Abstract
Mitochondria supply energy to cells by generating ATP; thus it can be considered as one of the essential organelles of the cell. For the efficient working of cells, a good quality of mitochondria is essential; thus the elimination of injured or nonfunctional mitochondria by means of mitophagy is a very important process for cell function. Mitophagy showed a neuroprotective property in cerebral ischemia by accurate labeling and entrapment of defective mitochondria into isolation membranes. Then the entrapped mitochondria were digested by lysosomes. Therefore, the regulation of mitophagy in ischemic brain injury may be used as a therapeutic strategy to protect the neuron by the efficient removal of injured mitochondria.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Paliwal, P., Dash, D., & Krishnamurthy, S. (2017). Pharmacokinetic study of piracetam in focal cerebral ischemic rats. European Journal of Drug Metabolism and Pharmacokinetics, 1–9.
Paliwal, P., Chauhan, G., Gautam, D., Dash, D., Patne, S. C. U., & Krishnamurthy, S. (2018). Indole-3-Carbinol improves neurobehavioral symptoms in a cerebral ischemic stroke model. Naunyn-Schmiedeberg’s Archives of Pharmacology, 391, 613–625.
Lipton, P. (1999). Ischemic cell death in brain neurons. Physiological Reviews, 79, 1431–1568.
Carloni, S., Girelli, S., Scopa, C., Buonocore, G., Longini, M., & Balduini, W. (2010). Activation of autophagy and Akt/CREB signaling play an equivalent role in the neuroprotective effect of rapamycin in neonatal hypoxia-ischemia. Autophagy, 6, 366–377.
Deter, R. L., & De Duve, C. (1967). Influence of glucagon, an inducer of cellular autophagy, on some physical properties of rat liver lysosomes. The Journal of Cell Biology, 33, 437–449.
Deter, R. L., Baudhuin, P., & De Duve, C. (1967). Participation of lysosomes in cellular autophagy induced in rat liver by glucagon. The Journal of Cell Biology, 35, C11–C16.
Yu, L., Alva, A., Su, H., Dutt, P., Freundt, E., Welsh, S., Baehrecke, E. H., & Lenardo, M. J. (2004). Regulation of an ATG7-beclin 1 program of autophagic cell death by caspase-8. Science, 304(5676), 1500–1502.
Liu, L., Sakakibar, a. K., Chen, Q., & Okamoto, K. (2014). Receptor-mediated mitophagy in yeast and mammalian systems. Cell Research, 24, 787–795.
Santos, R. X., SC, C. a., Wang, X., Perry, G., Smith, M. A., Moreira, P. I., et al. (2010). A synergistic dysfunction of mitochondrial fission/fusion dynamics and mitophagy in Alzheimer’s disease. Journal of Alzheimer’s Disease, 20(2), 401–412.
Vives-Bauza, C., & Przedborski, S. (2011). Mitophagy: The latest problem for Parkinson’s disease. Trends in Molecular Medicine, 17(3), 158–165.
Zhang, X., Yan, H., Yuan, Y., Gao, J., Shen, Z., Cheng, Y., Shen, Y., Wang, R. R., Wang, X., Hu, W. W., & Wang, G. (2013). Cerebral ischemia-reperfusion-induced autophagy protects against neuronal injury by mitochondrial clearance. Autophagy, 9(9), 1321–1333.
Zuo, W., Zhang, S., Xia, C. Y., Guo, X. F., He, W. B., & Chen, N. H. (2014). Mitochondria autophagy is induced after hypoxic/ischemic stress in a Drp1 dependent manner: The role of inhibition of Drp1 in ischemic brain damage. Neuropharmacology, 86, 103–115.
Huang, C., Andres, A. M., Ratliff, E. P., Hernandez, G., Lee, P., & Gottlieb, R. A. (2011). Preconditioning involves selective mitophagy mediated by Parkin and p62/SQSTM1. PLoS One, 6(6), e20975.
