Mitoptosis, a Novel Mitochondrial Death Mechanism Leading Predominantly to Activation of Autophagy

Jaganmohan Jangamreddy; Marek Los

doi:10.5812/hepatmon.6159

Mitoptosis, a Novel Mitochondrial Death Mechanism Leading Predominantly to Activation of Autophagy

authors:

Jaganmohan Jangamreddy ¹ , Marek Los ^{1
, *}

1 Deptartment of Clinical and Experimental Medicine, Integrative Regenerative Medicine Center (IGEN), Division of Cell Biology, Linköping University, Linkoping, Sweden

Hepatitis Monthly: Vol.12, issue 8; e6159

published online: August 20, 2012

article type: Editorial

received: February 28, 2012

revised: March 10, 2012

accepted: March 23, 2012

DOI: https://doi.org/10.5812/hepatmon.6159

how to cite: Jangamreddy J, Los M. Mitoptosis, a Novel Mitochondrial Death Mechanism Leading Predominantly to Activation of Autophagy. Hepat Mon. 2012;12(8):e6159. https://doi.org/10.5812/hepatmon.6159.

Keywords

Homeostasis Cytochromes C DNM1L Protein Human

Acknowledgements

Footnotes

Implication for health policy/practice/research/medical educationThe manuscript provides insight into the recently-discovered new form of cell death that may co-exist with autophagy, apoptosis or necorosis. The described below cellular extrusion of damaged mitochondria, may contribute to ethiology of some autoimmune diseases, as well as to the development of novel antiviral drugs that employ autophagy in their life-cycle.
Please cite this paper asJangamreddy JR, Los MJ. Mitoptosis, a Novel Mitochondrial Death Mechanism Leading Predominantly to Activation of Autophagy. Hepat Mon. 2012;12(8): e6159. DOI: 10.5812/hepatmon.6159
Please cite this paper asJangamreddy JR, Los MJ. Mitoptosis, a Novel Mitochondrial Death Mechanism Leading Predominantly to Activation of Autophagy. Hepat Mon. 2012;12(8): e6159. DOI: 10.5812/hepatmon.6159
Financial DisclosureNone declared.
Funding/SupportML and JR kindly acknowledge the core/startup support from Linköping University, the Integrative Regenerative Medicine Center (IGEN), and the Cancerfonden (CAN 2011/521).

