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2006 | 11 | 4 |

Tytuł artykułu

Current concepts in apoptosis: the physiological suicide program revisited

Warianty tytułu

Języki publikacji

EN

Abstrakty

EN
Apoptosis, or programmed cell death (PCD), involves a complex network of biochemical pathways that normally ensure a homeostatic balance between cellular proliferation and turnover in nearly all tissues. Apoptosis is essential for the body, as its deregulation can lead to several diseases. It plays a major role in a variety of physiological events, including embryonic development, tissue renewal, hormone-induced tissue atrophy, removal of inflammatory cells, and the evolution of granulation tissue into scar tissue. It also has an essential role in wound repair. The various cellular and biochemical mechanisms involved in apoptosis are not fully understood. However, there are two major pathways, the extrinsic pathway (receptor-mediated apoptotic pathway) and the intrinsic pathway (mitochondria-mediated apoptotic pathway), which are both well established. The key component in both is the activation of the caspase cascade. Caspases belong to the family of proteases that ultimately, by cleaving a set of proteins, cause disassembly of the cell. Although the caspase-mediated proteolytic cascade represents a central point in the apoptotic response, its initiation is tightly regulated by a variety of other factors. Among them, Bcl-2 family proteins, TNF and p53 play pivotal roles in the regulation of caspase activation and in the regulation of apoptosis. This review summarizes the established concepts in apoptosis as a physiological cell suicide program, highlighting the recent and significant advances in its study.

Wydawca

-

Rocznik

Tom

11

Numer

4

Opis fizyczny

p.506-525,fig.,ref.