Li, Q., Zhang, T., Wang, J., Zhang, Z., Zhai, Y., Yang, G. Y., & Sun, X. (2014). Rapamycin attenuates mitochondrial dysfunction via activation of mitophagy in experimental ischemic stroke. Biochemical and Biophysical Research Communications, 444, 182–188.
Youle, R. J., & Narendra, D. P. (2011). Mechanisms of mitophagy. Nature Reviews Molecular Cell Biology, 12(1), 9.
Kroemer, G., Dallaporta, B., & Resche-Rigon, M. (1998). The mitochondrial death/life regulator in apoptosis and necrosis. Annual Review of Physiology, 60(1), 619–642.
Chen, H., & Chan, D. C. (2010). Physiological functions of mitochondrial fusion. Annals of the New York Academy of Sciences, 1201, 21–25.
Chen, H., Chomyn, A., & Chan, D. C. (2005). Disruption of fusion results in mitochondrial heterogeneity and dysfunction. The Journal of Biological Chemistry, 280, 26185–26192.
Detmer, S. A., & Chan, D. C. (2007). Functions and dysfunctions of mitochondrial dynamics. Nature Reviews Molecular Cell Biology, 8, 870–879.
Cipolat, S., Rudka, T., Hartmann, D., Costa, V., Serneels, L., Craessaerts, K., Metzger, K., Frezza, C., Annaert, W., D'Adamio, L., & Derks, C. (2006). Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell, 126(1), 163–175.
Züchner, S., Mersiyanova, I. V., Muglia, M., Bissar-Tadmouri, N., Rochelle, J., Dadali, E. L., Zappia, M., Nelis, E., Patitucci, A., Senderek, J., & Parman, Y. (2004). Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nature Genetics, 36(5), 449.
Alexander, C., Votruba, M., Pesch, U. E., Thiselton, D. L., Mayer, S., Moore, A., Rodriguez, M., Kellner, U., Leo-Kottler, B., Auburger, G., & Bhattacharya, S. S. (2000). OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nature Genetics, 26(2), 211.
Chang, C. R., Manlandro, C. M., Arnoult, D., Stadler, J., Posey, A. E., Hill, R. B., & Blackstone, C. (2010). A lethal de novo mutation in the middle domain of the dynamin-related GTPase Drp1 impairs higher order assembly and mitochondrial division. Journal of Biological Chemistry, 285(42), 32494–32503.
James, D. I., Parone, P. A., Mattenberger, Y., & Martinou, J. C. (2003). hFis1, a novel component of the mammalian mitochondrial fission machinery. The Journal of Biological Chemistry, 278, 36373–36379.
Smirnova, E., Shurland, D. L., Ryazantsev, S. N., & van der Bliek, A. M. (1998). A human dynamin-related protein controls the distribution of mitochondria. The Journal of Cell Biology, 143, 351–358.
Ishihara, N., Nomura, M., & Jofuku, A. (2009). Mitochondrial fission factor Drp1 is essential for embryonic development and synapse formation in mice. Nature Cell Biology, 11, 958–966.
Hoppins, S., Lackner, L., & Nunnari, J. (2007). The machines that divide and fuse mitochondria. Annual Review of Biochemistry, 76, 751–780.
Takagi, H., Matsui, Y., Hirotani, S., Sakoda, H., Asano, T., & Sadoshima, J. (2007). AMPK mediates autophagy during myocardial ischemia in vivo. Autophagy, 3, 405–407.
Mengesdorf, T., Jensen, P. H., Mies, G., Aufenberg, C., & Paschen, W. (2002). Down-regulation of parkin protein in transient focal cerebral ischemia: A link between stroke and degenerative disease? Proceedings of the National Academy of Sciences of the United States of America, 99, 15042–15047.
Tang, Y. C., Tian, H. X., Yi, T., & Chen, H. B. (2016). The critical roles of mitophagy in cerebral ischemia. Protein & Cell, 7(10), 699–713.
Wang, P., Guan, Y. F., Du, H., Zhai, Q. W., Su, D. F., & Miao, C. Y. (2012). Induction of autophagy contributes to the neuroprotection of nicotinamide phosphoribosyltransferase in cerebral ischemia. Autophagy, 8(1), 77–87.
