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Calcium Overload and Mitochondrial Metabolism
Open accessAbstract
Mitochondria calcium is a double-edged sword. While low levels of calcium are essential to maintain optimal rates of ATP production, extreme levels of calcium overcoming the mitochondrial calcium retention capacity leads to loss of mitochondrial function. In moderate amounts, however, ATP synthesis rates are inhibited in a calcium-titratable manner. While the consequences of extreme calcium overload are well-known, the effects on mitochondrial function in the moderately loaded range remain enigmatic. These observations are associated with changes in the mitochondria ultrastructure and cristae network. The present mini review/perspective follows up on previous studies using well-established cryo–electron microscopy and poses an explanation for the observable depressed ATP synthesis rates in mitochondria during calcium-overloaded states. The results presented herein suggest that the inhibition of oxidative phosphorylation is not caused by a direct decoupling of energy metabolism via the opening of a calcium-sensitive, proteinaceous pore but rather a separate but related calcium-dependent phenomenon. Such inhibition during calcium-overloaded states points towards mitochondrial ultrastructural modifications, enzyme activity changes, or an interplay between both events.
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“Ca2+ activates mitochondrial metabolism and stimulates ATP synthesis”
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Computer Visualization of Three-Dimensional Image Data Using IMOD
Kremer, J. R., Mastronarde, D. N., & McIntosh, J. R. (1996) · Journal of Structural Biology · doi:10.1006/jsbi.1996.0013 · Cited by 5,530
Mitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,546
Annexins: linking Ca2+ signalling to membrane dynamics
Gerke, V., Creutz, C. E., & Moss, S. E. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1661 · Cited by 1,412
The mitochondrial calcium uniporter is a highly selective ion channel
Kirichok, Y., Krapivinsky, G., & Clapham, D. E. (2004) · Nature · doi:10.1038/nature02246 · Cited by 1,409
Mitochondria and calcium: from cell signalling to cell death
Duchen, M. R. (2000) · The Journal of Physiology · doi:10.1111/j.1469-7793.2000.00057.x · Cited by 1,261
Microdomains of Intracellular Ca2+: Molecular Determinants and Functional Consequences
Rizzuto, R., & Pozzan, T. (2005) · Physiological Reviews · doi:10.1152/physrev.00004.2005 · Cited by 1,234
What is the mitochondrial permeability transition pore?
Halestrap, A. P. (2009) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.02.021 · Cited by 966
Role of Mitochondrial Ca2+ in the Regulation of Cellular Energetics
Glancy, B. C., & Balaban, R. S. (2012) · Biochemistry · doi:10.1021/bi2018909 · Cited by 649
Annexins – unique membrane binding proteins with diverse functions
Rescher, U., & Gerke, V. (2004) · Journal of Cell Science · doi:10.1242/jcs.01245 · Cited by 595
MICU1 Controls Both the Threshold and Cooperative Activation of the Mitochondrial Ca2+ Uniporter
Csordás, G., Golenár, T., Seifert, E. L., Kamer, K. J., Sancak, Y., Perocchi, F., Moffat, C., Weaver, D., de la Fuente, S., Bogorad, R. L., et al. (2013) · Cell Metabolism · doi:10.1016/j.cmet.2013.04.020 · Cited by 499
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- Andrade, L.O. (2019). Chapter Three—Annexins and Plasma Membrane Repai. Plasma Membrane Repair, Elsevier.