Twórcy

autor
  • Morehouse School of Medicine, Atlanta, GA, USA
autor
autor

Bibliografia

  • 1. Vaux, D.L. and Korsmeyer, S.J. Cell death in development. Cell 96 (1999) 245-254.
  • 2. Kerr, J.F.R. An electron-microscope study of liver cell necrosis due to Albitocin. Pathology 2 (1970) 251-259.
  • 3. Kerr, J.F.R. Shrinkage necrosis: A distinct mode of cellular death. J. Path. 105 (1971) 13-20.
  • 4. Kerr, J.F. Wyllie, A.H. and Currie, A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26 (1972) 239-257.
  • 5. Thompson, C.B. Apoptosis in the pathogenesis and treatment of disease. Science 267 (1995)1456-1462.
  • 6. Wang, X. The expanding role of mitochondria in apoptosis. Genes Dev. 15 (2001) 2922-2933.
  • 7. Hortvitz, H.R. Worm, life and death (Nobel lecture). Chembiochem. 4 (2003) 697-711.
  • 8. Danial, N.N. and Krosmeyer, S.J. Cell death: critical control points. Cell 116 (2004) 205-219.
  • 9. Schwartzman, R.A. and Cidlowski, J.A. Apoptosis: the biochemistry and molecular biology of programmed cell death. Endocr. Rev. 14 (1993) 133-51.
  • 10. Cohen, J.J. Apoptosis. Immunol. Today 14 (1993) 126-130.
  • 11. Vaux, D.L. and Strasser, A. The molecular biology of apoptosis. Proc. Natl. Acad. Sci. USA 93 (1996) 2239-2244.
  • 12. Levine, B. and Yuan, J. Autophagy in cell death: an innocent convict? J. Clin. Invest. 115 (2005) 2679-2688.
  • 13. Clarke, P.G. Developmental cell death: morphological diversity and multiple mechanisms. Anat. Embryol. (Berl.) 181 (1990) 195-213.
  • 14. Bursch, W. The autophagosomal-lysosomal compartment in programmed cell death. Cell Death Differ. 8 (2001) 569-581.
  • 15. Majno, G. and Joris, I. Apoptosis, oncosis and necrosis. An overview of cell death. Am. J. Pathol. 146 (1995) 3-15.
  • 16. Broker, L.E., Kruyt, F. and Giaccone, G. Cell death independent of caspases: a review. Clin. Cancer Res. 11 (2005) 3155-3162.
  • 17. Castedo, M., Perfettini, J.L., Roumier, T., Andreau, K., Medema, R. and Kroemer, G. Cell death by mitotic catastrophe: a molecular definition. Oncogene 23 (2004) 2825-2837.
  • 18. Earnshaw, W.C. Nuclear changes in apoptosis. Cur. Opin. Cell Biol. 7 (1995) 337-343.
  • 19. Au, J.L., Panchal, N., Li, D. and Gan, Y. Apoptosis: a new pharmacodynamic endpoint. Pharm. Res. 14 (1997) 1659-1671.
  • 20. Gong, J., Traganos, F. and Darsynkiewicz, Z.A selective procedure for DNA extraction from apoptotic cells applicable for gel electrophoresis and flow cytometry. Anal. Biochem. 218 (1994) 314-319.
  • 21. Bortner, C.D., Oldenburg, N.D. and Cidlowski, J.A. The role of DNA fragmentation in apoptosis. Trends Cell Biol. 5 (1995) 21-26.
  • 22. Dive, C., Gregory, C.D., Phopps, D.J., Evans, D.L., Milner, A.E. and Wyllie, A.H. Analysis and discrimination of necrosis and apoptosis (programmed cell death) by multiparameter flow cytometry. Biochim. Biophys. Acta 1133 (1992) 275-285.
  • 23. Hamel, W., Dazin, P. and Israel, M. Adaptation of a simple flow cytometric assay to identify different stages during apoptosis. Cytometry 25 (1996) 173- 181.
  • 24. Gavrieli, Y., Sherman, Y. and Benassan, S.A. Identification of programmed cell death in situ via special labeling of nuclear DNA fragments. J. Cell Biol. 119 (1992) 493-501.
  • 25. Charriaut-Malangue, C. and Ben-Ari, Y. A cautionary note on the use of the TUNEL stain to determine apoptosis. Neuroreport 7 (1995) 61-64.
  • 26. Lecoeur, H., Prevost, M.C. and Gougeon, M.L. Oncosis is associated with exposure of phosphatidylserine residues on the outside layer of the plasma membrane: a reconsideration of the specificity of the annexin V/propidium iodide assay. Cytometry 44 (2001) 65-72.
  • 27. Alnemri, E.S., Livingston, D.W., Nicholson, D.W., Salvesen, G., Thornberry, N.A., Wong, W.W. and Yuan, J. Human ICE/CED-3 protease nomenclature. Cell 87 (1996) 171.
