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

Abstract:

: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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Jezek P,Modrianský M,Garlid KD

doi

10.1016/s0014-5793(97)00335-9

subject

Has Abstract

pub_date

1997-05-19 00:00:00

pages

166-70

issue

2

eissn

0014-5793

issn

1873-3468

pii

S0014-5793(97)00335-9

journal_volume

408

pub_type

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