A trigger model of apoptosis induced by tumor necrosis factor signaling
详细信息 查看全文
- 作者：Chang Gu (1)
Junjie Zhang (2)
Yingyu Chen (3) (4)
Jinzhi Lei (5) - 刊名：BMC Systems Biology
- 出版年：2011
- 出版时间：December 2011
- 年：2011
- 卷：5
- 期：1-supp
- 全文大小：364KB
- 参考文献：1. Nagata S: Apoptosis by death factor. / Cell 1997, 88:355-65. CrossRef
2. Eissing T, Conzelmann H, Gilles ED, Allg?wer F, Bullinger E, Scheurich P: Bistability analyses of a caspase activation model for receptor-induced apoptosis. / J. Biol. Chem. 2004, 279:36892-6897. CrossRef
3. Hengartner MO: The biochemistry of apoptosis. / Nature 2000, 407:770-76. CrossRef
4. Vil?ek J, Lee TH: Tumor necrosis factor. New insights into the molecular mechanisms of its multiple actions. / J. Biol. Chem. 1991,266(12):7313-316.
5. Camussi G, Albano E, Tetta C, Bussolino F: The molecular action of tumor necrosis factor- α . / Eur. J. Biochem. 1991, 202:3-4. CrossRef
6. Scaffidi C, Fulda S, Srinivasan A, Friesen C, Li F, Tomaselli KJ, Debatin K, Krammer PH, Peter ME: Two CD95 (APO-1/Fas) signaling pathways. / EMBO J. 1998, 17:1675-687. CrossRef
7. Roberston JD, Orrenius S, Zhivotovsky B: Review: Nuclear events in apoptosis. / J. Struct. Biol. 2000, 129:346-58. CrossRef
8. Casciola-Rosen L, Nicholson DW, Chong T, Rowan KR, Thornberry NA, Miller DK, Rosen A: Apopain/CPP32 cleaves proteins that are essential for cellular repair: A fundamental principle of apoptotic death. / J. Exp. Med. 1996, 183:1957-964. CrossRef
9. Bagci EZ, Vodovotz Y, Billiar TR, Ermentrout GB, Bahar I: Bistability in apoptosis: Roles of Bax, Bcl-2, and mitochondrial permeability transition pores. / Biophysical Journal 2006, 90:1546-559. CrossRef
10. Bentele M, Lavrik I, Ulrich M, St??er S, Heermann DW, Kalthoff H, Krammer PH, Eils R: Mathematical modeling reveals threshold mechanism in CD95-induced apoptosis. / J. Cell Biol. 2004, 166:839-51. CrossRef
11. Fussenegger M, Bailey J, Varner J: A mathematical model of caspase function in apoptosis. / Nat. Biotech. 2000, 18:768-74. CrossRef
12. Hua F, Cornejo MG, Cardone MH, Stokes CL, Lauffenburger DA: Effects of Bcl-2 levels on Fas signaling-induced caspase-3 activation: molecular genetic tests of computational model predictions. / J. Immunol. 2005, 175:985-95.
13. Legewie S, Blüthgen N, Herzel H, Hanspeter H: Mathematical modeling identifies inhibitors of apoptosis as mediators of positive feedback and bistability. / PLoS Comp. Biol. 2006, 2:1061-073. CrossRef
14. Okazaki N, Asano R, Kinoshita T, Chuman H: Simple computational models of typeI/typeII cells in Fas signaling-induced apoptosis. / J. Theor. Biol. 2008, 250:621-33. CrossRef
15. Stucki J, Simon H: Mathematical modeling of the regulation of caspase-3 activation and degradation. / J. Theor. Biol. 2005, 234:123-31. CrossRef
16. Geske FJ, Lieberman R, Strange R, Gerschenson LE: Early stages of p53-induced apoptosis are reversible. / Cell Death Diff. 2001, 8:182-91. CrossRef
17. Rodriguez-Lafrasse C, Alphonse G, Broquet P, Aloy MT, Louisot P, Rousson R: Temporal relationships between ceramide production, caspase activation and mitochondrial dysfunction in cell lines with varying sensitivity to anti-Fas-induced apoptosis. / Biochem. J. 2001, 357:407-16. CrossRef
18. Tawa P, Hell K, Giroux A, Grimm E, Han Y, Nicholson DW, Xanthoudakis S: Catalytic activity of caspase-3 is required for its degradation: stabilization of the active complex by synthetic inhibitors. / Cell Death Diff. 2004, 11:439-47. CrossRef
19. Lazebnik YA, Kaufmann SH, Desnoyers S, Poirier GG, Earnshaw WC: Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. / Nature 1994, 371:346-47. CrossRef
20. Geske FJ, Nelson AC, Lieberman R, Strange R, Sun T, Gerschenson LE: DNA repair is activated in early stages of p53-induced apoptosis. / Cell Death Diff. 2000, 7:393-01. CrossRef
21. Boesen-de Cock JGR, Tepper AD, de Vries E, van Blitterswijk WJ, Borst J: Common regulation of apoptosis signaling induced by CD95 and the DNA-damaging stimuli etoposide and γ -Radiation downstream from caspase-8 activation. / J Biol Chem 1999, 274:14255-4261. CrossRef
22. Pitti RM, Marsters SA, Ruppert S, Donahue CJ, Moore A, Ashkenazi A: Induction of apoptosis by Apo-2 ligand, a new member of the tumor necrosis factor cytokine family. / J. Biol. Chem. 1996, 271:12687-2690. CrossRef
23. Seol DW, Li J, Seol M, Park MH, Park SY, Talanian R, Billiar TR: Signaling events triggered by Tumor Necrosis Factor-Related Apoptosis-inducing Ligand (TRAIL): Caspase-8 is required for TRAIL-induced apoptosis. / Cancer Res. 2001, 61:1138-143.