  • 28. Salvesen, G.S. and Dixit, V.M. Caspases: intracellular signaling by proteolysis. Cell 91 (1997) 443-446.
  • 29. Lavarik, I.N., Golks, A. and Krammer, P.H. Caspases: pharmacological manipulation of cell death. J. Clin. Invest. 115 (2005) 2665-2672.
  • 30. Yuan, J., Shahan, S., Ledoux, S., Ellis, H.M. and Horvitz, H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1 beta converting enzyme. Cell 75 (1993) 641-652.
  • 31. Shi, Y. Mechanisms of caspase activation and inhibition during apoptosis. Mol. Cell 9 (2002) 459-470.
  • 32. Yan, N. and Shi, Y. Mechanisms of apoptosis through structural biology. Ann. Rev. Cell Dev. Biol. 21 (2005) 35-56.
  • 33. Stennicke, H.R. and Salvesen, G.S. Properties of the caspases. Biochim. Biophys. Acta 1387 (1998) 17-31.
  • 34. Grutter, M.G. Caspases: Key players in programmed cell death. Curr. Opin. Struct. Biol. 10 (2000) 649-655.
  • 35. Roth, K.A. Caspases, apoptosis, and Alzheimer’s disease: causation, correlation, and confusion. J. Neuropathol. Exp. Neurol. 60 (2001) 829-838.
  • 36. Cohen, G.M. Caspases: the executioners of apoptosis. Biochem. J. 326 (1997) 1-16.
  • 37. Marshman, E., Ottewell, P.D., Potten, C.S. and Watson, A.J. Caspase activation during spontaneous and radiation-induced apoptosis in the murine intestine. J. Pathol. 195 (2001) 285-292.
  • 38. Clerk, A., Cole, S.M., Cullingford, T.E., Harrison, J.C., Jormakka, M. and Valks, D.M. Regulation of cardiac myocyte cell death. Pharmacol. Ther. 97 (2003) 223-61.
  • 39. Nagata, S. Apoptotic DNA fragmentation. Exp. Cell Res. 256 (2000) 12-18.
  • 40. Earnshaw, W.C., Martins, L.M. and Kaufmann, S.H. Mammalian caspases: Structure, activation, substrates and functions during apoptosis. Ann. Rev. Biochem. 68 (1999) 383-424.
  • 41. Liu, X., Kim, C.N., Yang, J., Jemmerson, R. and Wang, X. Induction of apoptosis program in cell-free extracts: Requirement for dATP and cytochrome c. Cell 86 (1996) 147-157.
  • 42. Enari, M., Sakahira, H., Yokoyama, H., Okawa, K., Iwamatsu, A., and Nagata, S. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391 (1998) 43-50.
  • 43. Coleman, M.L., Sahai, E.A., Yeo, M., Bosch, M., Dewar, A. and Olson, M.F. Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nat. Cell Biol. 3 (2001) 339-345.
  • 44. Martinon, F. and Tschopp, J. Inflammatory caspases: linking an intracellular innate immune system to autoinflammatory disease. Cell 117 (2004) 561-574.
  • 45. Roy, N., Mahadevan, M.S., McLean, M., Shutler, G., Yaraghi, Z., Farahani, R., Baird, S., Benser-Johnson, A., Lefebvre, C., Kang, X.,Salih, M., Aubry, H., Tamai, K., Guan, X., Ioannou, P., Crawford, T.O., de Jong, P.J., Surh, L., Ikeda, J.E., Korneluk, R.G. and Mac Kenzie, A. The gene for neuronal apoptosis inhibitory protein is partially deleted in individuals with spinal muscular atrophy. Cell 80 (1995)167-178.
  • 46. Cheng, E.H., Levine, B., Boise, L.H., Thompson, C.B. and Hardwick, J.M. Bax-independent inhibition of apoptosis by Bcl-XL. Nature 379 (1996) 554- 556.
  • 47. Salvesen, G.S. and Duckett, C.S. IAP proteins: blocking the road to death’s door. Nat. Rev. Mol. Cell Biol. 3 (2002) 401-410.
  • 48. Deveraux, Q.L. and Reed, J.C. IAP family proteins: suppressors of apoptosis. Genes Dev. 13 (1999) 239-252.
  • 49. Ekert, P.G., Silke, J. and Vaux, D.L. Caspase inhibitor. Cell Death Differ. 6 (1999) 1081-1086.
  • 50. Birnbaum, M.J., Clem, R.J. and Miller, L.K. An apoptosis inhibiting gene from a nuclear polyhedrosis virus encoding a polypeptide with Cys/His sequence motifs. J. Virol. 68 (1994) 2521-2528.
  • 51. Deveraux, Q.L., Takahashi, R., Salvesen, G.S. and Reed, J.C. X-linked IAP is a direct inhibitor of cell-death proteases. Nature 388 (1997) 300-304.
