Adenine nucleotide translocase as a site of regulation by ADP of the rat liver mitochondria permeability to H+ and K+ ions.
Adenine nucleotide translocase as a site of regulation by ADP of the rat liver mitochondria permeability to H+ and K+ ions.
复制标题
腺嘌呤核苷酸转位酶作为 ADP 调节大鼠肝线粒体 H 和 K 离子通透性的位点。
DOI：
10.1016/0003-9861(80)90298-2
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发表时间：
1980
影响因子：
3.9
通讯作者：
V. Lyakhovich
中科院分区：
文献类型：
--
作者：
A. Panov;Svetlana Filippova;V. Lyakhovich
In the presence of oligomycin ADP inhibits the osmotic swelling of the nonenergized rat liver mitochondria in the NH4NO3medium. With the energized mitochondria ADP enhances contraction of the mitochondria swollen in the NH4NO3medium. Carboxyatractyloside and atractyloside abolish or prevent the effects of ADP. The direct measurements of the proton conductance of rat liver mitochondria shows that the inhibitory action of ADP + oligomycin on the H+permeability does not depend on the energization of mitochondria. In these experiments the local anesthetic nupercaine and ADP additively inhibit the inner membrane conductance for protons, but carboxyatractyloside abolishes only the effect of ADP. In the presence of oligomycin ADP also inhibits the osmotic swelling of the nonenergized liver mitochondria in the KNO3medium, and the energy-dependent swelling of rat liver mitochondria in the medium with K+ions andPi. The inhibition by ADP of the membrane passive permeability for K+is also sensitive to carboxyatractyloside. It is concluded that rat liver mitochondria possess an ADP-regulated channel for H+and K+. The properties of this pathway for protons and potassium ions favor the idea that ADP regulates the mitochondrial permeability via adenine nucleotide translocase. It is assumed that the adenine nucleotides carrier should operate according to the “gated pore” mechanism.
