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Regulation of mitochondrial dynamics in acute kidney injury in cell culture and rodent models
Open accessAbstract
The mechanism of mitochondrial damage, a key contributor to renal tubular cell death during acute kidney injury, remains largely unknown. Here, we have demonstrated a striking morphological change of mitochondria in experimental models of renal ischemia/reperfusion and cisplatin-induced nephrotoxicity. This change contributed to mitochondrial outer membrane permeabilization, release of apoptogenic factors, and consequent apoptosis. Following either ATP depletion or cisplatin treatment of rat renal tubular cells, mitochondrial fragmentation was observed prior to cytochrome c release and apoptosis. This mitochondrial fragmentation was inhibited by Bcl2 but not by caspase inhibitors. Dynamin-related protein 1 (Drp1), a critical mitochondrial fission protein, translocated to mitochondria early during tubular cell injury, and both siRNA knockdown of Drp1 and expression of a dominant-negative Drp1 attenuated mitochondrial fragmentation, cytochrome c release, caspase activation, and apoptosis. Further in vivo analysis revealed that mitochondrial fragmentation also occurred in proximal tubular cells in mice during renal ischemia/reperfusion and cisplatin-induced nephrotoxicity. Notably, both tubular cell apoptosis and acute kidney injury were attenuated by mdivi-1, a newly identified pharmacological inhibitor of Drp1. This study demonstrates a rapid regulation of mitochondrial dynamics during acute kidney injury and identifies mitochondrial fragmentation as what we believe to be a novel mechanism contributing to mitochondrial damage and apoptosis in vivo in mouse models of disease.
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“For example, mitochondrial fission occurs in the kidneys and heart after acute ischemia/reperfusion injury in mice, and prevention of this process is beneficial (5, 32).”
From Mitochondrial Fission Contributes to Mitochondrial Dysfunction and Insulin Resistance in Skeletal Muscle (2012) · cites this paper as [5]
In the citing paper
“For example, mitochondrial fission occurs in the kidneys and heart after acute ischemia/reperfusion injury in mice, and prevention of this process is beneficial (5, 32).”
From Mitochondrial Fission Contributes to Mitochondrial Dysfunction and Insulin Resistance in Skeletal Muscle (2012) · cites this paper as [5]
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“Moreover, these studies revealed that silencing of Drp1 expression was not associated with reduced translocation of the pro-apoptotic protein Bax to mitochondria, suggesting that Drp1 functions downstream of Bax during apoptosis.”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Brooks et al., 2009
In the citing paper
“The role of mitochondrial dynamics in regulating apoptosis is mainly based on the finding that overexpression of the dominant-negative mutant Drp1K38A induces mitochondrial fusion and confers resistance to apoptosis by preventing a loss of Δψm and inhibiting cytochrome c release (Breckenridge et al., 2003; Brooks et al., 2009; Frank et al., 2001; Karbowski et al., 2002).”
