Brustovetsky Nickolay
Department of Pharmacology and Toxicology, Stark Neurosciences Research Institute, Indiana University School of Medicine, Indianapolis, IN 46202, USA.
Cells. 2020 Dec 15;9(12):2686. doi: 10.3390/cells9122686.
The mitochondrial permeability transition, a Ca-induced significant increase in permeability of the inner mitochondrial membrane, plays an important role in various pathologies. The mitochondrial permeability transition is caused by induction of the permeability transition pore (PTP). Despite significant effort, the molecular composition of the PTP is not completely clear and remains an area of hot debate. The Ca-modified adenine nucleotide translocase (ANT) and FF ATP synthase are the major contenders for the role of pore in the PTP. This paper briefly overviews experimental results focusing on the role of ANT in the mitochondrial permeability transition and proposes that multiple molecular entities might be responsible for the conductance pathway of the PTP. Consequently, the term PTP cannot be applied to a single specific protein such as ANT or a protein complex such as FF ATP synthase, but rather should comprise a variety of potential contributors to increased permeability of the inner mitochondrial membrane.
线粒体通透性转换是一种由钙离子诱导的线粒体内膜通透性显著增加的现象，在各种病理过程中发挥着重要作用。线粒体通透性转换是由通透性转换孔（PTP）的诱导引起的。尽管人们付出了巨大努力，但PTP的分子组成仍不完全清楚，仍是一个激烈争论的领域。钙修饰的腺嘌呤核苷酸转位酶（ANT）和F₁F₀ ATP合酶是PTP中孔道作用的主要竞争者。本文简要概述了聚焦于ANT在线粒体通透性转换中作用的实验结果，并提出多个分子实体可能是PTP传导途径的原因。因此，术语PTP不能应用于单个特定蛋白质，如ANT或蛋白质复合物，如F₁F₀ ATP合酶，而应包括导致线粒体内膜通透性增加的各种潜在因素。
