Phospholipid import into mitochondria: Possible regulation mediated through lipid polymorphism

Ardail, Dominique; Lermé, F.; Louisot, Pierre

doi:10.1016/s0006-291x(05)81559-1

Cited by 21 publications

(25 citation statements)

References 20 publications

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“…The present evidence for a differential distribution of GPx and PHGPx in relation to the mitochondrial inner membrane is of special interest, suggesting a strategic role of the two enzymes in eliminating, on one hand, HzO2 generated in the inner and outer rnitochondrial compartments by superoxide dismutase and by monoamme oxidase; and, on the other hand, phospholipid hydroperoxides formed in the inner membrane which is an important potential site of lipid peroxidation (27)(28)(29). The data reported here further underline the functional importance of the contact sites between the inner and outer mitochondrial membranes, including their role in the transport of proteins [30][31][32] and lipids [33,34], as well as various enzyme activities [26], ion conductance [35] and, in general, the metabolic interplay between mitochondria and the rest of the cell.…”

Section: Methodsmentioning

confidence: 65%

Distribution of glutathione peroxidases glutathione reductase in rat brain mitochondria

1991

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The distribution of glutathione reductase (GR), gtutathione peroxidase (GPx) and phosphotipid hydroperoxide giutathione peroxidase (PHGPx) in isolated rat brain mitochondria was investigated, using a fractionation procedure for the separation of inner and outer membranes, contact sites between the two membranes and a soluble Fraction mainly originating from the mitochondrial matrix. The data indicate that GW and GPx are concentrated in the soluble fraction, with a minor portion of the two enzymes being associated with the contact sites. PHGPx is localized largely in the inner membrane. The possible functional significance of these findings is discussed.

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Section: Methodsmentioning

confidence: 65%

Distribution of glutathione peroxidases glutathione reductase in rat brain mitochondria

1991

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“…The transfer is controlled by an 18 000-M r benzodiazepine receptor [201] associated with VDAC [202] (Scheme 2). More generally, there are indications that the contact sites are also involved in the transfer of phosphatidylserine between the endoplasmic reticulum and the mitochondrial inner membrane [203,204]. In order to carry out these tasks the sites recruit other proteins, e.g.…”

Section: Discussionmentioning

confidence: 99%

The mitochondrial permeability transition pore and its role in cell death

Crompton

1999

Biochemical Journal

1,811

1,267

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This article reviews the involvement of the mitochondrial permeability transition pore in necrotic and apoptotic cell death. The pore is formed from a complex of the voltage-dependent anion channel (VDAC), the adenine nucleotide translocase and cyclophilin-D (CyP-D) at contact sites between the mitochondrial outer and inner membranes. In vitro, under pseudopathological conditions of oxidative stress, relatively high Ca2+ and low ATP, the complex flickers into an open-pore state allowing free diffusion of low-Mr solutes across the inner membrane. These conditions correspond to those that unfold during tissue ischaemia and reperfusion, suggesting that pore opening may be an important factor in the pathogenesis of necrotic cell death following ischaemia/reperfusion. Evidence that the pore does open during ischaemia/reperfusion is discussed. There are also strong indications that the VDAC-adenine nucleotide translocase-CyP-D complex can recruit a number of other proteins, including Bax, and that the complex is utilized in some capacity during apoptosis. The apoptotic pathway is amplified by the release of apoptogenic proteins from the mitochondrial intermembrane space, including cytochrome c, apoptosis-inducing factor and some procaspases. Current evidence that the pore complex is involved in outer-membrane rupture and release of these proteins during programmed cell death is reviewed, along with indications that transient pore opening may provoke ‘accidental’ apoptosis.

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“…Previous work from our laboratory [9,11] and from others [28] suggested that phosphatidylserine on its way from the outer to the inner mitochondrial membrane migrates via membrane contact sites. Similarly, phosphatidylethanolamine newly synthesized in the inner mitochondrial membrane and exported to the mitochondrial surface was highly enriched in the contact site fraction [9,11].…”

Section: Discussionmentioning

confidence: 99%

Import of phosphatidylinositol and phosphatidylcholine into mitochondria of the yeast, Saccharomyces cerevisiae

et al. 1994

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AI&net An in vitro assay was designed to study the import of 'H-labeled phosphatidylinositol and phosphatidylcholine, respectively, from unilamellar vesicles into isolated mitochondria of the yeast, Saccharomyces cerevisiae. Both phospholipids reached the inner mitochonclrial membrane.During import they were detected in contact sites between the outer and the inner mitochondrial membrane, supporting the notion that these zones are sites of intramitochondrial phospholipid transport. The uncoupler CCCP, the antibiotic adriamycin, and energy depletion caused by oligomycin and apyrase did not inhibit the transport of phosphatidylinositol and phosphatidylcholine into mitochondria.

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Phospholipid import into mitochondria: Possible regulation mediated through lipid polymorphism

Cited by 21 publications

References 20 publications

Distribution of glutathione peroxidases glutathione reductase in rat brain mitochondria

Distribution of glutathione peroxidases glutathione reductase in rat brain mitochondria

The mitochondrial permeability transition pore and its role in cell death

Import of phosphatidylinositol and phosphatidylcholine into mitochondria of the yeast, Saccharomyces cerevisiae

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