Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore

119Citations
Citations of this article
41Readers
Mendeley users who have this article in their library.

Abstract

Highly purified adenylate translocase (ANT) from rat heart mitochondria was functionally reconstituted as ATP/ADP exchange carrier in asotectin/cardiolipin vesicles. The ANT preparations used were free of porin, cyclophilin D, and Bax as analysed immunologically and by activity measurements. After pre-loading the ANT-containing proteoliposomes with ATP, malate or AMP, a gradual release of the trapped compounds by increasing the external Ca2+ concentrations could be demonstrated. N-Methyl-Val-4- cyclosporin did not inhibit the Ca2+ dependent release of internal substances from ANT liposomes. This inhibitor was found to be specific for the mitochondrial permeability transition pore (MTP) in intact mitochondria or reconstituted MTP-like protein complexes (e.g. hexokinase, porin, ANT complex). However, ADP in concentrations > 20 gM inhibited the liberation of internal compounds, while in contrast, atractyloside (30 μM) and HgCl2 (5 μM) both induced permeability of the ANT-containing liposomes resulting in a release of trapped substances. These results strongly suggest that ANT itself is capable to adopt a pore-like structure under conditions known to induce the permeability transition in mitochondria.

Cite

CITATION STYLE

APA

Rück, A., Dolder, M., Wallimann, T., & Brdiczka, D. (1998). Reconstituted adenine nucleotide translocase forms a channel for small molecules comparable to the mitochondrial permeability transition pore. FEBS Letters, 426(1), 97–101. https://doi.org/10.1016/S0014-5793(98)00317-2

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free