scholarly journals Role of hypoxia-induced Bax translocation and cytochrome c release in reoxygenation injury

Oncogene ◽  
1998 ◽  
Vol 17 (26) ◽  
pp. 3401-3415 ◽  
Author(s):  
Pothana Saikumar ◽  
Zheng Dong ◽  
Yogi Patel ◽  
Kristi Hall ◽  
Ulrich Hopfer ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Release ◽  
Reoxygenation Injury

scholarly journals Possible Role of Peroxynitrite in the Responses Induced by Fusicoccin in Plant Cultured Cells

Plants ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 182 ◽  
Author(s):  
Massimo Malerba ◽  
Raffaella Cerana
Keyword(s):  
Cytochrome C ◽  
Dna Fragmentation ◽  
Stress Responses ◽  
Molecular Chaperones ◽  
Caspase 3 ◽  
Cultured Cells ◽  
Acer Pseudoplatanus ◽  
Cytochrome C Release ◽  
Induced Stress

Fusicoccin (FC) is a well-known phytotoxin able to induce in Acer pseudoplatanus L. (sycamore) cultured cells, a set of responses similar to those induced by stress conditions. In this work, the possible involvement of peroxynitrite (ONOO−) in FC-induced stress responses was studied measuring both in the presence and in the absence of 2,6,8-trihydroxypurine (urate), a specific ONOO− scavenger: (1) cell death; (2) specific DNA fragmentation; (3) lipid peroxidation; (4) production of RNS and ROS; (5) activity of caspase-3-like proteases; and (6) release of cytochrome c from mitochondria, variations in the levels of molecular chaperones Hsp90 in the mitochondria and Hsp70 BiP in the endoplasmic reticulum (ER), and of regulatory 14-3-3 proteins in the cytosol. The obtained results indicate a role for ONOO− in the FC-induced responses. In particular, ONOO− seems involved in a PCD form showing apoptotic features such as specific DNA fragmentation, caspase-3-like protease activity, and cytochrome c release from mitochondria.

scholarly journals Calcium preconditioning inhibits mitochondrial permeability transition and apoptosis

2001 ◽  
Vol 280 (2) ◽  
pp. H899-H908 ◽  
Author(s):  
Meifeng Xu ◽  
Yigang Wang ◽  
Kyoji Hirai ◽  
Ahmar Ayub ◽  
Muhammad Ashraf
Keyword(s):  
Mitochondrial Permeability Transition ◽  
Adenine Nucleotide ◽  
Permeability Transition ◽  
Cytochrome C Release ◽  
Mitochondrial Permeability ◽  
Lactate Dehydrogenase Release ◽  
Viable Cells ◽  
Reoxygenation Injury ◽  
Injury Protection

We tested the hypothesis whether calcium preconditioning (CPC) reduces reoxygenation injury by inhibiting mitochondrial permeability transition (MPT). Cultured myocytes were preconditioned by a brief exposure to 1.5 mM calcium (CPC) and subjected to 3 h of anoxia followed by 2 h of reoxygenation (A-R). Myocytes were also treated with 0.2 μM/l cyclosporin A (CsA), an inhibitor of MPT, before A-R. A significant increase of viable cells and reduced lactate dehydrogenase release was observed both in CPC- and CsA-treated myocytes compared with the A-R group. Cytochrome c release was predominantly observed in the cytoplasm of myocytes in the A-R group in contrast with CPC- or CsA-treated groups, where it was restricted only to mitochondria. Similarly, the cell death by apoptosis was also markedly attenuated in these groups. Electron-dense Ca2+ deposits in mitochondria were also less frequent. Atractyloside (20 μM/l), an adenine nucleotide translocase inhibitor, caused changes similar to those in the A-R group, suggesting a role of MPT in A-R injury. Protection by inhibition of MPT by CsA and CPC suggests that MPT plays an important role in reoxygenation/reperfusion injury. The data further suggest that preconditioning inhibits MPT by inhibiting Ca2+accumulation by mitochondria.

scholarly journals The role of cytochrome c in caspase activation in Drosophila melanogaster cells

2002 ◽  
Vol 156 (6) ◽  
pp. 1089-1098 ◽  
Author(s):  
Loretta Dorstyn ◽  
Stuart Read ◽  
Dimitrios Cakouros ◽  
Jun R. Huh ◽  
Bruce A. Hay ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Mammalian Cells ◽  
Significant Proportion ◽  
Ectopic Expression ◽  
Caspase Activation ◽  
Cytochrome C Release ◽  
Cell Extracts ◽  
Effector Caspase ◽  
Drosophila Cells

