Cell metabolism and signal transduction has usually been considered independent processes. Interestingly mitochondria is an intracellular organelle that perform energy production to fuel the cell to carry out its normal functions, however, in certain circumstances, its components can also carry out programmed cell destruction via its resident proteins. In this review, the role of mitochondria and its component proteins in inducing apoptotic programmed cell death is discussed. The role of Bcl-2 family proteins that set up the mitochondria induced apoptotic threshold is also described. Further, how the metabolic stress leads to mitochondrial dysfunction via increased generation of reactive oxygen species are discussed. This article is a part of a special issue on mitochondria summarizes the induction of intracellular pathways that converge on mitochondria and ultimately impact the success of chemotherapeutic interventions.
| Published in |
Cell Biology (Volume 3, Issue 2-1)
This article belongs to the Special Issue Mitochondria: Implications in Human Health and Diseases |
| DOI | 10.11648/j.cb.s.2015030201.13 |
| Page(s) | 17-21 |
| Creative Commons |
This is an Open Access article, distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution and reproduction in any medium or format, provided the original work is properly cited. |
| Copyright |
Copyright © The Author(s), 2024. Published by Science Publishing Group |
Mitochondria, Cancer, Apoptosis, Programmed Cell Death
| [1] | Zimorski, V., Ku, C., Martin, W.F. and Gould, S.B. (2014) Endosymbiotic theory for organelle origins. Curr. Opin. Microbiol., 22C, 38-48. |
| [2] | Vogtle, F.N., Burkhart, J.M., Rao, S., Gerbeth, C., Hinrichs, J., Martinou, J.C., Chacinska, A., Sickmann, A., Zahedi, R.P. and Meisinger, C. (2012) Intermembrane space proteome of yeast mitochondria. Mol. Cell. Proteomics, 11, 1840-1852. |
| [3] | Herrmann, J.M., Longen, S., Weckbecker, D. and Depuydt, M. (2012) Biogenesis of mitochondrial proteins. Adv. Exp. Med. Biol., 748, 41-64. |
| [4] | Kim A. A panoramic overview of mitochondria and mitochondrial redox biology. Toxicol Res. 2014 Dec; 30(4): 221-34. doi: 10.5487/TR.2014.30.4.221 |
| [5] | Johnstone RW, Ruefli AA, Lowe SW (2002) Apoptosis: a link between cancer genetics and chemotherapy. Cell 108: 153-64. |
| [6] | Lowe SW, Lin AW (2000) Apoptosis in cancer. Carcinogenesis 21: 485-95. |
| [7] | Kerr JF, Wyllie AH, Currie AR (1972) Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br J Cancer 26: 239-57. |
| [8] | Majno G, Joris I (1995) Apoptosis, oncosis, and necrosis. An overview of cell death. Am J Pathol 146: 3-15. |
| [9] | Green DR, Reed JC (1998) Mitochondria and apoptosis. Science 281: 1309-12. |
| [10] | Danial NN, Korsmeyer SJ (2004) Cell death: critical control points. Cell 116: 205-19. |
| [11] | Newmeyer DD, Ferguson-Miller S (2003) Mitochondria: releasing power for life and unleashing the machineries of death. Cell 112:481-90. |
| [12] | Liu X, Kim CN, Yang J, Jemmerson R, Wang X (1996) Induction of apoptotic program in cell-free extracts: requirement for dATP and cytochrome c. Cell 86: 147-57. |
| [13] | Adrain C, Martin SJ (2001) The mitochondrial apoptosome: a killer unleashed by the cytochrome seas. Trends Biochem Sci 26: 390-7. |
| [14] | Lorenzo HK, Susin SA, Penninger J, Kroemer G (1999) Apoptosis inducing factor (AIF): a phylogenetically old, caspase-independent effector of cell death. Cell Death Differ 6:516-24. |
