Sulfate transport mediated by the mammalian anion exchangers in reconstituted proteoliposomes Academic Article uri icon

abstract

  • The kinetic properties of sulfate transport mediated by the anion exchangers AE1 and AE2 have been examined. Microsomes isolated from HEK cells transiently overexpressing either protein were reconstituted in unilamellar, 200-600-nm diameter proteoliposomes. Transport mediated by the exchangers was monitored by loading the reconstituted proteoliposomes with the slowly transportable anion SO4 (2-) using [35S] SO4 (2-) as a tracer and performing [35S] SO4 (2-)/SO4 (2-) exchange. The following data suggest that AE1 and AE2 have been functionally reconstituted:(i) the rate of SO4 (2-) transport in AE1 and AE2 containing proteoliposomes was 10-20 times higher than in proteoliposomes derived from control microsomes;(ii) the transport of SO4 (2-) was strongly dependent on the presence of a trans anion; and (iii) the anion exchanger inhibitors, 4, 4′-diisothiocyanostilbene-2, 2 …

publication date

  • May 1, 1995