UCPs, at the interface between bioenergetics and metabolism
UCPs, at the interface between bioenergetics and metabolism
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DOI：
10.1016/j.bbamcr.2016.04.013
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发表时间：
2016-10-01
影响因子：
5.1
通讯作者：
Ricquier, Daniel
中科院分区：
文献类型：
--
作者：
Bouillaud, Frederic;Alves-Guerra, Marie-Clotilde;Ricquier, Daniel
解偶联蛋白（UCP）家族的第一个成员，棕色脂肪组织解偶联蛋白1（UCP 1），于1976年被发现。20年后，两种密切相关的蛋白质UCP 2和UCP 3在哺乳动物中被描述。这些蛋白质的同源物存在于其他生物体中，包括植物。解偶联是指底物氧化和ADP磷酸化之间的能量守恒恶化。完全的能量守恒损失将是致命的，但微调可能有利于产热、氧化还原控制和防止线粒体ROS释放等过程。线粒体的偶联/解偶联状态与内膜的渗透性有关，并且由活化的UCP介导的质子转运是这些蛋白的解偶联活性的基础。UCP 1的质子运输被脂肪酸激活，这确保了产热。在体内，在没有这种激活的情况下，UCP 1仍然被抑制，没有转运活性。现在UCP 2和UCP 3似乎不太可能出现类似的情况，虽然已经描述了它们的质子转运的激活，但其生理相关性仍然不确定，可以设想它们的影响是在没有激活的情况下发生的另一种转运途径的结果。这篇文章是由Pierre Sonveaux，Pierre Maechler和Jean-Claude Martinou编辑的线粒体通道特刊的一部分。(C)© 2016 Elsevier B. V.版权所有。
The first member of the uncoupling protein (UCP) family, brown adipose tissue uncoupling protein 1 (UCP1), was identified in 1976. Twenty years later, two closely related proteins, UCP2 and UCP3, were described in mammals. Homologs of these proteins exist in other organisms, including plants. Uncoupling refers to a deterioration of energy conservation between substrate oxidation and ADP phosphorylation. Complete energy conservation loss would be fatal but fine-tuning can be beneficial for processes such as thermogenesis, redox control, and prevention of mitochondrial ROS release. The coupled/uncoupled state of mitochondria is related to the permeability of the inner membrane and the proton transport mediated by activated UCPs underlies the uncoupling activity of these proteins. Proton transport by UCP1 is activated by fatty acids and this ensures thermogenesis. In vivo in absence of this activation UCP1 remains inhibited with no transport activity. A similar situation now seems unlikely for UCP2 and UCP3 and while activation of their proton transport has been described its physiological relevance remains uncertain and their influence can be envisaged as a result of another transport pathway that takes place in the absence of activation. This article is part of a Special Issue entitled: Mitochondrial Channels edited by Pierre Sonveaux, Pierre Maechler and Jean-Claude Martinou. (C) 2016 Elsevier B.V. All rights reserved.