302-1311.
20. Doerre S., Corley R.B. Constitutive nuclear translocation of NF-kappa B in B cells in the absence of I kappa degradation. J. Immunol. 163:1999;269-277.
21. Du Y., Bales K.R., Dodel R.C., Hamilton-Byrd E., Horn J.W., Czilli D.L., Simmons L.K., Ni B., Paul S.M. Activation of a caspase 3-related cysteine protease is required for glutamate-mediated apoptosis of cultured cerebellar granule neurons. Proc. Natl. Acad. Sci. USA. 94:1997;11657-11662.
22. Faleiro L., Kobayashi R., Fearnhead H., Lazebnik Y. Multiple species of CPP-32 and Mch2 are the major active caspase present in apoptotic cells. EMBO J. 16:1997;2271-2281.
23. Grilli M., Pizzi M., Memo M., Spano P. Neuroprotection by aspirin and sodium salicylate through blockade of NF-κB activation. Science. 274:1996;1383-1385.
24. Grimm S., Baeuerle P.A. The inducible transcription factor NF-κB: structure-function relationship of its protein subunits. Biochem. J. 290:1993;297-308.
25. Guerrini L., Blast F., Denis-Donini S. Synaptic activation of NF-κB by glutamate in cerebellar granule neurons in vitro. Proc. Natl. Acad. Sci. USA. 92:1995;9077-9081.
26. Guerrini L., Molteni A., Wirth T., Kistler B., Blasi F. Glutamate-dependent activation of NF-κB during mouse cerebellum development. J. Neurosci. 17:1997;6057-6063.
27. Jänicke R.U., Ng P., Sprengart M.L., Porter A.G. Caspase-3 is required for α-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. J. Biol. Chem. 273:1998;15540-15545.
28. Kaltschmidt C., Kaltschmidt B., Baeuerle P.A. Brain synapses contain inducible forms of the transcription factor NF-κB. Mech. Dev. 43:1993;135-147.
29. Kaltschmidt C., Kaltschmidt B., Neumann H., Wekerle H., Baeuerle P.A. Constitutive NF-κB activity in neurons. Mol. Cell. Biol. 14:1994;3981-3992.
30. Kaltschmidt C., Kaltschmidt B., Baeuerle P.A. Stimulation of ionotropic glutamate receptors activates transcription factor NF-κB in primary neurons. Proc. Natl. Acad. Sci. USA. 92:1995;9618-9622.
31. Kaul N., Gopalakrishna R., Gundimeda U., Choi J., Forman H.J. Role of protein kinase C in basal and hydrogen peroxide-stimulated NF-κB activation in the murine macrophage J 774A1 cell line. Arch. Biochem. Biophy. 350:1998;79-86.
32. Kretz-Remy C., Bates E.E.M., Arrigo A.P. Amino acid analogs activate NF-κB through redox-dependent IκB degradation by the proteasome without apparent IκB-α phosphorylation. J. Biol. Chem. 273:1998;3180-3191.
33. Kuida K., Zheng T.S., Na S., Kuan C., Yang D., Karasuyama H., Rakic P., Flavell R.A. Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature. 384:1996;368-372.
34. Larm J.A., Cheung N.S., Beart P.M. Apoptosis induced via AMPA-selective glutamate receptors in cultured murine cortical neurons. J. Neurochem. 69:1997;617-622.
35. ffak and disassembly of focal adhesions in human endothelial cell apoptosis. J. Exp. Med. 187:1998;579-586.
36. Liu X., Kim C.N., Pohl J., Wang X. Purification and characterization of an interleukin-1β-converting enzyme family protease that activates cysteine protease p32 (CPP32). J. Biol. Chem. 271:1996;1337-13376.
37. Liu X., Zou H., Slaughter C., Wang X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell. 89:1997;175-184.
38. Maggirwar S.B., Harhaj E. S-C. Sun, Activation of NF-κB/Rel by Tax involves degradation of IκBα and is blocked by a proteasome inhibitor. Oncogene. 11:1995;993-998.
39. Mattson M.P., Goodman Y., Luo H., Fu W., Furukawa K. Activation of NF-κB protects hippocampal neurons against oxidative stress-induced apoptosis: evidence for induction of manganese superoxide dismutase and suppression of peroxynitrite production and protein tyrosine nitration. J. Neurosci. Res. 49:1997;681-697.
40. Mercurio F., Zhu H., Murray B.W., Shevchenko A., Bennett B.L., Li J.W., Young D.B., Barbosa M., Mann M., Manning A., Rao A. IKK-1 and IKK-2: cytokine-activated IκB kinases essential for NF-κB activation. Science. 278:1997;860-866.
41. Nakai M., Qin Z-H., Chen J-F., Wang Y., Chase T.N. Kainic acid-induced apoptosis in rat striatum is associated with NF-κB activation. J. Neurochem. 74:2000;647-658.
42. Nakai M., Qin Z-H., Wang Y., Chase T.N. NMDA and non-NMDA receptor-stimulated IκB-α degradation: Differential effects of the caspase-3 inhibitor DEVD·CHO, ethanol and free radical scavenger OPC-14117. Brain Res. 859:2000;207-216.