Yamamori, T., Ike, S., Bo, T., Sasagawa, T., Sakai, Y., Suzuki, M., Yamamoto, K., Nagane, M., Yasui, H., & Inanami, O. (2015). Inhibition of the mitochondrial fission protein dynamin-related protein 1 (Drp1) impairs mitochondrial fission and mitotic catastrophe after x-irradiation. Molecular Biology of the Cell, 26(25), 4607–4617.
Gomes, L. C., Di Benedetto, G., & Scorrano, L. (2011). During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nature Cell Biology, 13, 589–598.
Kumari, S., Anderson, L., Farmer, S., Mehta, S. L., & Li, P. A. (2012). Hyperglycemia alters mitochondrial fission and fusion proteins in mice subjected to cerebral ischemia and reperfusion. Translational Stroke Research, 3, 296–304.
Zuo, W., Yang, P. F., Chen, J., Zhang, Z., & Chen, N. H. (2016). Drp-1, a potential therapeutic target for brain ischaemic stroke. British Journal of Pharmacology, 173(10), 1665–1677.
Gurung, P., Lukens, J. R., & Kanneganti, T. D. (2015). Mitochondria: Diversity in the regulation of the NLRP3 inflammasome. Trends in Molecular Medicine, 21, 193–201.
Zhong, Z., Umemura, A., Sanchez-Lopez, E., Liang, S., Shalapour, S., Wong, J., He, F., Boassa, D., Perkins, G., Ali, S. R., & McGeough, M. D. (2016). NF-κB restricts inflammasome activation via elimination of damaged mitochondria. Cell, 164(5), 896–910.
Zhao, J., Mou, Y., Bernstock, J. D., Klimanis, D., Wang, S., Spatz, M., Maric, D., Johnson, K., Klinman, D. M., Li, X., & Li, X. (2015). Synthetic oligodeoxynucleotides containing multiple telemeric TTAGGG motifs suppress inflammasome activity in macrophages subjected to oxygen and glucose deprivation and reduce ischemic brain injury in stroke-prone spontaneously hypertensive rats. PLoS One, 10(10), e0140772.
Malagelada, C., Jin, Z. H., Jackson-Lewis, V., Przedborski, S., & Greene, L. A. (2010). Rapamycin protects against neuron death in in vitro and in vivo models of Parkinson’s disease. The Journal of Neuroscience, 30, 1166–1175.
Miclescu, A., Sharma, H. S., Martijn, C., & Wiklund, L. (2010). Methylene blue protects the cortical blood–brain barrier against ischemia/reperfusion-induced disruptions. Critical Care Medicine, 38, 2199–2206.
Di, Y., He, Y. L., Zhao, T., Huang, X., Wu, K. W., Liu, S. H., Zhao, Y. Q., Fan, M., Wu, L. Y., & Zhu, L. L. (2015). Methylene blue reduces acute cerebral ischemic injury via the induction of mitophagy. Molecular Medicine, 21, 420–429.
Jin, R., Yang, G., & Li, G. (2010). Inflammatory mechanisms in ischemic stroke: Role of inflammatory cells. Journal of Leukocyte Biology, 87, 779–789.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2019 Springer Nature Singapore Pte Ltd.
About this chapter
Cite this chapter
Paliwal, P., Krishnamurthy, S., Kumar, G., Patnaik, R. (2019). Critical Role of Mitochondrial Autophagy in Cerebral Stroke. In: Patnaik, R., Tripathi, A., Dwivedi, A. (eds) Advancement in the Pathophysiology of Cerebral Stroke. Springer, Singapore. https://doi.org/10.1007/978-981-13-1453-7_6
Download citation
DOI: https://doi.org/10.1007/978-981-13-1453-7_6
Published:
Publisher Name: Springer, Singapore
Print ISBN: 978-981-13-1452-0
Online ISBN: 978-981-13-1453-7
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)