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

Authors
  • Jezek, P
  • Modrianský, M
  • Garlid, K D
Type
Published Article
Journal
FEBS Letters
Publisher
Wiley (John Wiley & Sons)
Publication Date
May 19, 1997
Volume
408
Issue
2
Pages
166–170
Identifiers
PMID: 9187360
Source
Medline
License
Unknown

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.

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