The DOI matches its Crossref record; 13 of the 13 references it cites were found in a registry or an index.
Mitochondrial Ca2+ and apoptosis
Open accessAbstract
Mitochondria are key decoding stations of the apoptotic process. In support of this view, a large body of experimental evidence has unambiguously revealed that, in addition to the well-established function of producing most of the cellular ATP, mitochondria play a fundamental role in triggering apoptotic cell death. Various apoptotic stimuli cause the release of specific mitochondrial pro-apoptotic factors into the cytosol. The molecular mechanism of this release is still controversial, but there is no doubt that mitochondrial calcium (Ca2+) overload is one of the pro-apoptotic ways to induce the swelling of mitochondria, with perturbation or rupture of the outer membrane, and in turn the release of mitochondrial apoptotic factors into the cytosol. Here, we review as different proteins that participate in mitochondrial Ca2+ homeostasis and in turn modulate the effectiveness of Ca2+-dependent apoptotic stimuli. Strikingly, the final outcome at the cellular level is similar, albeit through completely different molecular mechanisms: a reduced mitochondrial Ca2+ overload upon pro-apoptotic stimuli that dramatically blunts the apoptotic response.
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Cites
1 retracted
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RetractedApoptosis in the Pathogenesis and Treatment of Disease
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The versatility and universality of calcium signalling
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Mitochondrial membrane permeabilization in cell death
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Mitochondria and cell death: outer membrane permeabilization and beyond
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The p66shc adaptor protein controls oxidative stress response and life span in mammals
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“At he early phase of apoptosis, simultaneously with cytochrome c elease (before caspases activation), fragmentation of the mitohondrial network has been observed [30].”
BackgroundCárdenas, C., Miller, R. A., Smith, I., Bui, T., Molgó, J., Müller, M., Vais, H., Cheung, K.-H., Yang, J., Parker, I., et al. (2010) · Cell · doi:10.1016/j.cell.2010.06.007 · Cited by 1,026
Function of Mitochondrial Stat3 in Cellular Respiration
Wegrzyn, J., Potla, R., Chwae, Y.-J., Sepuri, N. B. V., Zhang, Q., Koeck, T., Derecka, M., Szczepanek, K., Szelag, M., Gornicka, A., et al. (2009) · Science · doi:10.1126/science.1164551 · Cited by 1,014
VDAC2 Inhibits BAK Activation and Mitochondrial Apoptosis
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Cited by
The machineries, regulation and cellular functions of mitochondrial calcium
Giorgi, C., Marchi, S., & Pinton, P. (2018) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-018-0052-8 · Cited by 941
Self-citationThe endoplasmic reticulum–mitochondria connection: One touch, multiple functions
Marchi, S., Patergnani, S., & Pinton, P. (2014) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2013.10.015 · Cited by 475
Self-citationAntioxidants of Edible Mushrooms
Kozarski, M., Klaus, A., Jakovljevic, D., Todorovic, N., Vunduk, J., Petrović, P., Niksic, M., Vrvic, M., & Van Griensven, L. (2015) · Molecules · doi:10.3390/molecules201019489 · Cited by 413
BAP1 regulates IP3R3-mediated Ca2+ flux to mitochondria suppressing cell transformation
Bononi, A., Giorgi, C., Patergnani, S., Larson, D., Verbruggen, K., Tanji, M., Pellegrini, L., Signorato, V., Olivetto, F., Pastorino, S., et al. (2017) · Nature · doi:10.1038/nature22798 · Cited by 401
Self-citationBonora, M., Wieckowski, M. R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., & Pinton, P. (2015) · Oncogene · doi:10.1038/onc.2014.96 · Cited by 330
Self-citation
Metadata
- Authors
- Giorgi, C., Baldassari, F., Bononi, A., Bonora, M., De Marchi, E., Marchi, S., Missiroli, S., Patergnani, S., Rimessi, A., Suski, J. M., Wieckowski, M. R., & Pinton, P.
- Venue
- Cell Calcium
- Publisher
- Elsevier BV
- Published
- 2012-07
- Volume
- 52
- Issue
- 1
- Pages
- 36-43
- ISSN
- 0143-4160 (ISSN-L)
- OpenAlex
- W2024866328
- Cited by
- 474
- References
- 13
- FWCI
- 9.53
- Type
- journal article
- Language
- en
- Open access
- green
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