Bernardi Paolo, Forte Michael
Department of Biomedical Sciences and CNR Institute of Neurosciences, University of Padova, Viale Giuseppe Colombo 3, I-35121 Padova, Italy.
Novartis Found Symp. 2007;287:157-64; discussion 164-9.
The mitochondrial permeability transition pore (PTP) is a high conductance channel of the inner membrane whose opening leads to an increase of permeability to solutes with molecular masses up to about 1500Da, the 'permeability transition'. This potentially catastrophic event has long been known, yet the molecular bases for its occurrence remain unsolved despite its established importance in several in vivo models of pathology. Recent studies based on inactivation of genes encoding putative pore components (such as the adenine nucleotide translocators and the voltage-dependent anion channel) have raised major questions about the involvement of these proteins in PTP formation, yet they have conclusively demonstrated the role of matrix cyclophilin D as the mitochondrial receptor for the desensitizing effects of cyclosporin A. While the nature of the components forming the PTP remains controversial, the identification of novel inhibitors that can be used as affinity labels is offering new perspectives towards the molecular definition of the PTP.
线粒体通透性转换孔（PTP）是内膜上的一种高电导通道，其开放会导致分子量高达约1500Da的溶质通透性增加，即“通透性转换”。这一潜在的灾难性事件早已为人所知，然而尽管其在多种体内病理模型中已被证实具有重要性，但其发生的分子基础仍未解决。最近基于对编码假定孔道成分的基因（如腺嘌呤核苷酸转位酶和电压依赖性阴离子通道）进行失活的研究，引发了关于这些蛋白质是否参与PTP形成的重大问题，但这些研究确凿地证明了基质亲环蛋白D作为环孢素A脱敏作用的线粒体受体的作用。虽然构成PTP的成分的性质仍存在争议，但能够用作亲和标记的新型抑制剂的鉴定为PTP的分子定义提供了新的视角。