From New insights into the role of mitochondria in aging: mitochondrial dynamics and more (2010) · cites this paper as Brooks et al., 2009
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Citations
Cites
The BCL-2 protein family: opposing activities that mediate cell death
Youle, R. J., & Strasser, A. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2308 · Cited by 4,806
Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
(2001) · PubMed · Cited by 2,381
Cisplatin nephrotoxicity: Mechanisms and renoprotective strategies
Pabla, N., & Dong, Z. (2008) · Kidney International · doi:10.1038/sj.ki.5002786 · Cited by 1,959
Self-citationDynamin-related Protein Drp1 Is Required for Mitochondrial Division in Mammalian Cells
Smirnova, E., Griparić, L., Shurland, D., & van der Bliek, A. M. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.8.2245 · Cited by 1,938
Disruption of Fusion Results in Mitochondrial Heterogeneity and Dysfunction
Chen, H., Chomyn, A., & Chan, D. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m503062200 · Cited by 1,376
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
Cassidy-Stone, A., Chipuk, J. E., Ingerman, E., Song, C., Yoo, C., Kuwana, T., Kurth, M. J., Shaw, J. T., Hinshaw, J. E., Green, D. R., et al. (2008) · Developmental Cell · doi:10.1016/j.devcel.2007.11.019 · Cited by 1,200
Cribbs, J. T., & Strack, S. (2007) · EMBO Reports · doi:10.1038/sj.embor.7401062 · Cited by 1,061
Roles of the mammalian mitochondrial fission and fusion mediators Fis1, Drp1, and Opa1 in apoptosis
Lee, Y.-J., Jeong, S.-Y., Karbowski, M., Smith, C. L., & Youle, R. J. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-04-0294 · Cited by 1,042
Update on Mechanisms of Ischemic Acute Kidney Injury
Devarajan, P. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2006010017 · Cited by 1,026
Mitochondrial Fusion and Fission in Mammals
Chan, D. C. (2006) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.22.010305.104638 · Cited by 972
Breaking the mitochondrial barrier
Martinou, J., & Green, D. R. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35048069 · Cited by 950
Life-or-death decisions by the Bcl-2 protein family
Adams, J. M., & Cory, S. (2001) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(00)01740-0 · Cited by 888
Karbowski, M., Lee, Y.-J., Gaume, B., Jeong, S.-Y., Frank, S., Nechushtan, A., Santel, A., Fuller, M., Smith, C. L., & Youle, R. J. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200209124 · Cited by 846
Mitochondrial fission in apoptosis
Youle, R. J., & Karbowski, M. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1697 · Cited by 773
Recent Advances in the Pathophysiology of Ischemic Acute Renal Failure
Bonventre, J. V., & Weinberg, J. M. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000079785.13922.f6 · Cited by 766
Incidence and Mortality of Acute Renal Failure in Medicare Beneficiaries, 1992 to 2001
Xue, J. L., Daniels, F., Star, R. A., Kimmel, P. L., Eggers, P. W., Molitoris, B. A., Himmelfarb, J., & Collins, A. J. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2005060668 · Cited by 765
A Lethal Defect of Mitochondrial and Peroxisomal Fission
Waterham, H. R., Koster, J., van Roermund, C. W. T., Mooyer, P. A. W., Wanders, R. J. A., & Leonard, J. V. (2007) · New England Journal of Medicine · doi:10.1056/nejmoa064436 · Cited by 749
Mitochondrial Morphology and Dynamics in Yeast and Multicellular Eukaryotes
Okamoto, K., & Shaw, J. M. (2005) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.093019 · Cited by 737
Acute renal failure: definitions, diagnosis, pathogenesis, and therapy
Schrier, R. W., Wang, W., Poole, B., & Mitra, A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci22353 · Cited by 683
Nitric oxide‐induced mitochondrial fission is regulated by dynamin‐related GTPases in neurons
Barsoum, M. J., Yuan, H., Gerencser, A. A., Liot, G., Kushnareva, Y., Gräber, S., Kovács, I., Lee, W. D., Waggoner, J., Cui, J., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601253 · Cited by 677
Acute renal failure: definitions, diagnosis, pathogenesis, and therapy
Schrier, R. W., Wang, W., Poole, B., & Mitra, A. (2004) · Journal of Clinical Investigation · doi:10.1172/jci200422353 · Cited by 640
