Mammalian mitochondrial uncoupling proteins

被引:81
作者
Jezek, P
Garlid, KD
机构
[1] Acad Sci Czech Republ, Dept Membrane Transport Biophys, Inst Physiol, CZ-14220 Prague, Czech Republic
[2] Oregon Grad Inst, Dept Chem Biochem & Mol Biol, Portland, OR 97291 USA
关键词
D O I
10.1016/S1357-2725(98)00076-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The mammalian uncoupling protein (UCP-1) from the gene family of mitochondrial carriers is a dimer of identical 33 kDa subunits, each containing six membrane-spanning alpha-helices. Its expression, restricted to brown fat, occurs upon birth, cold acclimation and overfeeding. UCP-1 dissipates redox energy and thereby provides heat to the animal. Two additional isoforms have recently been discovered, 59% homologous UCP-2, widely expressed (heart, kidney, lung, placenta, lymphocytes, white fat); and UCP-3 (57% homologous), found in brown fat and skeletal muscle. Their physiological roles are unknown, but may include the regulation of body weight and energy balance, muscle nonshivering thermogenesis, fever, and defense against generation of reactive oxygen species. Consequently, great pharmacological potential is expected in revealing their biochemical and hormonal regulators. UCP-1 mediates a purine-nucleotide-sensitive uniport of monovalent unipolar anions, including fatty acids, that lead to fatty acid cycling and uncoupling. UCP-2 and UCP-3 are expected to share a similar mechanism. (C) 1998 Elsevier Science Ltd. All rights reserved.
引用
收藏
页码:1163 / 1168
页数:6
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