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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
9
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pubmed:dateCreated |
1996-3-1
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pubmed:abstractText |
Earlier it has been demonstrated that the recoupling action of cyclosporin A on mitochondria deenergized by the opening of the Ca(+)-dependent pore requires higher cyclosporin A concentrations than those, which are necessary for preventing the permeabilization as well as the presence of additional effectors, such as adenine nucleotides and Mg2+. It has been shown that cyclosporin A reseals the pore and prevents its opening when used at the same low concentrations (0.1-0.4 microM), while its higher concentrations (0.5-1.0 microM) produce the recoupling of mitochondria. In contrast with recoupling, resealing of the pore by cyclosporin A does not require Mg2+ or adenine nucleotides. Carboxyatractylate which reverses the cyclosporin A-induced restoration of the membrane potential does not induce repeated opening of the pore. The carboxyatractylate-induced depolarization of the inner mitochondrial membrane is sensitive to ruthenium red. Besides, ruthenium red restores the recoupling action of cyclosporin A in the absence of carboxyatractylate. The data obtained suggest that the loss by cyclosporin A of its recoupling potency may result from the induction of the Ca2+/2H+ antiporter. Induction of the Ca2+/2H+ antiporter in combination with a ruthenium red-sensitive Ca2+ uniporter provides the uncoupling mitochondria even with a closed Ca(2+)-dependent pore. Apparently, Ca2+/2H+ antiporter induction is a result of inhibition of the ADP/ATP antiporter by a natural or exogenous inhibitor. This process seems to require a preliminary release of certain protective factors from the mitochondrial matrix.
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pubmed:language |
rus
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Antiporters,
http://linkedlifedata.com/resource/pubmed/chemical/Atractyloside,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cation Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Cyclosporine,
http://linkedlifedata.com/resource/pubmed/chemical/Magnesium,
http://linkedlifedata.com/resource/pubmed/chemical/Ruthenium Red,
http://linkedlifedata.com/resource/pubmed/chemical/calcium-hydrogen antiporters,
http://linkedlifedata.com/resource/pubmed/chemical/carboxyatractyloside
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0320-9725
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
60
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1502-11
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pubmed:dateRevised |
2007-7-23
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pubmed:meshHeading |
pubmed-meshheading:8562656-Adenine Nucleotides,
pubmed-meshheading:8562656-Animals,
pubmed-meshheading:8562656-Antiporters,
pubmed-meshheading:8562656-Atractyloside,
pubmed-meshheading:8562656-Calcium,
pubmed-meshheading:8562656-Calcium-Binding Proteins,
pubmed-meshheading:8562656-Cation Transport Proteins,
pubmed-meshheading:8562656-Cyclosporine,
pubmed-meshheading:8562656-Intracellular Membranes,
pubmed-meshheading:8562656-Magnesium,
pubmed-meshheading:8562656-Membrane Potentials,
pubmed-meshheading:8562656-Mitochondria, Liver,
pubmed-meshheading:8562656-Rats,
pubmed-meshheading:8562656-Ruthenium Red
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pubmed:year |
1995
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pubmed:articleTitle |
[Low concentrations of cyclosporin A close Ca2+-dependent inner mitochondrial membrane pores in the absence of other effectors].
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pubmed:publicationType |
Journal Article,
English Abstract
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