Mitochondrial bioenergetics and structural network organization
Benard, G., Bellance, N., James, D., Parrone, P., Fernandez, H., Letellier, T., & Rossignol, R. (2007) · Journal of Cell Science · doi:10.1242/jcs.03381 · Cited by 618
Declining Mortality in Patients with Acute Renal Failure, 1988 to 2002
Waikar, S. S., Curhan, G. C., Wald, R., McCarthy, E. P., & Chertow, G. M. (2006) · Journal of the American Society of Nephrology · doi:10.1681/asn.2005091017 · Cited by 587
Wasiak, S., Zunino, R., & McBride, H. M. (2007) · The Journal of Cell Biology · doi:10.1083/jcb.200610042 · Cited by 537
The role of the Bcl-2 family in the regulation of outer mitochondrial membrane permeability
Harris, M. H., & Thompson, C. B. (2000) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4400781 · Cited by 517
Padanilam, B. J. (2003) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00284.2002 · Cited by 373
Bak regulates mitochondrial morphology and pathology during apoptosis by interacting with mitofusins
Brooks, C., Wei, Q., Feng, L., Dong, G., Tao, Y., Mei, L., Xie, Z.-J., & Dong, Z. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0703976104 · Cited by 351
Self-citationThe cell biology of ischemic renal injury
Weinberg, J. M. (1991) · Kidney International · doi:10.1038/ki.1991.58 · Cited by 336
DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
Jagasia, R., Grote, P., Westermann, B., & Conradt, B. (2005) · Nature · doi:10.1038/nature03316 · Cited by 319
ATR-Chk2 Signaling in p53 Activation and DNA Damage Response during Cisplatin-induced Apoptosis
Pabla, N., Huang, S., Mi, Q.-S., Daniel, R., & Dong, Z. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m707568200 · Cited by 309
Self-citationRole of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury
Saikumar, P., Dong, Z., Patel, Y., Hall, K., Hopfer, U., Weinberg, J. M., & Venkatachalam, M. A. (1998) · Oncogene · doi:10.1038/sj.onc.1202590 · Cited by 296
Self-citationBax- or Bak-Induced Mitochondrial Fission Can Be Uncoupled from Cytochrome c Release
Sheridan, C., Delivani, P., Cullen, S. P., & Martin, S. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.08.002 · Cited by 276
Acute renal failure. II. Experimental models of acute renal failure: imperfect but indispensable
Lieberthal, W., & Nigám, S. K. (2000) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.2000.278.1.f1 · Cited by 269
Molecular Machinery of Mitochondrial Fusion and Fission
Westermann, B. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.r800011200 · Cited by 258
Mechanisms of Renal Apoptosis in Health and Disease
Sanz, A. B., Accent]a, B. S. A., Ruiz‐Ortega, M., Egido, J., & Ortíz, A. (2008) · Journal of the American Society of Nephrology · doi:10.1681/asn.2007121336 · Cited by 247
The mechanism of IL-5 signal transduction
Adachi, T., & Alam, R. (1998) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.1998.275.3.c623 · Cited by 245
Minocycline Up-regulates Bcl-2 and Protects against Cell Death in Mitochondria
Wang, J., Wei, Q., Wang, C., Hill, W., Hess, D. C., & Dong, Z. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313629200 · Cited by 242
Self-citationThe mitochondrial protein MTP18 contributes to mitochondrial fission in mammalian cells
Tondera, D., Czauderna, F., Paulick, K., Schwarzer, R., Kaufmann, J., & Santel, A. (2005) · Journal of Cell Science · doi:10.1242/jcs.02415 · Cited by 239
Activation and involvement of p53 in cisplatin-induced nephrotoxicity
Wei, Q., Dong, G., Yang, T., Megyesi, J. K., Price, P. M., & Dong, Z. (2007) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00230.2007 · Cited by 232
Self-citationThe pathological role of Bax in cisplatin nephrotoxicity
Wei, Q., Dong, G., Franklin, J. L., & Dong, Z. (2007) · Kidney International · doi:10.1038/sj.ki.5002256 · Cited by 228
Self-citationAcute renal failure. I. Relative importance of proximal vs. distal tubular injury
Lieberthal, W., & Nigám, S. K. (1998) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.1998.275.5.f623 · Cited by 220
Regulation of PUMA-α by p53 in cisplatin-induced renal cell apoptosis
Jiang, M., Wei, Q., Wang, J., Du, Q., Yu, J., Zhang, L., & Dong, Z. (2006) · Oncogene · doi:10.1038/sj.onc.1209440 · Cited by 214
