1H-n.m.r. evaluation of the ferricytochrome <i>c</i>-cardiolipin interaction. Effect of superoxide radicals

Soussi, B.; Bylund-Fellenius, Ann-Christin; Scherstén, T; Ångström, Jonas

doi:10.1042/bj2650227

Cited by 50 publications

(33 citation statements)

References 34 publications

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“…It has been hypothesized that the extent of cytochrome c association with the inner mitochondrial membrane is dependent on the interaction with CL and is regulated by the redox state (33). We found that phosphate, although acting on mPTP opening, did not induce cytochrome c release up to 10 mM, confirming that cytochrome c release is independent of the mPTP (34).…”

Section: Discussionsupporting

confidence: 72%

Exogenous Phospholipids Specifically Affect Transmembrane Potential of Brain Mitochondria and Cytochrome c Release

Piccotti¹,

Marchetti

Migliorati

et al. 2002

Journal of Biological Chemistry

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Release of cytochrome c, a decrease of membrane potential (⌬ m ), and a reduction of cardiolipin (CL) of rat brain mitochondria occurred upon incubation in the absence of respiratory substrates. Since CL is critical for mitochondrial functioning, CL enrichment of mitochondria was achieved by fusion with CL liposomes. Fusion was triggered by potassium phosphate at concentrations producing mitochondrial permeability transition pore opening but not cytochrome c release, which was observed only at >10 mM. Cyclosporin A inhibited phosphate-induced CL fusion, whereas Pronase pretreatment of mitochondria abolished it, suggesting that mitochondrial permeability transition pore and protein(s) are involved in the fusion process. Phosphate-dependent fusion was enhanced in respiratory state 3 and influenced by phospholipid classes in the order CL > phosphatidylglycerol (PG) > phosphatidylserine. The probe 10-nonylacridine orange indicated that fused CL had migrated to the inner mitochondrial membrane. In state 3, CL enrichment of mitochondria resulted in a pH decrease in the intermembrane space. Cytofluorimetric analysis of mitochondria stained with 3,3-diexyloxacarbocyanine iodide and 5,5,6,6-tetrachloro-1,1,3,3-tetraethylbenzymidazolylcarbocyanine iodide showed ⌬ m increase upon fusion with CL or PG. In contrast, phosphatidylserine fusion required ⌬ m consumption, suggesting that ⌬ m is the driving force in mitochondrial phospholipid importation. Moreover, enrichment with CL and PG brought the low energy mitochondrial population to high ⌬ m values and prevented phosphate-dependent cytochrome c release.The role of mitochondria in neurodegenerative disease has been increasingly supported (1). Mitochondrial dysfunction can lead to deleterious cell injury due to free radical generation, intracellular calcium concentration imbalance, and activation of mitochondrial permeability transition pore (mPTP) 1 (2). In apoptosis, a caspase cascade often mediates cell death (3). Despite the complexity of the mechanisms involved, mitochondria appear to provide a link between the initiator caspases and the downstream effector caspases. Mitochondria release apoptosis-inducing factors that trigger DNA fragmentation of isolated nuclei (4, 5). In addition, Bax acts on mPTP, causing the release of cytochrome c into the cytosol (3, 6). Released cytochrome c binds to Apaf-1, thus initiating activation of caspase-1 and of downstream processes, leading to nuclear DNA fragmentation. Cytochrome c release is also stimulated by Bid (7, 8), whereas Bcl2 prevents it (9). The mechanism responsible for signaling molecule release from mitochondria is under extensive study. It is known that these molecules are bound to the inner mitochondrial membrane, whose integrity appears to be essential for mitochondrial functions. Cardiolipin (CL) is present only within the inner mitochondrial membrane, strictly associated to mitochondrial electron transport complexes and transporters (10). The specific requirement of heart cytochrome c oxidase for CL has been demonst...

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Section: Discussionsupporting

confidence: 72%

Exogenous Phospholipids Specifically Affect Transmembrane Potential of Brain Mitochondria and Cytochrome c Release

Piccotti¹,

Marchetti

Migliorati

et al. 2002

Journal of Biological Chemistry

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“…If the latter is the case, the dissociation of cytochrome c from mitochondrial inner membrane is also necessary to release cytochrome c from mitochondria. Association of cytochrome c to mitochondrial inner membrane is dependent on its interaction with acidic lipid cardiolipin and their association is downregulated by ROS (Soussi et al, 1990). It is possible that an antioxidant-sensitive mechanism induced by complex I inhibition can dissociate cytochrome c from mitochondrial inner membrane.…”

Section: Discussionmentioning

confidence: 99%

Inhibition of mitochondrial respiratory chain complex I by TNF results in cytochrome c release, membrane permeability transition, and apoptosis

1998

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“…Although several research groups have studied the interaction of cyt c with different anionic phospholipids in liposomes (11,(13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23), the redox properties of cyt c in the presence of CLcontaining liposomes have not been characterized. The redox behavior of cyt c under equilibrium conditions was determined by titrating it with sodium dithionite (E 0 =−564 mV) (41) under anaerobic conditions and in the presence of indicator dyes (mediators) so that it could be followed optically.…”

Section: Redox Titration Of Cyt C In the Presence Of Cl-containing Limentioning

confidence: 99%

Cardiolipin Switch in Mitochondria: Shutting off the Reduction of Cytochrome c and Turning on the Peroxidase Activity

et al. 2007

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Upon interaction with anionic phospholipids, particularly mitochondria-specific cardiolipin (CL), cytochrome c (cyt c) loses its tertiary structure and its peroxidase activity dramatically increases. CL induced peroxidase activity of cyt c has been found to be important for selective CL oxidation in cells undergoing programmed death. During apoptosis, the peroxidase activity and the fraction of CL-bound cyt c markedly increases suggesting that CL may act as a switch to regulate cyt c's mitochondrial functions. Using cyclic voltammetry and equilibrium redox-titrations, we show that the redox potential of cyt c shifts negatively by 350-400 mV upon binding to CL-containing membranes. Consequently, functions of cyt c as an electron transporter and cyt c reduction by Complex III are strongly inhibited. Further, CL/cyt c complexes are not effective in scavenging superoxide anions and are not effectively reduced by ascorbate. Thus, both redox properties and functions of cyt c change upon interaction with CL in the mitochondrial membrane, diminishing cyt c's electron donor/acceptor role and stimulating its peroxidase activity.

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1H-n.m.r. evaluation of the ferricytochrome c-cardiolipin interaction. Effect of superoxide radicals

Cited by 50 publications

References 34 publications

Exogenous Phospholipids Specifically Affect Transmembrane Potential of Brain Mitochondria and Cytochrome c Release

Exogenous Phospholipids Specifically Affect Transmembrane Potential of Brain Mitochondria and Cytochrome c Release

Inhibition of mitochondrial respiratory chain complex I by TNF results in cytochrome c release, membrane permeability transition, and apoptosis

Cardiolipin Switch in Mitochondria: Shutting off the Reduction of Cytochrome c and Turning on the Peroxidase Activity

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