Involvement of SH-groups during interaction of diazoxide with the inner membrane of rat heart mitochondria

Abstract

It is known that adenine nucleotide translocase plays an important role in the formation of calcium-dependent mitochondrial permeability transition pore in the inner mitochondrial membrane [1] and activation of basal mitochondrial respiration by diazoxide, an agonist of mitochondrial K ATP channels [2]. Recent findings suggest that mitochondrial permeability transition pore and mitochondrial K ATP channel, which are regulated by [Ca 2+ ] m and ∆Ψ , respectively, and play a key role in the initiation of apoptosis [3], have close structural interconnections. It was hypothesized that some molecules in the inner mitochondrial membrane (in particular, adenine nucleotide translocase) are involved in formation of both the calcium-dependent mitochondrial permeability transition pore and mitochondrial K ATP channel [4]. It was previously shown that diazoxide, which mimicked the effect of pharmacological preconditioning during ischemia/reperfusion of an isolated heart [5], induced the opening of calcium-dependent mitochondrial permeability transition pore in the low-conductance state in the presence of