43. Natarajan K., Manna S.K., Chaturvedi M.M., Aggarwal B.B. Protein Tyrosine kinase inhibitors block tumor necrosis factor-induced activation of nuclear factor-κB, degradation of IκBα, nuclear translocation, and subsequent gene expression. Arch. Biochem. Biophy. 352:1998;59-70.
44. Ni B., Wu X., Su Y., Stephenson D., Smalstig E.B., Clements J., Paul S.M. Transient global forebrain ischemia induces a prolonged expression of the caspase-3 mRNA in rat hippocampal CA1 pyramidal neurons. J. Cereb. Blood Metab. 18:1998;248-256.
45. O'Neill L.A.J., Kaltschmidt C. NF-κB: a crucial transcription factor for glia and neuronal cell function. Trends Neurosci. 20:1997;252-258.
46. Piette J., Piret B., Bonizzi G., Schoonbroodt S., Merville M-P., Legrand-Poels S., Bours V. Multiple redox regulation in NF-κB transcription factor activation. J. Biol. Chem. 378:1997;1237-1245.
47. Qin Z-H., Wang Y., Chase T.N. Stimulation of N-Methyl-D-aspartate receptors induces apoptosis in rat brain. Brain Res. 725:1996;166-177.
48. Qin Z-H., Wang Y., Nakai M., Chase T.N. Transcription factor NF-κB contributes to excitotoxin-induced apoptosis. Mol. Pharmacol. 53:1998;33-42.
49. Qin Z-H., Chen R-W., Wang Y., Nakai M., Chuang D-M., Chase T.N. NF-κB nuclear translocation upregulates c-Myc and p53 expression during N-methyl-D-aspartate receptor mediated apoptosis in rat striatum. J. Neurosci. 19:1999;4023-4033.
50. Sahni S.K., Van Antwerp D.J., Eremeeva M.E., Silverman D.J., Marder V.J., Sporn L.A. Proteasome-independent activation of nuclear factor êB in cytoplasmic extracts from human endothelial cells by Rickettsia rickettsii. Infect. and Immun. 66:1998;1827-1833.
51. Schneider A., Maartin-Villalba A., Weih F., Vogel J., Wirth T., Schwaninger T.M. NF-κB is activated and promotes cell death in focal cerebral ischemia. Nat. Med. 5:1999;554-559.
52. Sen R., Baltimore D. Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell. 46:1986;705-716.
53. Siebenlist U., Franzoso G., Brown K. Structure, regulation and function of NF-κB. Ann. Rev. Cell Biol. 10:1994;405-455.
54. Siebenlist U. NF-κB/IκB proteins. Their role in cell growth, differentiation and development. Biochim. Biophy. Acta. 1332:1997;R7-R13.
55. Simonian N.A., Getz R.L., Leveque J.C., Konradi C., Coyle J.T. Kainate induces apoptosis in neurons. Neuroscience. 74:1996;675-683.
56. Slee E.A., Zhu H., Chow S.C., MacFarlane M., Nicholson D.W., Cohen G.M. Benzyloxycarbonyl-Val-Ala-Asp (OMe) fluoromethylketone (Z-VAD.FMK) inhibits apoptosis by blocking the processing of CPP32. Biochem. J. 315:1996;21-24.
57. Song Q., Lees-Miller S.P., Kumar S., Zhang N., Chan D.W., Smith G.C.M., Jackson S.P., Alnemri E.S., Litwack G., Khanna K.K., Lavin M.F. DNA-dependent protein kinase catalytic subunit: a target for an ICE-like protease in apoptosis. EMBO J. 15:1996;3238-3246.
58. Suzuki A., Iwasaki M., Wagai N. Involvement of cytoplasmic serine protease and CPP-32 subfamily in the molecular machinery of caspase 3 activation during Fas-mediated apoptosis. Exp. Cell Res. 233:1997;48-55.
59. Tewari M., Quan L.T., O'Rourke K., Desnoyers S., Zeng Z., Beidler D.R., Poirier G.G., Salvesen G.S., Dixit V.M. Yama/CPP32b, a mammalian homologue of CED-3, is a CrmA-inhibitable protease that cleaves the death substrate poly(ADP-ribose) polymerase. Cell. 81:1995;801-809.
60. Thanos D., Maniatis T. NF-κB: a lesson in family values. Cell. 80:1995;529-532.
61. Traenckner E.B-M., Wilk S., Baeuerle P.A. A proteasome inhibitor prevents activation of NF-κB and stabilizes a newly phosphorylated form of IκB-α that is still bound to NF-κB. EMBO J. 13:1994;5433-5441.
62. Traenckner E.B-M., Pahl H.L., Henkel T., Schmidt K.N., Wilk S., Baeuerle P.A. Phosphorylation of human IκB-α on serines 32 and 36 controls IκB-α proteolysis and NF-κB activation in response to diverse stimuli. EMBO J. 14:1995;2876-2883.
63. Yakovlev A.G., Knoblach S.M., Fan L., Fox G.B., Goodnight R., Faden A.I. Activation of CPP- 32-like caspases contributes to neuronal apoptosis and neurological dysfunction after traumatic brain injury. J. Neurosci. 17:1997;7415-7424.
64. Yu Z., Zhou D., Bruce-Keller A.J., Kindy M.S., Mattson M.P. Lack of the p50 subunit of nuclear factor-kappaB increases the vulnerability of hippocampal neurons to excitotoxic injury. J. Neurosci. 19:1999;8856-8865.