24. Wiley SR, Schooley K, Smolak PJ, Din WS, Huang CP, Nicholl JK, Sutherland GR, Smith TD, Rauch C, Smith CA, Goodwin RG: Identification and characterization of a new member of the TNF family that induces apoptosis. / Immunity 1995, 3:673-82. CrossRef
25. Hetz CA, Hunn M, Rojas P, Torres V, Leyton L, Quest AFG: Caspase-dependent initiation of apoptosis and necrosis by the Fas receptor in lymphoid cells: onset of necrosis is associated with delay ceremide increase. / J. Cell Sci. 2002, 115:4671-683. CrossRef
26. Deveraux QL, Takahashi R, Salvesen GS, Reed JC: X-linked IAP is a direct inhibitor of cell-death proteases. / Nature 1997, 388:300-04. CrossRef
27. Riedl SJ, Renatus M, Schwarzenbacher R, Zhou Q, Sun C, Fesik SW, Liddington RC, Salvesen GS: Structural basis for the inhibition for caspase-3 by XIAP. / Cell 2001, 104:791-00. CrossRef
28. Salvesen GS, Duckett CS: IAP proteins: Blocking the road to death’s door. / Nat. Rev. Mol. Cell Biol. 2002, 3:401-10. CrossRef
29. Zou H, Yang R, Hao J, Wang J, Sun C, Fesik SW, Wu JC, Tomaselli KJ, Armstronget RC: Regulation of the Apaf-1/caspase-9 apoptosome by caspase-3 and XIAP. / J. Biol. Chem. 2003, 278:8091-098. CrossRef
30. Irmler M, Thome M, Hahne M, Schnieder P, Hoffmann K, Steiner V, Bodmer JL, Schr?ter M, Burns K, Mattmann C, Rimoldi D, Frech LE, Tschopp J: Inhibition of death receptor signals by cellular FLIP. / Nature 1997, 388:190-95. CrossRef
31. Peter ME, Budd RC, Desbarats J, Hedrick SM, Hueber A, Newell MK, Owen LB, Pope RM, Tschopp J, Wajant H, Wallach D, Wiltrout RH, Z?rnig M, Lynch DH: The CD95 receptor: apoptosis revisited. / Cell 2007, 129:447-50. CrossRef - 作者单位：Chang Gu (1)
Junjie Zhang (2)
Yingyu Chen (3) (4)
Jinzhi Lei (5)
1. School of Mathematical Sciences, Peking University, Beijing, 100871, China
2. The Key Laboratory for Cell Proliferation and Regulation Biology of Ministry of Education, Institute of Cell Biology, College of Life Sciences, Beijing Normal University, Beijing, 100875, China
3. Laboratory of Medical Immunology, School of Basic Medical Science, Health Science Center, Peking University, 38 Xueyuan Road, Beijing, 100083, China
4. Center for Human Disease Genomics, Peking University, 38 Xueyuan Road, Beijing, 100083, China
5. Zhou Pei-Yuan Center for Applied Mathematics, Tsinghua University, Beijing, 100084, China
文摘
Background The ability of living cells to respond appropriately to apoptosis signals is crucial for the proper development and homeostasis of multicellular organisms. For example, viable cells must be stable enough to appropriately respond to apoptosis signaling so that an irreversible death program is only induced when apoptosis signaling reaches a certain threshold. Previous studies have introduced bistability models in which signaling by caspase-3 activity represents a key regulator of cell fate in response to apoptosis stimuli. Results In this study, apoptosis induced by tumor necrosis factor (TNF) signaling is investigated, and a mathematical model without the requirement for bistability is proposed. In this model, rapid degradation of the active forms of caspases -8 and -3 are included, and TNF-signaling is found to induce a pulse of caspase-3 activation and trigger an irreversible death program. This result agrees with experimental observations. The ability of a cell to respond to, or resist, apoptosis stimuli is also discussed. Furthermore, the activation efficiencies of caspases -8 and -3 that are essential to a cell’s response to extracellular apoptosis stimuli are defined. Based on the simulations performed, it is observed that activation efficiencies must be sufficiently sensitive to appropriately compromise a cell’s resistance and effectiveness in response to apoptosis stimuli. Conclusions Our results suggest that bistability may not be a necessary condition for the induction of apoptosis by TNF signaling. Rather, a sharp increase in caspase-3 activity might be sufficient to trigger the induction of an irreversible death program. Accordingly, regulation of caspase activity and degradation of active caspases is essential for a cell’s response to apoptosis stimuli.