  • 52. Deveraux, Q.L., Roy, H.R., Stennicke, H.R., Van Arsdale, T., Zhou, Q., Srinivasula, M., Alnemri, E.S., Salvesen, G.S. and Reed, J.C. IAPs block apoptotic events induced by caspase-8 and cytochrome c by direct inhibition of distinct caspases. EMBO J. 17 (1998) 2215-2223.
  • 53. Roy, N., Deveraux, Q.I., Takashashi, R., Salvesen, G.S. and Reed, J.C. The c-IAP-1 and c-IAP-2 proteins are direct inhibitors of specific caspases. EMBO J. 16 (1997) 6914-6925.
  • 54. Miller, L.K. An exegesis of IAPs: salvation and surprises from BIR motifs. Trends Cell Biol. 9 (1999) 323-328.
  • 55. Xu, G., Cirilli, M., Huang, Y., Rich, R.L., Myszka, D.G. and Wu, H. Covalent inhibition revealed by the crystal structure of the caspase-8/p35 complex. Nature 410 (2001) 494-497.
  • 56. Renatus, M., Zhou, Q., Stennicke, H.R., Snipas, S.J., Turk, D., Bankston, L.A., Liddington, R.C. and Salvesen, G.S. Crystal structure of the apoptotic suppressor CrmA in its cleaved form. Structure Fold. Des. 8 (2000) 789-797.
  • 57. Sato, T., Irie, S., Krajewski, S. and Reed, J.C. Cloning and sequencing of a cDNA encoding the rat Bcl2 protein. Gene 140 (1994) 291-292.
  • 58. Adams, J.M. and Cory, S. The Bcl-2 protein family : Arbiters of cell survival. Science 281 (1998)1322-26.
  • 59. Burlacu, A. Regulation of apoptosis by Bcl-2 family proteins. J. Cell. Mol. Med. 7 (2003) 249-257.
  • 60. Tsujimoto, Y., Cossman, J., Jaffe, E. and Croce, C.M. Involvement of the Bcl2 gene in human follicular lymphoma. Science 228 (1985) 1440-1443.
  • 61. Cory, S. and Adams, J.M. The Bcl2 family: regulators of the cellular life or death switch. Nat. Rev. Cancer 2 (2002) 647-656.
  • 62. Puthalakath, H. and Strasser, A. Keeping killers on a tight leash: transcriptional and post-transcriptional control of the pro-apoptotic activity of BH3-only proteins. Cell Death Differ. 9 (2002) 505-512.
  • 63. Zhu, W., Cowie, A., Wasfy, G.W., Penn, L.Z., Leber, B. and Andrew, D.W. Bcl2 mutants with restricted sub cellular location reveal spatially distinct pathways for apoptosis in different cell types. EMBO J. 15 (1996) 4130- 4141.
  • 64. Griffiths, G.J., Dubrez, L., Morgan, C.P., Jones, N.A., Whitehouse, J., Corfe, B.M., Dive, C. and Hickman, J.A. Cell damage-induced conformational changes of the pro-apoptotic protein Bak in-vivo precede the onset of apoptosis. J. Cell Biol. 144 (1999) 903-914.
  • 65. Krajewski, S., Tanaka, S., Takayama, S., Schibler, M.J., Fenton, W. and Reed, J.C. Investigation of the Bcl-2 oncoprotein: Residence in the nuclear envelop, endoplasmic reticulum, and outer mitochondrial membranes. Cancer Res. 53 (1993) 4701-4714.
  • 66. Nguyen, M., Millar, D.G., Yong, V.W., Korsmeyer, S.J. and Shore, G.C. Targeting of Bcl-2 to the mitochondrial outer membrane by a COOH-terminal signal anchor sequence. J. Biol. Chem. 268 (1993) 25265-25268.
  • 67. Hussein, M.R., Haemel, A.K. and Wood, G.S. Apoptosis and melanoma: molecular mechanism. J. Pathol. 199 (2003) 275-288.
  • 68. Gross, A., Mcdonnell, J.M. and Krosmeyer, S.J. Bcl-2 family members and the mitochondria in apoptosis. Genes Develop. 13 (1999) 1899-1911.
  • 69. Erster, S. and Moll, U.M. Stress induced p53 runs a transcription-independent death program. Biochem. Biophys. Res. Commun. 331 (2005) 843-850.
  • 70. Owen-Schaub, L.B., Angelo, L.S., Radinsky, R., Ware, C.F., Gesner, T.G. and Bartos, D.P. Soluble FAS/APO-1 in tumor cells: a potential regulator of apoptosis? Cancer Lett. 94 (1995) 1-8.
  • 71. Park, D.S., Stefanis, L. and Greene, L.A. Ordering the multiple pathways of apoptosis. Trends Cardiovasc. Med. 7 (1997) 294-299.
  • 72. Duensing, A. and Duensing, S. Guilt by association? p53 and development of aneuploidy in cancer. Biochem. Biophys. Res. Commun. 331 (2005) 694- 700.
