Membrane permeability transition as induced by dysfunction of the electron transport chain.
The results in this paper indicate that mitochondrial permeability transition is activated by dysfunction of the respiratory chain caused by anaerobiosis, exhaustion of the oxidative substrate, and antimycin A, in the presence of 100 microM Ca2+. Membrane damage coincides with the collapse of the electric gradient. The opening of the non-selective pore is prevented by cyclosporin A.
Chávez
E
E
Departamento de Bioquímica Instituto Nacional de Cardiología, Ignacio Chávez, México, D.F., México.
Meléndez
E
E
Zazueta
C
C
Reyes-Vivas
H
H
Perales
S G
SG
D000255:Adenosine Triphosphate / Q000378:metabolism / Q000494:pharmacology; D000693:Anaerobiosis; D000818:Animals; D000968:Antimycin A / Q000494:pharmacology; D002118:Calcium / Q000378:metabolism / Q000493:pharmacokinetics; D004579:Electron Transport; D007425:Intracellular Membranes / Q000378:metabolism*; D008564:Membrane Potentials / Q000502:physiology; D008928:Mitochondria / Q000378:metabolism* / Q000502:physiology / Q000648:ultrastructure*; D010100:Oxygen / Q000378:metabolism; D010101:Oxygen Consumption / Q000502:physiology; D010539:Permeability; D051381:Rats; D014614:Vaccines, Synthetic / Q000276:immunology
D014614:Vaccines, Synthetic; D000968:Antimycin A; D000255:Adenosine Triphosphate; D010100:Oxygen; D002118:Calcium