Effect of cyclosporin A on energy coupling in pea stem mitochondria

Vianello, Angelo; Macrı̀, Francesco; Braidot, Enrico; Mokhova, E. N.

doi:10.1016/0014-5793(95)00897-i

Cited by 26 publications

(2 citation statements)

References 16 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In plants, a collapse of transmembrane electrical potential (ΔΨ), induced by Ca 2+ and delayed by CsA, has been described in isolated pea stem mitochondria (Vianello et al, 1995). Subsequently, PT was observed in several plants, although it showed different features, depending on tissues and species.…”

Section: Introductionmentioning

confidence: 99%

Properties of the Permeability Transition of Pea Stem Mitochondria

et al. 2018

View full text Add to dashboard Cite

In striking analogy with Saccharomyces cerevisiae, etiolated pea stem mitochondria did not show appreciable Ca2+ uptake. Only treatment with the ionophore ETH129 (which allows electrophoretic Ca2+ equilibration) caused Ca2+ uptake followed by increased inner membrane permeability, membrane depolarization and Ca2+ release. Like the permeability transition (PT) of mammals, yeast and Drosophila, the PT of pea stem mitochondria was stimulated by diamide and phenylarsine oxide and inhibited by Mg-ADP and Mg-ATP, suggesting a common underlying mechanism; yet, the plant PT also displayed distinctive features: (i) as in mammals it was desensitized by cyclosporin A, which does not affect the PT of yeast and Drosophila; (ii) similarly to S. cerevisiae and Drosophila it was inhibited by Pi, which stimulates the PT of mammals; (iii) like in mammals and Drosophila it was sensitized by benzodiazepine 423, which is ineffective in S. cerevisiae; (iv) like what observed in Drosophila it did not mediate swelling and cytochrome c release, which is instead seen in mammals and S. cerevisiae. We find that cyclophilin D, the mitochondrial receptor for cyclosporin A, is present in pea stem mitochondria. These results indicate that the plant PT has unique features and suggest that, as in Drosophila, it may provide pea stem mitochondria with a Ca2+ release channel.

show abstract

Section: Introductionmentioning

confidence: 99%

Properties of the Permeability Transition of Pea Stem Mitochondria

et al. 2018

View full text Add to dashboard Cite

show abstract

“…The first evidence of a Ca 2+ -induced and CsA-delayed collapse of transmembrane electrical potential difference (ΔΨ) in pea stem mitochondria dates back to 1995 ( Vianello et al, 1995 ). PT has been then observed in different plant species, although the features of this phenomenon cannot be summarized in a straightforward model ( Table 1 ).…”

Section: The Pt In Plantsmentioning

confidence: 99%

The Permeability Transition in Plant Mitochondria: The Missing Link

et al. 2015

View full text Add to dashboard Cite

The synthesis of ATP in mitochondria is dependent on a low permeability of the inner membrane. Nevertheless, mitochondria can undergo an increased permeability to solutes, named permeability transition (PT) that is mediated by a permeability transition pore (PTP). PTP opening requires matrix Ca2+ and leads to mitochondrial swelling and release of intramembrane space proteins (e.g., cytochrome c). This feature has been initially observed in mammalian mitochondria and tentatively attributed to some components present either in the outer or inner membrane. Recent works on mammalian mitochondria point to mitochondrial ATP synthase dimers as physical basis for PT, a finding that has been substantiated in yeast and Drosophila mitochondria. In plant mitochondria, swelling and release of proteins have been linked to programmed cell death, but in isolated mitochondria PT has been observed in only a few cases and in plant cell cultures only indirect evidence is available. The possibility that mitochondrial ATP synthase dimers could function as PTP also in plants is discussed here on the basis of the current evidence. Finally, a hypothetical explanation for the origin of PTP is provided in the framework of molecular exaptation.

show abstract

Plant mitochondrial carriers: an overview

Laloi

1999

Cellular and Molecular Life Sciences (CMLS)

107

View full text Add to dashboard Cite

In the two last decades, biochemical studies using mitochondrial swelling experiments or direct solute uptake in isolated mitochondria have lead to the identification of different transport systems at the level of the plant mitochondrial inner membrane. Although most of them have been found to have similar features to those identified in animal mitochondria, some differences have been observed between plant and animal transporters. More recently, molecular biology studies have revealed that most of the mitochondrial exchanges are performed by nuclear encoded proteins, which form a superfamily. Members of this family have been reported in animals, yeast as well as plants. This review attempts to give an overview of the present knowledge concerning the biochemical and molecular characterisation of plant members of the mitochondrial carrier family and, when possible, a comparison with carriers from other organisms.

show abstract

Effect of cyclosporin A on energy coupling in pea stem mitochondria

Cited by 26 publications

References 16 publications

Properties of the Permeability Transition of Pea Stem Mitochondria

Properties of the Permeability Transition of Pea Stem Mitochondria

The Permeability Transition in Plant Mitochondria: The Missing Link

Plant mitochondrial carriers: an overview

Contact Info

Product

Resources

About