45
Views
450
CrossRef citations to date
0
Altmetric
Cell Growth and Development

NF-κB Induces Expression of the Bcl-2 Homologue A1/Bfl-1 To Preferentially Suppress Chemotherapy-Induced Apoptosis

, , &
Pages 5923-5929 | Received 18 Mar 1999, Accepted 09 Jun 1999, Published online: 27 Mar 2023

REFERENCES

  • Adams, J., and J. Cory 1998. The Bcl-2 protein family: arbiters of cell survival. Science 281:1322–1326.
  • Ashkenazi, A., and J. Dixit 1998. Death receptors: signaling and modulation. Science 281:1305–1308.
  • Baeuerle, P. A., and J. Baltimore 1996. NF-κB: ten years after. Cell 87:13–20.
  • Baker, S., and J. Reddy 1998. Modulation of life and death by the TNF receptor superfamily. Oncogene 25:3261–3270.
  • Baldwin, A. S. 1996. The NF-κB and IκB proteins: new discoveries and insights. Annu. Rev. Immunol. 14:649–681.
  • Beg, A. A., and J. Baltimore 1996. An essential role for NF-κB in preventing TNF-α-induced cell death. Science 274:782–784.
  • Boise, L. H., and J. Thompson 1997. Bcl-xL can inhibit apoptosis in cells that have undergone Fas-induced protease activation. Proc. Natl. Acad. Sci. USA 94:3759–3763.
  • Boothby, M. R., A. Mora, D. Scherer, J. Brockman, and J. Ballard 1997. Perturbation of the T lymphocyte lineage in transgenic mice expressing a constitutive repressor of nuclear factor (NF)-kappaB. J. Exp. Med. 185:1897–1907.
  • Bradham, C., T. Qian, K. Streetz, C. Trautwein, D. Brenner, and J. LeMasters 1998. The mitochondrial permeability transition is required for tumor necrosis factor alpha-mediated apoptosis and cytochrome c release. Mol. Cell. Biol. 18:6353–6364.
  • Chao, D. T., and J. Korsmeyer 1998. Bcl-2 family: regulators of cell death. Annu. Rev. Immunol. 16:395–419.
  • Chu, Z. L., T. McKinsey, L. Liu, J. Gentry, M. Malim, and J. Ballard 1997. Suppression of tumor necrosis factor-induced cell death by inhibitor of apoptosis c-IAP2 is under NF-κB control. Proc. Natl. Acad. Sci. USA 94:10057–10062.
  • Chuang, P., E. Yee, A. Karsan, R. Winn, and J. Harlan 1998. A1 is a constitutive and inducible Bcl-2 homologue in mature human neutrophils. Biochem. Biophys. Res. Commun. 249:361–365.
  • Clem, R. J., and J. Duckett 1997. The iap genes: unique arbitrators of cell death. Trends Cell Biol. 7:337–339.
  • Datta, R., D. Banach, H. Kojima, R. Talanian, E. Alnemri, W. Wong, and J. Kufe 1996. Activation of the CPP32 protease in apoptosis induced by Ara-C and other DNA-damaging agents. Blood 86:1936–1943.
  • Deveraux, Q., N. Roy, H. Stennicke, T. Van Arsdale, Q. Zhou, S. Srinivasula, E. Alnemri, G. Salvesen, and J. Reed 1998. IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. EMBO J. 17:2215–2223.
  • Deveraux, Q., and J. Reed 1999. IAP family proteins—suppressors of apoptosis. Genes Dev. 13:239–252.
  • Dragovich, T., C. Rudin, and J. Thompson 1998. Signal transduction pathways that regulate cell survival and cell death. Oncogene 25:3207–3214.
  • D’Sa-Eipper, C., T. Subramanian, and J. Chinnadurai 1996. Bfl-1, a Bcl-2 homologue, suppresses p53-induced apoptosis and exhibits potent cooperative transforming activity. Cancer Res. 56:3879–3882.
  • D’Sa-Eipper, C., and J. Chinnadurai 1998. Functional dissection of Bfl-1, a Bcl-3 homolog: anti-apoptosis, oncogene-cooperation and cell proliferation activities. Oncogene 16:3105–3114.
  • Duckett, C. S., V. Nava, R. Gedrich, R. Clem, J. Van Dongen, M. Gilfillan, H. Shiels, J. Hardwick, and J. Thompson 1996. A conserved family of cellular genes related to the baculovirus iap gene and encoding apoptosis inhibitors. EMBO J. 15:2685–2694.
  • Duckett, C. S., F. Li, Y. Wang, K. J. Tomaselli, C. B. Thompson, and J. Armstrong 1997. Human IAP-like protein regulates programmed cell death downstream of Bcl-xL and cytochrome c . Mol. Cell. Biol. 18:608–615.
  • Ghosh, S., M. May, and J. Kopp 1998. NF-κB and rel proteins: evolutionarily conserved mediators of immune responses. Annu. Rev. Immunol. 16:225–260.
  • Green, D., and J. Reed 1998. Mitochondria and apoptosis. Science 281:1309–1312.