The release of cytochrome c from mitochondria is necessary for the formation of the Apaf-1 apoptosome and subsequent activation of caspase-9 in mammalian cells. However, the role of cytochrome c in caspase activation in Drosophila cells is not well understood. We demonstrate here that cytochrome c remains associated with mitochondria during apoptosis of Drosophila cells and that the initiator caspase DRONC and effector caspase DRICE are activated after various death stimuli without any significant release of cytochrome c in the cytosol. Ectopic expression of the proapoptotic Bcl-2 protein, DEBCL, also fails to show any cytochrome c release from mitochondria. A significant proportion of cellular DRONC and DRICE appears to localize near mitochondria, suggesting that an apoptosome may form in the vicinity of mitochondria in the absence of cytochrome c release. In vitro, DRONC was recruited to a >700-kD complex, similar to the mammalian apoptosome in cell extracts supplemented with cytochrome c and dATP. These results suggest that caspase activation in insects follows a more primitive mechanism that may be the precursor to the caspase activation pathways in mammals.

Role of cardiolipin in cytochrome c release from mitochondria

2007 ◽  
Vol 14 (7) ◽  
pp. 1243-1247 ◽  
Author(s):  
M Ott ◽  
B Zhivotovsky ◽  
S Orrenius
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Release

scholarly journals Melatonin Protects Tobacco Suspension Cells against Pb-Induced Mitochondrial Dysfunction

2021 ◽  
Vol 22 (24) ◽  
pp. 13368
Author(s):  
Agnieszka Kobylińska ◽  
Małgorzata Maria Posmyk
Keyword(s):  
Cytochrome C ◽  
Mitochondrial Dysfunction ◽  
Plant Tolerance ◽  
Suspension Cells ◽  
Cytochrome C Release ◽  
Bright Yellow ◽  
Nicotiana Tabacum L ◽  
Tobacco Suspension Cells ◽  
Defence Strategies

Recent studies have shown that melatonin is an important molecule in plant physiology. It seems that the most important is that melatonin effectively eliminates oxidative stress (direct and indirect antioxidant) and switches on different defence strategies (preventive and interventive actions) during environmental stresses. In the presented report, exogenous melatonin potential to protect Nicotiana tabacum L. line Bright Yellow 2 (BY-2) exposed to lead against death was examined. Analyses of cell proliferation and viability, the level of intracellular calcium, changes in mitochondrial membrane potential (ΔΨm) as well as possible translocation of cytochrome c from mitochondria to cytosol and subsequent caspase-like proteolytic activity were conducted. Our results indicate that pretreatment BY-2 with melatonin protected tobacco cells against mitochondrial dysfunction and caspase-like activation caused by lead. The findings suggest the possible role of this indoleamine in the molecular mechanism of mitochondria, safeguarding against potential collapse and cytochrome c release. Thus, it seems that applied melatonin acted as an effective factor, promoting survival and increasing plant tolerance to lead.

scholarly journals Mitochondria-Associated Membranes (MAMs) are involved in Bax mitochondrial localization and cytochrome c release

2018 ◽  
Author(s):  
Alexandre Légiot ◽  
Claire Céré ◽  
Thibaud Dupoiron ◽  
Mohamed Kaabouni ◽  
Stéphen Manon
Keyword(s):  
Endoplasmic Reticulum ◽  
Cytochrome C ◽  
Mitochondrial Membrane ◽  
Human Protein ◽  
Outer Mitochondrial Membrane ◽  
Yeast Mutant ◽  
Mitochondrial Localization ◽  
Cytochrome C Release ◽  
Apoptotic Protein

AbstractThe distribution of the pro-apoptotic protein Bax in the outer mitochondrial membrane (OMM) is a central point of regulation of apoptosis. It is now widely recognized that parts of the endoplasmic reticulum (ER) are closely associated to the OMM, and are actively involved in different signalling processes. We adressed a possible role of these domains, called Mitochondria-Associated Membranes (MAMs) in Bax localization and fonction, by expressing the human protein in a yeast mutant deleted of MDM34, a ERMES component (ER-Mitochondria Encounter Structure). By affecting MAMs stability, the deletion of MDM34 altered Bax mitochondrial localization, and decreased its capacity to release cytochrome c. Furthermore, the deletion of MDM34 decreased the size of an uncompletely released, MAMs-associated pool of cytochrome c.

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