References

1.
Los M, van de Craen M, Penning CL, Schenk H, Westendorp M, Baeuerle PA, et al. Requirement of an ICE/Ced-3 protease for Fas/ Apo-1-1mediated apoptosis. Nature. 1995;371:81-3. [PubMed ID: 7536901]. https://doi.org/10.1038/375081a0.
2.
Los M, Wesselborg S, Schulze-Osthoff K. The role of caspases in development, immunity, and apoptotic signal transduction: lessons from knockout mice. Immunity. 1999;10:629-39. https://doi.org/10.1016/S1074-7613(00)80062-X.
3.
Ghavami S, Mutawe MM, Hauff K, Stelmack GL, Schaafsma D, Sharma P, et al. Statin-triggered cell death in primary human lung mesenchymal cells involves p53-PUMA and release of Smac and Omi but not cytochrome c. Biochim Biophys Acta. 2010;1803(4):452-67. [PubMed ID: 20045437]. https://doi.org/10.1016/j.bbamcr.2009.12.005.
4.
Ghavami S, Mutawe MM, Sharma P, Yeganeh B, McNeill KD, Klonisch T, et al. Mevalonate Cascade Regulation of Airway Mesenchymal Cell Autophagy and Apoptosis: A Dual Role for p53. PLoS One. 2011;6(1):e16523. [PubMed ID: 21304979]. https://doi.org/10.1371/journal.pone.0016523.
5.
Vincent FC, Los MJ. New potential instrument to fight hepatocellular cancer by restoring p53. Hepat Mon. 2011;11(5):331-2. [PubMed ID: 22087156].
6.
Ghavami S, Eshraghi M, Kadkhoda K, Mutawe MM, Maddika S, Bay GH, et al. Role of BNIP3 in TNF-induced cell death--TNF up regulates BNIP3 expression. Biochim Biophys Acta. 2009;1793(3):546-60. [PubMed ID: 19321129]. https://doi.org/10.1016/j.bbamcr.2009.01.002.
7.
Ghavami S, Eshragi M, Ande SR, Chazin WJ, Klonisch T, Halayko AJ, et al. S100A8/A9 induces autophagy and apoptosis via ROSmediated cross-talk between mitochondria and lysosomes that involves BNIP3. Cell Res. 2010;20(3):314-31. [PubMed ID: 19935772]. https://doi.org/10.1038/cr.2009.129.
8.
Ghavami S, Hashemi M, Ande SR, Yeganeh B, Xiao W, Eshraghi M, et al. Apoptosis and cancer: mutations within caspase genes. J Med Genet. 2009;46(8):497-510. [PubMed ID: 19505876]. https://doi.org/10.1136/jmg.2009.066944.
9.
Stroh C, Cassens U, Samraj AK, Sibrowski W, Schulze-Osthoff K, Los M. The role of caspases in cryoinjury: caspase inhibition strongly improves the recovery of cryopreserved hematopoietic and other cells. Faseb J. 2002;16(12):1651-3. [PubMed ID: 12207004].
10.
Ghavami S, Asoodeh A, Klonisch T, Halayko AJ, Kadkhoda K, Kroczak TJ, et al. Brevinin-2R(1) semi-selectively kills cancer cells by a distinct mechanism, which involves the lysosomal-mitochondrial death pathway. J Cell Mol Med. 2008;12(3):1005-22. [PubMed ID: 18494941]. https://doi.org/10.1111/j.1582-4934.2008.00129.x.
11.
Gokay O, Kuhner D, Los M, Gotz F, Bertsche U, Albert K. An efficient approach for the isolation, identification and evaluation of antimicrobial plant components on an analytical scale, demonstrated by the example of Radix imperatoriae. Anal Bioanal Chem. 2010;398(5):2039-47. [PubMed ID: 20827467]. https://doi.org/10.1007/s00216-010-4153-2.
12.
Mendoza FJ, Espino PS, Cann KL, Bristow N, McCrea K, Los M. Anti-tumor chemotherapy utilizing peptide-based approaches- -apoptotic pathways, kinases, and proteasome as targets. Arch Immunol Ther Exp (Warsz). 2005;53(1):47-60.
13.
Alavian SM, Ande SR, Coombs KM, Yeganeh B, Davoodpour P, Hashemi M, et al. Virus-triggered autophagy in viral hepatitis- possible novel strategies for drug development. J Viral Hepat. 2011;18(12):821-30. [PubMed ID: 22093031]. https://doi.org/10.1111/j.1365-2893.2011.01530.x.
14.
Maddika S, Ande SR, Panigrahi S, Paranjothy T, Weglarczyk K, Zuse A, et al. Cell survival, cell death and cell cycle pathways are interconnected: Implications for cancer therapy. Drug Resist Updat. 2007;10(1-2):13-29. [PubMed ID: 17303468]. https://doi.org/10.1016/j.drup.2007.01.003.
15.
Maddika S, Ande SR, Wiechec E, Hansen LL, Wesselborg S, Los M. Akt-mediated phosphorylation of CDK2 regulates its dual role in cell cycle progression and apoptosis. J Cell Sci. 2008;121(Pt 7):979-88. [PubMed ID: 18354084]. https://doi.org/10.1242/jcs.009530.
16.
Barczyk K, Kreuter M, Pryjma J, Booy EP, Maddika S, Ghavami S, et al. Serum cytochrome c indicates in vivo apoptosis and can serve as a prognostic marker during cancer therapy. Int J Cancer. 2005;116(2):167-73. [PubMed ID: 15800951]. https://doi.org/10.1002/ijc.21037.
17.
Skulachev VP. Mitochondria in the programmed death phenomena; a principle of biology: “it is better to die than to be wrong”. IUBMB Life. 2000;49(5):365-73. [PubMed ID: 10902567].
18.
Skulachev VP. Bioenergetic aspects of apoptosis, necrosis and mitoptosis. Apoptosis. 2006;11(4):473-85. [PubMed ID: 16532373]. https://doi.org/10.1007/s10495-006-5881-9.
19.
Lyamzaev KG, Nepryakhina OK, Saprunova VB, Bakeeva LE, Pletjushkina OY, Chernyak BV, et al. Novel mechanism of elimination of malfunctioning mitochondria (mitoptosis): formation of mitoptotic bodies and extrusion of mitochondrial material from the cell. Biochim Biophys Acta. 2008;1777(7-8):817-25. [PubMed ID: 18433711]. https://doi.org/10.1016/j.bbabio.2008.03.027.
20.
Izyumov DS, Avetisyan AV, Pletjushkina OY, Sakharov DV, Wirtz KW, Chernyak BV, et al. “Wages of fear”: transient threefold decrease in intracellular ATP level imposes apoptosis. Biochim Biophys Acta. 2004;1658(1-2):141-7. [PubMed ID: 15282185]. https://doi.org/10.1016/j.bbabio.2004.05.007.
21.
Xue L, Fletcher GC, Tolkovsky AM. Mitochondria are selectively eliminated from eukaryotic cells after blockade of caspases during apoptosis. Curr Biol. 2001;11(5):361-5. https://doi.org/10.1016/S0960-9822(01)00100-2.
22.
Dagda RK, Cherra SJ, 3rd, Kulich SM, Tandon A, Park D, Chu CT. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem. 2009;284(20):13843-55. [PubMed ID: 19279012]. https://doi.org/10.1074/jbc.M808515200.

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