  • Gross, A., X. Yin, K. Wang, M. Wei, J. Jockel, C. Milliman, H. Erdjument-Bromage, P. Tempst, and J. Korsmeyer 1999. Caspase cleaved BID targets mitochondria and is required for cytochrome c release, while Bcl-xL prevents this release but not tumor necrosis factor-R1/Fas death. J. Biol. Chem. 274:1156–1163.
  • Grumont, R., I. J. Rourke, and J. Gerondakis 1999. Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis. Gene Dev. 13:400–411.
  • Hakem, R., A. Hakem, G. S. Duncan, J. T. Henderson, M. Woo, M. S. Soengas, A. Elisa, J. Pompa, D. Kagi, W. Khoo, J. Potter, R. Yoshida, S. A. Kaufman, S. W. Lowe, J. M. Penninger, and J. Mak 1998. Differential requirement for caspase-9 in apoptotic pathways in vivo. Cell 94:339–352.
  • Hu, Y., M. Benedict, D. Wu, N. Inohara, and J. Nunez 1998. Bcl-xL interacts with Apaf-1 and inhibits Apaf-1 dependent caspase-9 activation. Proc. Natl. Acad. Sci. USA 95:4386–4391.
  • Karsan, A., E. Yee, M. Kaushansky, and J. Harlan 1996. Cloning of a human Bcl-2 homologue: inflammatory cytokines induce human A1 in cultured endothelial cells. Blood 87:3089–3096.
  • Karsan, A., E. Yee, and J. Harlan 1996. Endothelial cell death induced by TNFα is inhibited by the Bcl-2 homologue, A1. J. Biol. Chem. 271:27201–27204.
  • Kasibhatla, S., L. Genestier, and J. Green 1999. Regulation of Fas-ligand expression during activation-induced cell death in T lymphocytes via nuclear factor κB. J. Biol. Chem. 274:987–992.
  • Kluck, R. M., E. Bossy-Wetzel, D. R. Green, and J. Newmeyer 1997. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science 275:1132–1136.
  • Kuida, K., T. Haydar, C. Kuan, Y. Gu, C. Taya, H. Karasuyama, M. Su, P. Rakic, and J. Flavell 1998. Reduced apoptosis and cytochrome c-mediated caspase activation in mice lacking caspase 9. Cell 94:325–337.
  • Li, H., H. Zhu, C.-J. Xu, and J. Yuan 1998. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94:491–501.
  • Li, P., D. Nijhawan, I. Budihardjo, S. Srinivasula, M. Ahmad, E. Alnemri, and J. Wang 1996. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell 91:479–489.
  • Lin, E. Y., A. Orlofsky, H. Wang, J. C. Reed, and J. Prystowsky 1996. A1, a Bcl-2 family member, prolongs cell survival and permits myeloid differentiation. Blood 87:983–992.
  • Liu, X., C. N. Kim, J. Yang, R. Jemmerson, and J. Wang 1996. Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86:147–157.
  • Liu, X., H. Zou, C. Slaughter, and J. Wang 1997. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89:175–184.
  • Liu, Z.-G., H. Hsu, D. V. Goeddel, and J. Karin 1996. Dissection of TNF receptor 1 effector function: JNK activation is not linked to apoptosis while NF-κB activation prevents cell death. Cell 87:565–576.
  • Luo, X., I. Budihardjo, H. Zou, C. Slaughter, and J. Wang 1998. Bid, a Bcl-2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94:481–490.
  • Mayo, M. W., C.-Y. Wang, P. C. Cogswell, K. S. Rogers-Graham, S. W. Lowe, C. J. Der, and J. Baldwin 1997. Requirement of NF-κB activation to suppress p53-independent apoptosis induced by oncogenic Ras. Science 278:1812–1815.
  • Nicholson, D. W., and J. Thornberry 1997. Caspase: killer proteases. Trends Biochem. Sci. 22:299–306.
  • Opipari, A. W., H. Hu, R. Yabkowitz, and J. Dixit 1992. The A20 zinc finger protein protects cell from tumor nectosis factor cytotoxicity. J. Biol. Chem. 267:12424–12427.
  • Pan, G., K. O’Rourke, and J. Dixit 1998. Caspase-9, Bcl-xL and Apaf-1 form a ternary complex. J. Biol. Chem. 273:5841–5845.
  • Reed, J. C. 1997. Double identity for proteins of the Bcl-2 family. Nature 387:773–776.
  • Reed, J. C. 1998. Bcl-2 family proteins. Oncogene 25:3225–3236.
  • Rosse, T., R. Olivier, L. Monney, M. Rager, S. Conus, I. Fellay, B. Jansen, and J. Borner 1998. Bcl-2 prolongs cell survival after Bax-induced release of cytochrome c. Nature 391:496–499.
  • Roy, N., Q. Deveraux, R. Takashashi, G. Salvesen, and J. Reed 1999. The c-IAP1 and 2 proteins are direct inhibitors of specific caspases. EMBO J. 16:6914–6925.