Self-citationRevisiting the host as a growth medium
Brown, S. A., Palmer, K. L., & Whiteley, M. (2008) · Nature Reviews Microbiology · doi:10.1038/nrmicro1955 · Cited by 210
Servais, H., Ortíz, A., Devuyst, O., Denamur, S., Tulkens, P. M., & Mingeot‐Leclercq, M. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0151-z · Cited by 193
Castaneda, M. P., Swiatecka‐Urban, A., Mitsnefes, M. M., Feuerstein, D., Kaskel, F. J., TELLIS, V. A., & Devarajan, P. (2003) · Transplantation · doi:10.1097/01.tp.0000069835.95442.9f · Cited by 192
Mitochondrial fusion and fission in the control of apoptosis
Perfettini, J., Roumier, T., & Kroemer, G. (2005) · Trends in Cell Biology · doi:10.1016/j.tcb.2005.02.005 · Cited by 180
Breckenridge, D. G., Kang, B., Kokel, D., Mitani, S., Staehelin, L. A., & Xue, D. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.07.015 · Cited by 149
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Kaushal, G. P., Basnakian, A. G., & Shah, S. V. (2004) · Kidney International · doi:10.1111/j.1523-1755.2004.761_6.x · Cited by 148
Shared components of mitochondrial and peroxisomal division
Schrader, M. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.01.004 · Cited by 134
Transitioning to Therapy in Ischemic Acute Renal Failure
Molitoris, B. A. (2003) · Journal of the American Society of Nephrology · doi:10.1097/01.asn.0000048852.53881.d9 · Cited by 114
Brooks, C. R., & Dong, Z. (2007) · Cell Cycle · doi:10.4161/cc.6.24.5115 · Cited by 93
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Dong, Z., & Wang, J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312225200 · Cited by 86
Self-citationBid deficiency ameliorates ischemic renal failure and delays animal death in C57BL/6 mice
Wei, Q., Yin, X., Wang, M.-H., & Dong, Z. (2005) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00184.2005 · Cited by 72
Self-citationMitochondrial Dynamics: To be in Good Shape to Survive
Herzig, S., & Martinou, J. (2008) · Current Molecular Medicine · doi:10.2174/156652408783769625 · Cited by 64
Mitochondrial Dynamics and Apoptosis: A Painful Separation
James, D. I., & Martinou, J. (2008) · Developmental Cell · doi:10.1016/j.devcel.2008.08.011 · Cited by 43
Characterization of cell clones isolated from hypoxia-selected renal proximal tubular cells
Brooks, C. R., Wang, J., Yang, T., & Dong, Z. (2006) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00236.2006 · Cited by 11
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Metadata
- Authors
- Brooks, C., Wei, Q., Cho, S.-G., & Dong, Z.
- Affiliations
- Charlie Norwood VA Medical Center (US)
- Corresponding author
- Dong, Zheng
- Venue
- Journal of Clinical Investigation
- Published
- 2009-05-01
- Volume
- 119
- Issue
- 5
- Pages
- 1275-1285
- ISSN
- 0021-9738 (ISSN-L)
- PMC
- PMC2673870
- OpenAlex
- W2155978870
- Cited by
- 735
- References
- 58
- Citations by year
- 2026: 24 · 2025: 31 · 2024: 51 · 2023: 34 · 2022: 59 · 2021: 49 · 2020: 64 · 2019: 59 · 2018: 43 · 2017: 54 · 2016: 42 · 2015: 40 · 2014: 45 · 2013: 36 · 2012: 41
- FWCI
- 13.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Journal of Clinical Investigation (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- U.S. Department of Veterans Affairs
- Brigham and Women's Hospital
- Silence Therapeutics
- National Institutes of Health
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial dynamics, mitochondrial fragmentation, acute kidney injury, apoptosis, mitochondrial outer membrane permeabilization, cytochrome c release, Drp1, Mdivi-1, renal ischemia-reperfusion, cisplatin nephrotoxicity, Bcl-2, caspase activation, ATP depletion
- MeSH terms
- Adenosine Triphosphate, Animals, Cell Line, Cells, Cultured, Cisplatin, Enzyme Inhibitors, Kidney Tubular Necrosis, Acute, Kidney Tubules, Proximal, Male, Mice, Inbred C57BL, Microtubule-Associated Proteins, Mitochondria, Reperfusion Injury, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Sodium Azide, GTP Phosphohydrolases, Imaging, Three-Dimensional, Dynamins, RNA, Small Interfering, Cytochromes c, Mice, Rats, Caspase Inhibitors
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