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 Lettjournal_title
FEBS lettersauthors
Jezek P,Modrianský M,Garlid KDdoi
10.1016/s0014-5793(97)00335-9subject
Has Abstractpub_date
1997-05-19 00:00:00pages
166-70issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(97)00335-9journal_volume
408pub_type
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