| [15] | van Loo G, Schotte P, van Gurp M, Demol H, Hoorelbeke B, Gevaert K, Rodriguez I, Ruiz-Carrillo A, Vandekerckhove J, Declercq W, Beyaert R, Vandenabeele P. (2001) Endonuclease G: a mitochondrial protein released in apoptosis and involved in caspase-independent DNA degradation. Cell Death Differ 8: 1136-42. |
| [16] | Du C, Fang M, Li Y, Li L, Wang X (2000) Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition. Cell 102: 33-42. |
| [17] | Faccio L, Fusco C, Chen A, Martinotti S, Bonventre JV, Zervos AS (2000) Characterization of a novel human serine protease that has extensive homology to bacterial heat shock endoprotease HtrA and is regulated by kidney ischemia. J Biol Chem 275: 2581-8. |
| [18] | Gray CW, Ward RV, Karran E, Turconi S, Rowles A, Viglienghi D, Southan C, Barton A, Fantom KG, West A, Savopoulos J, Hassan NJ, Clinkenbeard H, Hanning C, Amegadzie B, Davis JB, Dingwall C, Livi GP, Creasy CL (2000) Characterization of human HtrA2, a novel serine protease involved in the mammalian cellular stress response. Eur J Biochem 267: 5699-710. |
| [19] | Jan Y, Matter M, Pai JT, Chen YL, Pilch J, Komatsu M, Ong E, Fukuda M, Ruoslahti E (2004) A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell 116: 751-62. |
| [20] | Adams JM, Cory S (1998) The Bcl-2 protein family: arbiters of cell survival. Science 281:1322-6. |
| [21] | Reed JC (1999) Dysregulation of apoptosis in cancer. J Clin Oncol 17: 2941-53. |
| [22] | Hockenbery D, Nunez G, Milliman C, Schreiber RD, Korsmeyer SJ (1990) Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 348: 334-6. |
| [23] | McDonnell TJ, Deane N, Platt FM, Nunez G, Jaeger U, McKearn JP, Korsmeyer SJ (1989) bcl-2-immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation. Cell 57: 79-88. |
| [24] | Hsu YT, Wolter KG, Youle RJ (1997) Cytosol-to-membrane redistribution of Bax and Bcl-X(L) during apoptosis. Proc Natl Acad Sci USA 94: 3668-72. |
| [25] | Pastorino JG, Chen ST, Tafani M, Snyder JW, Farber JL (1998) The overexpression of Bax produces cell death upon induction of the mitochondrial permeability transition. J Biol Chem 273: 7770-5. |
| [26] | Desagher S, Osen-Sand A, Nichols A, Eskes R, Montessuit S, Lauper S, Maundrell K, Antonsson B, Martinou JC (1999) Bid-induced conformational change of Bax is responsible for mitochondrial cytochrome c release during apoptosis. J Cell Biol 144: 891-901. |
| [27] | Zha J, Harada H, Yang E, Jockel J, Korsmeyer SJ (1996) Serine phosphorylation of death agonist BAD in response to survival factor results in binding to 14-3-3 not BCL-X(L) Cell 87: 619-28. |
| [28] | Cheng EH, Wei MC, Weiler S, Flavell RA, Mak TW, Lindsten T, Korsmeyer SJ (2001) BCL-2, BCL-X(L) sequester BH3 domain-only molecules preventing BAX- and BAK-mediated mitochondrial apoptosis. Mol Cell 8:705-11. |
| [29] | Narita M, Shimizu S, Ito T, Chittenden T, Lutz RJ, Matsuda H, Tsujimoto Y (1998) Bax interacts with the permeability transition pore to induce permeability transition and cytochrome c release in isolated mitochondria. Proc Natl Acad Sci USA 95: 14681-6. |
| [30] | Basanez G, Nechushtan A, Drozhinin O, Chanturiya A, Choe E, Tutt S, Wood KA, Hsu Y, Zimmerberg J, Youle RJ (1999) Bax, but not Bcl-xL, decreases the lifetime of planar phospholipid bilayer membranes at subnanomolar concentrations. Proc Natl Acad Sci U S A 96: 5492-7. |
| [31] | Thornberry NA, Lazebnik Y (1998) Caspases: enemies within. Science 281: 1312-6. |
| [32] | Simonian NA, Coyle JT (1996) Oxidative stress in neurodegenerative diseases. Annu Rev Pharmacol Toxicol 36: 83-106. |
| [33] | Korshunov SS, Skulachev VP, Starkov AA. (1997) High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett 416:15-8. |