  • 73. Aggarwal, B.B. Tumor necrosis factor receptor associated signalling molecules and their role in activation of apoptosis, JNK and NF-kB. Ann. Rheum. Dis. 59 (2000) 6-16.
  • 74. Idriss, H.T. and Naismith, J.H. TNF alpha and the TNF receptor super family: structure-function relationship(s). Micro. Res. Tech. 50 (2000) 184-195.
  • 75. MacEwan, D.J. TNF ligands and receptors – a matter of life and death. Br. J. Pharm. 135 (2002) 855-875.
  • 76. Wajant, H., Pfizenmaier, K. and Scheurich, P. Tumor necrosis factor signaling. Cell Death Diff. 10 (2003) 45-65.
  • 77. Hussein, M.R., Haemel, A.K. and Wood, G.S. p53 related pathways and the molecular pathogenesis of melanoma. Eur. J. Cancer Prev. 12 (2003) 93- 100.
  • 78. Green, D. and Reed, J. Mitochondria and apoptosis. Science 281 (1998) 1309- 1312.
  • 79. Tsujimoto, Y. and Shimizu, S. The voltage-dependent anion channel: an essential player in apoptosis. Biochimie 84 (2002) 187-193.
  • 80. Reed, J.C. Bcl-2 family proteins. Oncogene 17 (1998) 3225-3236.
  • 81. Shimizu, S., Narita, M. and Tsujimoto, Y. Bcl-2 family protein regulates the release of apoptogenic cytochrome c by the mitochondrial channel VDAC. Nature 399 (1999) 483-487.
  • 82. Ashkenazi, A. and Dixit, V.M. Death receptors: signaling and modulation. Science 281 (1998) 1305-1308.
  • 83. Schulze-Osthoff, K., Ferrari, D., Los, M., Wesselborg, S. and Peter, M.E. Apoptosis signaling by death receptors. Eur. J. Biochem. 254 (1998) 439- 459.
  • 84. Peter, M.E. and Krammer, P.H. Mechanisms of CD95 (APO-1/ Fas)-mediated apoptosis. Curr. Opin. Immunol. 10 (1998) 545-551.
  • 85. Peter, M.E. and Krammer, P.H. The CD95 (APO-1/ Fas) DISC and beyond. Cell Death Differ. 10 (2003) 26-35.
  • 86. Li, H., Zhu, H., Xu, C.J. and Yuan, J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell 94 (1998) 491-501.
  • 87. Luo, X., Budihardjo, I., Zou, H., Slaughter, C. and Wang, X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell 94 (1998) 481-490.
  • 88. Chaudhary, P.M., Eby, M., Jasmin, A., Bookwalter, A., Murray, J. and Hood, L. Death receptor 5, a new member of the TNFR family, and DR4 induce FADD-dependent apoptosis and activate the NF-kappa B pathway. Immunity 7 (1997) 821-830.
  • 89. Stennicke, H.R., Jurgensmeier, J.M., Shin, H., Deveraux, Q., Wolf, B.B., Yang, X., Zhou, Q., Ellerby, H.M., Ellerby, L.M., Bredesen, D., Green, D.R., Reed, J.C., Froelich, C.J. and Salvesen, G. S. Procaspase-3 is a major physiologic target of caspase-8. J. Biol. Chem. 273 (1998) 27084-27090.
  • 90. Scaffidi, C., Schmitz, I., Krammer, P.H. and Peter, M.E. The role of c-FLIP in modulation of CD95 induced apoptosis. J. Biol. Chem. 274 (1999) 1541- 1548.
  • 91. Golks, A., Brenner, D., Fritsch, C., Krammer, P.H. and Lavrik, L.N. cFLIPR: a new regulator of death receptor-induced apoptosis. J. Biol. Chem. 280 (2005) 14507-14513.
  • 92. Harris, S.L. and Levine, A.J. The p53 pathway: positive and negative feed back loops. Oncogene 24 (2005) 2899-2908.
  • 93. Li, F., Srinivasam, A., Wang, Y., Armstrong, R.C., Tomaselli, K.J. and Fritz, L.C. Cell-specific induction of apoptosis by microinjection of cytochrome c. J. Biol. Chem. 272 (1997) 30299-30305.
  • 94. Hengartner, M.O. The biochemistry of apoptosis. Nature 407 (2000) 770-776.
  • 95. Xu, C., Bailly-Maitre, B. and Reed, J.C. Endoplasmic reticulam stress: cell life and death decisions. J. Clin. Invest. 115 (2005) 2656-2664.
  • 96. Hick, S.W. and Machamer, C.E. Golgi structure in stress sensing and apoiptosis. Biochim. Biophys. Acta 1744 (2005) 406-414.
  • 97. Wu, Y., Tibrewal, N. and Brige, R.B. Phospohatidylserine recognition by phagocytes: a view to a kill. Trends Cell Biol. 16 (2006) 189-197.
  • 98. Savill, J. Recognition and phagocytosis of cells undergoing apoptosis. Br. Med. Bull. 53 (1997) 491-508.

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