Jarmuszkiewicz W, Milani G, Fortes F, Schreiber A Z, Sluse F E, Vercesi A E
Department of Bioenergetics, Adam Mickiewicz University, Fredry 10, 61-701, Poznan, Poland.
FEBS Lett. 2000 Feb 11;467(2-3):145-9. doi: 10.1016/s0014-5793(00)01138-8.
An uncoupling protein (UCP) was identified in mitochondria from Candida parapsilosis (CpUCP), a non-fermentative parasitic yeast. CpUCP was immunodetected using polyclonal antibodies raised against plant UCP. Activity of CpUCP, investigated in mitochondria depleted of free fatty acids, was stimulated by linoleic acid (LA) and inhibited by GTP. Activity of CpUCP enhanced state 4 respiration by decreasing DeltaPsi and lowered the ADP/O ratio. Thus, it was able to divert energy from oxidative phosphorylation. The voltage dependence of electron flux indicated that LA had a pure protonophoretic effect. The discovery of CpUCP proves that UCP-like proteins occur in the four eukaryotic kingdoms: animals, plants, fungi and protists.
在近平滑念珠菌(一种非发酵寄生酵母)的线粒体中鉴定出一种解偶联蛋白(CpUCP)。使用针对植物UCP产生的多克隆抗体对CpUCP进行免疫检测。在去除游离脂肪酸的线粒体中研究发现,CpUCP的活性受到亚油酸(LA)的刺激并被GTP抑制。CpUCP的活性通过降低ΔΨ增强了状态4呼吸,并降低了ADP/O比值。因此,它能够使氧化磷酸化过程中的能量发生转移。电子通量的电压依赖性表明LA具有单纯的质子载体效应。CpUCP的发现证明了类似UCP的蛋白质存在于动物、植物、真菌和原生生物这四个真核生物界中。