| [34] | Huang P, Feng L, Oldham EA, Keating MJ, Plunkett W (2000) Superoxide dismutase as a target for the selective killing of cancer cells. Nature 407(6802):390-5. |
| [35] | Chandra J, Samali A, Orrenius S (2000) Triggering and modulation of apoptosis by oxidative stress. Free Radic Biol Med 29:323-33. |
APA Style
Ashutosh Shrivastava. (2015). The Mechanisms of Mitochondria-Mediated Apoptosis in Cancer Chemotherapy. Cell Biology, 3(2-1), 17-21. https://doi.org/10.11648/j.cb.s.2015030201.13
ACS Style
Ashutosh Shrivastava. The Mechanisms of Mitochondria-Mediated Apoptosis in Cancer Chemotherapy. Cell Biol. 2015, 3(2-1), 17-21. doi: 10.11648/j.cb.s.2015030201.13
AMA Style
Ashutosh Shrivastava. The Mechanisms of Mitochondria-Mediated Apoptosis in Cancer Chemotherapy. Cell Biol. 2015;3(2-1):17-21. doi: 10.11648/j.cb.s.2015030201.13
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Download@article{10.11648/j.cb.s.2015030201.13,
author = {Ashutosh Shrivastava},
title = {The Mechanisms of Mitochondria-Mediated Apoptosis in Cancer Chemotherapy},
journal = {Cell Biology},
volume = {3},
number = {2-1},
pages = {17-21},
doi = {10.11648/j.cb.s.2015030201.13},
url = {https://doi.org/10.11648/j.cb.s.2015030201.13},
eprint = {https://article.sciencepublishinggroup.com/pdf/10.11648.j.cb.s.2015030201.13},
abstract = {Cell metabolism and signal transduction has usually been considered independent processes. Interestingly mitochondria is an intracellular organelle that perform energy production to fuel the cell to carry out its normal functions, however, in certain circumstances, its components can also carry out programmed cell destruction via its resident proteins. In this review, the role of mitochondria and its component proteins in inducing apoptotic programmed cell death is discussed. The role of Bcl-2 family proteins that set up the mitochondria induced apoptotic threshold is also described. Further, how the metabolic stress leads to mitochondrial dysfunction via increased generation of reactive oxygen species are discussed. This article is a part of a special issue on mitochondria summarizes the induction of intracellular pathways that converge on mitochondria and ultimately impact the success of chemotherapeutic interventions.},
year = {2015}
}
TY - JOUR T1 - The Mechanisms of Mitochondria-Mediated Apoptosis in Cancer Chemotherapy AU - Ashutosh Shrivastava Y1 - 2015/03/12 PY - 2015 N1 - https://doi.org/10.11648/j.cb.s.2015030201.13 DO - 10.11648/j.cb.s.2015030201.13 T2 - Cell Biology JF - Cell Biology JO - Cell Biology SP - 17 EP - 21 PB - Science Publishing Group SN - 2330-0183 UR - https://doi.org/10.11648/j.cb.s.2015030201.13 AB - Cell metabolism and signal transduction has usually been considered independent processes. Interestingly mitochondria is an intracellular organelle that perform energy production to fuel the cell to carry out its normal functions, however, in certain circumstances, its components can also carry out programmed cell destruction via its resident proteins. In this review, the role of mitochondria and its component proteins in inducing apoptotic programmed cell death is discussed. The role of Bcl-2 family proteins that set up the mitochondria induced apoptotic threshold is also described. Further, how the metabolic stress leads to mitochondrial dysfunction via increased generation of reactive oxygen species are discussed. This article is a part of a special issue on mitochondria summarizes the induction of intracellular pathways that converge on mitochondria and ultimately impact the success of chemotherapeutic interventions. VL - 3 IS - 2-1 ER -
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