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Items 101–187 of 187
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Wang, Y., Xiang, Q., Wu, Y., Zhang, X., Huang, Z., Hou, Y., Wang, Y., Yang, J., Wan, W., Zou, H., et al. (2025) · Biomaterials Research · doi:10.34133/bmr.0255 · Cited by 3
Su, Z., Zeng, Y., Li, Q., Li, J., Zheng, G., Zhang, W., Xiao, Z., Chen, Z., Lin, Y., Liu, Z., et al. (2026) · Research · doi:10.34133/research.1137 · Cited by 3
Luo, X., Assal, D. C. E., Liu, Y., Ranjbar, S., & Fleming, R. M. T. (2025) · Frontiers in Computational Neuroscience · doi:10.3389/fncom.2025.1594330 · Cited by 3
Li, L., Wang, Z., Yan, H., Zhao, P., & Yuan, Y. (2025) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c04431 · Cited by 3
Pan, Q., Xu, H., Xiao, Z., Liu, G., Zhang, H., & Li, Y. (2025) · Human Molecular Genetics · doi:10.1093/hmg/ddaf091 · Cited by 3
Xu, Y.-W., Xie, S.-Q., Han, L., Xu, L., & Zhu, Y.-Q. (2025) · Acta Biochimica et Biophysica Sinica · doi:10.3724/abbs.2025153 · Cited by 2
Pei, Y., Wan, S., Qi, J., Xi, X., Zhu, Y., An, P., Luo, J., & Luo, Y. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26178475 · Cited by 3
Dubey, N., Singh, S., Panchbhai, P., Chaturvedi, G., Goyal, A., Singh, N., Bhatia, J., Yadav, R. K., Arava, S. K., Kumar, A., et al. (2026) · Cell Biochemistry and Biophysics · doi:10.1007/s12013-026-02054-8 · Cited by 2
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Meng, Q., Liu, J. G., Gao, Y., Liu, A., Liu, Y., Xia, Y., Xie, Z., He, S., Chen, L. X., Sulaman, U., et al. (2026) · Inflammation · doi:10.1007/s10753-026-02504-8 · Cited by 2
Zhang, Y., Li, X., Meng, Z., Ma, M., Huang, R., Liang, X., Liu, S., Wei, W., Huo, Y., Li, Y., et al. (2026) · Bioactive Materials · doi:10.1016/j.bioactmat.2026.03.037 · Cited by 2
雷, 小. (2023) · Advances in Clinical Medicine · doi:10.12677/acm.2023.1381847 · Cited by 2
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Ma, L., Yao, L., Zhang, Z., & Hao, B. (2025) · Human Cell · doi:10.1007/s13577-025-01174-2 · Cited by 2
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Choi, J. B., Do, H., Seol, D., Yang, H., Kim, T.-M., Byun, Y. G., Park, J.-M., Go, H., Park, J., Chung, W., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-94795-4 · Cited by 1
Gong, C., Li, S., An, Y., Yang, C., Tan, Z., Chen, W., Lv, D., Wu, H., Wang, H., Fu, S., et al. (2025) · Cell Calcium · doi:10.1016/j.ceca.2025.103071 · Cited by 1
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Pu, L., Wang, J., Nilsson, L., Zhao, L., Williams, C., Chi, G., Gilthorpe, J. D., Tuck, S., Henriksson, J., Tang, Y., et al. (2025) · PLoS Genetics · doi:10.1371/journal.pgen.1011554
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He, J., Ge, X., Lin, S., Bao, Y., Cheng, H., Hu, S., Feng, X., Fan, Q., Yang, Y. K., & Yang, X. (2025) · Journal of Environmental Sciences · doi:10.1016/j.jes.2025.05.022
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Xu, W., Ren, S., Li, Z., & Pang, L. (2025) · International Immunopharmacology · doi:10.1016/j.intimp.2025.115210
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Self-citationHaigh, S. B., Chen, F., Yu, Y., Bordán, Z., Li, X., Sridhar, S., Romero, M. J., Chakraborty, T., Csanyi, G., Joshua, A. T., et al. (2026) · Antioxidants · doi:10.3390/antiox15030275
Farombi, E. O., Ikeji, C. N., Akpan, M. M., Adedara, I. A., & Akinmoladun, C. A. (2026) · Advances in neurotoxicology · doi:10.1016/bs.ant.2025.04.008
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Shang, S., Zhai, Q., Huang, Y., Yin, J., Wang, J., & Shi, X. (2026) · Pharmaceuticals · doi:10.3390/ph19040601
Kim, M., Park, W., Lim, W., Song, G., & Park, S. (2026) · Environmental Toxicology and Pharmacology · doi:10.1016/j.etap.2026.105031
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Lin, T.-C., Lee, M.-J., Nguyen, N. T., Hsiao, S., Chen, Y., Chen, L.-H., Visitsattapongse, S., & Chiu, W. (2026) · Cell Calcium · doi:10.1016/j.ceca.2026.103151
Zhan, D., Li, D., Guo, S., Chai, X., Cao, R., Deng, W., Wu, K., Li, Y., Tsang, S. Y., Cai, Z., et al. (2026) · Toxics · doi:10.3390/toxics14050450
Marcinek, A., Katarzyńska, J., & Gebicki, J. L. (2026) · Frontiers in Aging · doi:10.3389/fragi.2026.1822261 · Cited by 1
