A structure–activity study of fatty acid interaction with mitochondrial uncoupling protein

FEBS Letters

Garlid, Keith D²  Modrianský, Martin²  Ježek, Petr¹ 

[1] Institute of Physiology, Department of Membrane Transport Biophysics, Academy of Sciences of the Czech Republic, Vı́deňská 1083, CZ 14220 Prague, Czech Republic;Oregon Graduate Institute, Department of Chemistry, Biochemistry and Molecular Biology, 20000 NW Walker Road, Portland, OR 97291-1000, USA

关键词: Reconstitution;    Uncoupling protein;    H+ transport;    Fatty acid uniport;    Chloride uniport;    Fatty acid flip-flop;    BAT;    brown adipose tissue;    FA;    free fatty acids (non-esterified);    Octyl-POE;    octylpentaoxyethylene;    PBFI;    potassium-binding benzofuran phthalate;    SPQ;    6-methoxy-N-(3-sulfopropyl)quinolinium;    TEA;    tetraethylammonium-;    TES;    N-tris [hydroxymethyl]methyl-2-aminoethane-sulfonic acid;    TNP;    trinitrophenyl-;    UcP;    uncoupling protein;   

DOI  :  10.1016/S0014-5793(97)00335-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Fatty acid (FA) uniport via mitochondrial uncoupling protein (UcP) was detected fluorometrically with PBFI, potassium-binding benzofuran phthalate and SPQ, 6-methoxy-N-(3-sulfopropyl)-quinolinium, indicating K⁺ and H⁺, respectively. The FA structural patterns required for FA flip-flop, UcP-mediated FA uniport, activation of UcP-mediated H⁺ transport in proteoliposomes, and inhibition of UcP-mediated Cl⁻ uniport by FA, were identical. Positive responses were found exclusively with FA which were able to flip-flop in a protonated form across the membrane and no responses were found with ‘inactive’ FA lacking the flip-flop ability. The findings support the existence of FA cycling mechanism.

【 授权许可】

Unknown