About: Alkylsulfonates as probes of uncoupling protein transport mechanism: ion pair transport demonstrates that H+ translocation by UCP1 is not necessary for uncoupling     Goto   Sponge   NotDistinct   Permalink

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  • The mechanism of fatty acid-dependent uncoupling by mitochondrial uncoupling proteins (UCP) is still in debate. We have hypothesized that the anionic fatty acid head group is translocated by UCP, and the proton is transported electroneutrally in the bilayer by flip-flop of the protonated fatty acid. Alkylsulfonates are useful as probes of the UCP transport mechanism. They are analogues of fatty acids, and they are transported by UCP1, UCP2, and UCP3. We show that undecanesulfonate and laurate are mutually competitive inhibitors, supporting the hypothesis that fatty acid anion is transported by UCP1. Alkylsulfonates cannot be protonated because of their low pK(a), consequently, they cannot catalyze electroneutral proton transport in the bilayer and cannot support uncoupling by UCP. We report for the first time that propranolol forms permeant ion pairs with the alkylsulfonates, thereby removing this restriction.
  • The mechanism of fatty acid-dependent uncoupling by mitochondrial uncoupling proteins (UCP) is still in debate. We have hypothesized that the anionic fatty acid head group is translocated by UCP, and the proton is transported electroneutrally in the bilayer by flip-flop of the protonated fatty acid. Alkylsulfonates are useful as probes of the UCP transport mechanism. They are analogues of fatty acids, and they are transported by UCP1, UCP2, and UCP3. We show that undecanesulfonate and laurate are mutually competitive inhibitors, supporting the hypothesis that fatty acid anion is transported by UCP1. Alkylsulfonates cannot be protonated because of their low pK(a), consequently, they cannot catalyze electroneutral proton transport in the bilayer and cannot support uncoupling by UCP. We report for the first time that propranolol forms permeant ion pairs with the alkylsulfonates, thereby removing this restriction. (en)
Title
  • Alkylsulfonates as probes of uncoupling protein transport mechanism: ion pair transport demonstrates that H+ translocation by UCP1 is not necessary for uncoupling
  • Alkylsulfonates as probes of uncoupling protein transport mechanism: ion pair transport demonstrates that H+ translocation by UCP1 is not necessary for uncoupling (en)
skos:prefLabel
  • Alkylsulfonates as probes of uncoupling protein transport mechanism: ion pair transport demonstrates that H+ translocation by UCP1 is not necessary for uncoupling
  • Alkylsulfonates as probes of uncoupling protein transport mechanism: ion pair transport demonstrates that H+ translocation by UCP1 is not necessary for uncoupling (en)
skos:notation
  • RIV/00216224:14330/01:00030508!RIV10-MSM-14330___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • V
http://linked.open...iv/cisloPeriodika
  • 34
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 672867
http://linked.open...ai/riv/idVysledku
  • RIV/00216224:14330/01:00030508
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • UCP1; uncoupling protein; mitochondria (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [1AC23154A32B]
http://linked.open...i/riv/nazevZdroje
  • Journal of Biological Chemistry
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 276
http://linked.open...iv/tvurceVysledku
  • Vařecha, Miroslav
  • Ježek, P.
  • Garlid, K. D.
  • Jabůrek, M.
http://linked.open...ain/vavai/riv/wos
  • 000170613500060
issn
  • 0021-9258
number of pages
http://localhost/t...ganizacniJednotka
  • 14330
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