Li, C., Zhao, S. S., Shi, C., Sun, S., He, Z., Xu, Y., Zheng, L., Tang, T., Qiu, S., Liang, K., et al. (2026) · Science China Life Sciences · doi:10.1007/s11427-025-3314-1
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Xing, L., Liu, A., Li, J., Yao, M., Song, J., Duan, P., & Li, H. (2026) · Molecular Neurobiology · doi:10.1007/s12035-026-05997-4
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Dastan, M., Bellut-Staeck, U. M., Zhou, J., & Lehmann, C. (2026) · Medical Hypotheses · doi:10.1016/j.mehy.2026.112055
Yan, Y., Jia, F., Gao, Z., Liang, C., & Geng, W. (2026) · Journal of Cellular Physiology · doi:10.1002/jcp.70203
Rubio, C., Serrano‐García, N., Pérez-Rubio, R., Pérez-Villavicencio, J., Parra, H. R., Lee, Á., & Rubio‐Osornio, M. (2026) · Journal of Integrative Neuroscience · doi:10.31083/jin52316
Guo, Z., Tian, J., Wei, X., Zhou, J., Meng, X., Mou, L., He, Y., Wei, J., Duan, J., Zuo, D., et al. (2026) · Cellular Signalling · doi:10.1016/j.cellsig.2026.112728
Selvam, K., Chinnaswamy, S. M., Jawahar, S., & Gunasekaran, V. (2026) · Egyptian Liver Journal · doi:10.1186/s43066-026-00526-3
Magawa, C. T., Eaton-Fitch, N., Muraki, K., & Marshall‐Gradisnik, S. (2026) · European Journal of Immunology · doi:10.1002/eji.70240
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Deshpande, A., Methner, A., Frey, N., & Rangrez, A. Y. (2026) · Trends Open · doi:10.1016/j.treopn.2026.07.005
Huang, W., Zhang, Q., Qiu, Y., Suo, H., Liu, Z., Bai, B., Wang, Q., & Zhou, Q. (2026) · Advanced Science · doi:10.1002/advs.76941
Chen, Z., Wu, H., Chen, S., Rao, Y., Yan, J., Ran, B., Zeng, Q., Cao, J., Yang, X., cao, H., et al. (2026) · Nano Today · doi:10.1016/j.nantod.2026.103152
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Li, J., Fu, J., Pan, Y., Zheng, H., & Xing, X. (2026) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2026.1903038
Huang, Y., Zheng, Y., Zhang, Q., Fan, Y., Zhou, F., Ma, Y., Yan, J., Chen, J., Wang, F., Tan, Y., et al. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.71736
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Sun, N., Sun, P., Xuan, F., Zhong, J., Ma, W., Song, Y., Xuan, H., Yu, D., Sun, Z., Zhao, Y., et al. (2026) · Cell Reports · doi:10.1016/j.celrep.2026.118036
Xu, J., Yang, J., Sun, W., Shi, Q., Ni, Q., Chen, J., Luan, C., Ma, X., & Yang, C. (2026) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2026.131010
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Sheng, J., & Zheng, X. (2026) · ACS Synthetic Biology · doi:10.1021/acssynbio.6c00350
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Roth, C. I., Vadovsky, A. C., Steele, K. J., Raftu, A., Shaman, S., Roberts, J. G., & Bazil, J. N. (2026) · Mitochondrion · doi:10.1016/j.mito.2026.102222
Self-citationYang, H., Zhao, Y., Mu, S., Wang, S., Tong, A., Wang, D., Jia, J., & Li, J. (2026) · Chemical Engineering Journal · doi:10.1016/j.cej.2026.182945
窦报敏, Chen, J., Zhao, H., Sun-Yan, A., Zhu, X., & Xu, Y. (2026) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2026.109130
Metadata
- Authors
- Walkon, L. L., Strubbe-Rivera, J. O., & Bazil, J. N.
- Affiliations
- Michigan State University (US)
- Department of Pharmacology and Toxicology, Michigan State University, East Lansing, MI 48824, USA
- Venue
- Biomolecules
- Publisher
- MDPI AG
- Published
- 2022-12-17
- Volume
- 12
- Issue
- 12
- Pages
- 1891
- ISSN
- 2218-273X (ISSN-L)
- PMC
- PMC9775684
- OpenAlex
- W4313236994
- Cited by
- 187
- References
- 95
- Citations by year
- 2026: 50 · 2025: 75 · 2024: 50 · 2023: 12
- FWCI
- 3.57
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- Biomolecules (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Institutes of Health (F31HL152623)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
- Keywords
- mitochondrial calcium overload, mitochondrial calcium retention capacity, ATP synthesis inhibition, oxidative phosphorylation, mitochondrial ultrastructure, cryo-electron microscopy, mitochondrial function
- MeSH terms
- Adenosine Triphosphate, Calcium, Energy Metabolism, Mitochondria, Cryoelectron Microscopy
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