Jezek P
Institute of Physiology, Department of Membrane Transport Biophysics, Academy of Sciences of the Czech Republic, Prague.
J Bioenerg Biomembr. 1999 Oct;31(5):457-66. doi: 10.1023/a:1005496306893.
The phenomena of fatty acid interaction with mitochondrial integral membrane proteins, namely uncoupling proteins (UCPs), are reviewed to emphasize the fatty acid cycling mechanism that has been suggested to explain the UCP function. Fatty acid-induced uncoupling is suggested to serve in bioenergetic systems, to set the optimum efficiency, and to tune the degree of coupling of oxidative phosphorylation. Fatty acid interaction with the "classic" uncoupling protein (UCP1) from mitochondria of thermogenic brown adipose tissue (BAT) is well known. UCP1 is considered to mediate purine nucleotide-sensitive uniport of monovalent unipolar anions, including anionic fatty acids. The return of protonated fatty acid leads to H+ uniport and uncoupling. Experiments supporting this mechanism are also reviewed for plant uncoupling mitochondrial protein (PUMP) and ADP/ATP carrier. The fatty acid cycling mechanism is predicted, as well for the recently discovered uncoupling proteins, UCP2 and UCP3.
本文综述了脂肪酸与线粒体整合膜蛋白（即解偶联蛋白，UCPs）的相互作用现象，以强调为解释UCP功能而提出的脂肪酸循环机制。脂肪酸诱导的解偶联作用被认为在生物能量系统中发挥作用，设定最佳效率，并调节氧化磷酸化的偶联程度。脂肪酸与产热棕色脂肪组织（BAT）线粒体中的“经典”解偶联蛋白（UCP1）的相互作用是众所周知的。UCP1被认为介导包括阴离子脂肪酸在内的单价单极阴离子的嘌呤核苷酸敏感单向转运。质子化脂肪酸的返回导致H+单向转运和解偶联。也对支持该机制的植物解偶联线粒体蛋白（PUMP）和ADP/ATP载体的实验进行了综述。对于最近发现的解偶联蛋白UCP2和UCP3，也预测了脂肪酸循环机制。