  • Salvesen, G., and J. Dixit 1997. Caspases: intracellular signaling by proteolysis. Cell 91:443–446.
  • Scaffidi, C., S. Fulda, A. Srinivasan, C. Friesen, F. Li, K. Tomaselli, K. Debatin, P. Krammer, and J. Peter 1998. Two CD95 (Apo-1/Fas) signaling pathways. EMBO J. 17:1675–1687.
  • Stehlik, C., R. de Martin, I. Kumabashiri, J. Schmid, B. Binder, and J. Lipp 1998. NF-κB-regulated XIAP gene expression protects endothelial cells from TNFα-induced apoptosis. J. Exp. Med. 188:211–216.
  • Stennicke, H., J. Jurgensmeier, H. Shin, Q. Devereaux, B. Wolf, X. Yang, Q. Zhou, H. Ellerby, L. Ellerby, D. Bredesen, D. Green, J. Reed, C. Froelich, and J. Salvesen 1998. Pro-caspase-3 is a major physiologic target of caspase-8. J. Biol. Chem. 273:27084–27090.
  • Susin, S. A., N. Zamzami, M. Castedo, E. Daugas, H. Wang, S. Geley, F. Fassy, J. C. Reed, and J. Kroemer 1997. The central executioner of apoptosis: multiple connections between protease activation and mitochondria in Fas/APO-1/CD95- and ceramide-induced apoptosis. J. Exp. Med. 186:25–37.
  • Thompson, C. 1995. Apoptosis in the pathogenesis and treatment of cancer. Science 267:1456–1462.
  • Thornberry, N., and J. Lazebnik 1998. Caspases: enemies within. Science 281:1312–1316.
  • Van Antwerp, D. J., S. Martin, T. Kafri, D. R. Green, and J. Verma 1996. Suppression of TNF-α-induced apoptosis by NF-κB. Science 274:787–789.
  • Varfolomeev, E., M. Schuchmann, V. Luria, N. Chiannilkulchai, J. Beckmann, I. Mett, D. Rebrikov, V. Brodianski, O. Kemper, O. Kollet, T. Lapidot, D. Soffer, T. Sobe, K. Avraham, T. Goncharov, H. Holtmann, P. Lonai, and J. Wallach 1998. Targeted disruption of the mouse caspase 8 gene ablates cell death induction by the TNF receptorsm /Fas/Apo1, and DR3 is lethal prenatally. Immunity 9:267–278.
  • Wang, C.-Y., M. Mayo, and J. Baldwin 1996. TNF- and cancer therapy-induced apoptosis potentiation by inhibition of NF-κB. Science 274:784–787.
  • Wang, C.-Y., M. W. Mayo, R. C. Korneluk, D. V. Goeddel, and J. Baldwin 1998. NF-κB antiapoptosis: induction of TRAF1 and TRAF2 and c-IAP1 and c-IAP2 to suppress caspase-8 activation. Science 281:1680–1683.
  • Wang, H. G., U. R. Rapp, and J. Reed 1996. Bcl-2 targets the protein kinase Raf-1 to mitochondria. Cell 87:629–638.
  • Woo, M., R. Hakem, M. Soengas, G. Duncan, A. Shahinian, D. Kagi, A. Hakem, M. McCurrach, W. Khoo, S. Kaufman, G. Senaldi, T. Howard, S. Lowe, and J. Mak 1998. Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev. 12:806–819.
  • Wu, M., H. Lee, R. Ballas, S. Schauer, M. Arsura, D. Katz, M. FitzGerald, T. Rothestein, D. Sherr, and J. Sonenshein 1996. Inhibition of NF-κB/Rel induces apoptosis of murine B cells. EMBO J. 15:4682–4690.
  • Wu, M. X., Z. Ao, K. V. S. Prasad, R. Wu, and J. Schlossman 1998. IEX-1L, an apoptosis inhibitor involved in NF-κB-mediated cell survival. Science 281:998–1001.
  • Yang, J., X. Liu, K. Bhalla, C. Kim, A. Ibrado, J. Cai, T.-I. Peng, D. Jones, and J. Wang 1997. Prevention of apoptosis by Bcl-2: release of cytochrome c from mitochondria blocked. Science 275:1129–1132.
  • Zamzami, N., S. Susin, P. Marchetti, T. Hirsch, I. Gomez-Monterey, M. Castedo, and J. Kroemer 1996. Mitochondrial control of nuclear apoptosis. J. Exp. Med. 183:1523–1544.
  • Zha, J., H. Hirashi, E. Yang, J. Jockel, and J. Korsmeyer 1996. Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-xL. Cell 87:619–628.
  • Zong, W., L. C. Edelstein, C. Chen, J. Bash, and J. Gélinas 1999. The prosurvival Bcl-2 homolog Bfl-1/A1 is a direct transcriptional target of NF-B that blocks TNF-induced apoptosis. Genes Dev. 13:382–387.
  • Zou, H., W. Henzel, X. Liu, A. Lutschg, and J. Wang 1997. Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3. Cell 90:405–413.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.