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The involvement of cyclosporin A binding proteins in regulating and uncoupling mitochondrial energy transduction.

Crompton, M; McGuinness, O; Nazareth, W; (1992) The involvement of cyclosporin A binding proteins in regulating and uncoupling mitochondrial energy transduction. Biochim Biophys Acta , 1101 (2) pp. 214-217.

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Abstract

The uncoupling of mitochondrial energy transduction by excess Ca2+ may be a factor in the pathogenesis of tissue injury brought about by energy deprivation, for example, in ischaemia. In isolated mitochondria the lesion appears as a large, 20 A, pore in the inner membrane. The pore is blocked potently by the immunosuppressant cyclosporin A. Cyclosporin A also markedly retards collapse of the mitochondrial inner membrane potential in energy-deprived (respiration-inhibited) cardiomyocytes as judged by changes in rhodamine 123 fluorescence, and prolongs cell viability. A potential mitochondrial target for cyclosporin A is the matrix protein cyclophilin. Purified cyclophilin activates the respiratory chain of submitochondrial particles. This might reflect not only a physiological function of this protein, but also a component involved in the generation of the 20 A pore under pathological conditions.

Type: Article
Title: The involvement of cyclosporin A binding proteins in regulating and uncoupling mitochondrial energy transduction.
Location: Netherlands
Keywords: Animals, Calcium, Cyclosporine, Energy Metabolism, Mitochondria, Protein Binding, Rats, Receptors, Immunologic
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Life Sciences > Div of Biosciences
URI: http://discovery.ucl.ac.uk/id/eprint/1344283
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