Effect of oxidative stress on dynamics of mitochondrial reticulum

Pletjushkina, Olga Yu.; Lyamzaev, Konstantin G.; Попова, Е. Н.; Nepryakhina, O. K.; Ivanova, O. Yu.; Domnina, L. V.; Chernyak, Boris V.; Vp, Skulachev

doi:10.1016/j.bbabio.2006.03.018

Cited by 122 publications

(72 citation statements)

References 19 publications

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“…Thus, cleavage of both molecules of cyto.c1 in the same complex would result in the loss of its physical interaction with cyto.c and mitochondrial functions. In addition, the cleavage of cyto.c1 could affect the respiration status, ROS production and redox potential of mitochondria that may also contribute to cyto.c release in normal cells [35,36]. It should be noted that reduced form of cyto.c functions as an electron acceptor and physically interacts with cyto.…”

Section: Discussionmentioning

confidence: 99%

Caspase cleavage of cytochrome c1 disrupts mitochondrial function and enhances cytochrome c release

Zhu

Wang

et al. 2011

Cell Res

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Mitochondrial catastrophe can be the cause or consequence of apoptosis and is associated with a number of pathophysiological conditions. The exact relationship between mitochondrial catastrophe and caspase activation is not completely understood. Here we addressed the underlying mechanism, explaining how activated caspase could feedback to attack mitochondria to amplify further cytochrome c (cyto.c) release. We discovered that cytochrome c1 (cyto.c1) in the bc1 complex of the mitochondrial respiration chain was a novel substrate of caspase 3 (casp.3). We found that cyto.c1 was cleaved at the site of D106, which is critical for binding with cyto.c, following apoptotic stresses or targeted expression of casp.3 into the mitochondrial intermembrane space. We demonstrated that this cleavage was closely linked with further cyto.c release and mitochondrial catastrophe. These mitochondrial events could be effectively blocked by expressing non-cleavable cyto.c1 (D106A) or by caspase inhibitor z-VAD-fmk. Our results demonstrate that the cleavage of cyto.c1 represents a critical step for the feedback amplification of cyto.c release by caspases and subsequent mitochondrial catastrophe.

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Section: Discussionmentioning

confidence: 99%

Caspase cleavage of cytochrome c1 disrupts mitochondrial function and enhances cytochrome c release

Zhu

Wang

et al. 2011

Cell Res

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“…Depolarization and oxidative stress have been shown to inhibit mitochondrial fusion and/or to promote mitochondrial fragmentation (3,(27)(28)(29). Indeed, CCCP treatment led to mitochondrial fragmentation, which was not dependent on the autophagy machinery ( Fig.…”

Section: Mitochondrial Spheroid Formation Is a Response To Oxidative mentioning

confidence: 94%

Parkin and Mitofusins Reciprocally Regulate Mitophagy and Mitochondrial Spheroid Formation

Ding

Guo

et al. 2012

Journal of Biological Chemistry

121

137

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Background:The mechanistic relationship of Parkin and mitofusins in mitochondria quality control is not known. Results: CCCP-induced mitophagy and mitochondrial spheroid formation differentially require Parkin and mitofusins. Conclusion: Parkin and mitofusins reciprocally regulate mitophagy and mitochondrial spheroid formation. Significance: This study revealed a default response of mitochondria to oxidative stress and a molecular mechanism by which Parkin primes the mitochondria for mitophagy.

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“…Finally, accumulated ROS (and reactive nitrogen species, RNS) are able, in turn, to modify either directly or indirectly several mitochondriashaping proteins, thus creating a positive feedback loop [110,111].…”

Section: Mitochondrial Dynamics and Ros Production In Cancermentioning

confidence: 99%

The mitochondrial dynamics in cancer and immune-surveillance

Simula

Nazio

Campello

2017

Seminars in Cancer Biology

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A B S T R A C TMitochondria-shaping proteins control the dynamic equilibrium between fusion and fission of the mitochondrial network. Their balance is strictly required to regulate various processes, including the quality of mitochondria, cell metabolism, cell death, proliferation and cell migration. Alterations in these processes are frequently encountered in cancer, during both its onset and later progression, as evidence emerge connecting alterations in mitochondrial dynamics with cancer development. In recent years, novel therapeutic approaches to fight against different human tumors aim at exploiting the immune system's ability to specifically recognize tumor antigens, thus killing malignant cells in a process named immune-surveillance. Interestingly, data are accumulating on the role that mitochondrial dynamics play also for the correct function of both the innate and the adaptive immune system. By this review, we overview how mitochondrial dynamics can affect various processes during cancer development, acting directly on tumor cells or indirectly on cells responsible for tumor aggression and defence.

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Effect of oxidative stress on dynamics of mitochondrial reticulum

Cited by 122 publications

References 19 publications

Caspase cleavage of cytochrome c1 disrupts mitochondrial function and enhances cytochrome c release

Caspase cleavage of cytochrome c1 disrupts mitochondrial function and enhances cytochrome c release

Parkin and Mitofusins Reciprocally Regulate Mitophagy and Mitochondrial Spheroid Formation

The mitochondrial dynamics in cancer and immune-surveillance

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