Diverse transport modes by the solute carrier 26 family of anion transporters - PubMed (original) (raw)

Review

Diverse transport modes by the solute carrier 26 family of anion transporters

Ehud Ohana et al. J Physiol. 2009.

Abstract

The solute carrier 26 (SLC26) transporters are anion transporters with diverse substrate specificity. Several members are ubiquitous while others show limited tissue distribution. They are expressed in many epithelia and to the extent known, play a central role in anion secretion and absorption. Members of the family are primarily Cl- transporters, although some members transport mainly SO(4)2-, Cl-, HCO(3)- or I-. A defining feature of the family is their functional diversity. Slc26a1 and Slc26a2 function as specific SO(4)2- transporters while Slc26a4 functions as an electroneutral Cl-/I-/HCO(3)- exchanger. Slc26a3 and Slc26a6 function as coupled electrogenic Cl-/HCO(3)- exchangers or as bona fide anion channels. SLC26A7 and SLC26A9 function exclusively as Cl- channels. This short review discusses the functional diversity of the SLC26 transporters.

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Figures

Figure 1

Figure 1. Cl−/HCO3− exchange and channel function of slc26a3, SLC26A4 and slc26a6

The transporters were expressed in Xenopus oocytes and Cl−/HCO3− exchange or anion current were measured as described in the respective publications. The results in A and B were modified from Shcheynikov et al. (2006_b_) and show Cl−/HCO3− exchange (A) and NO3− and SCN− current (B) in the absence of pHi changes (C) by Slc26a3. The results in D–F were modified mostly from Shcheynikov et al. (2008) and show Cl−/HCO3− exchange (D), I−/Cl− exchange at two membrane potentials (E) and I−/HCO3− exchange (F) by SLC26A4. The results in panels G–I were modified from Shcheynikov et al. (2006_b_) and show Cl−/HCO3− exchange (G), NO3− and SCN− current (H) in the absence of pHi changes (I) by Slc26a6.

Figure 2

Figure 2. Cl− channel activity and lack of Cl−/HCO3− exchange by SLC26A7 and SLC26A9

The results in A and B were modified from Kim et al. (2005) and show Cl− channel activity in Hepes- and in HCO3−-buffered media (A) and the minimal Cl−/HCO3− exchange activity (B) by SLC26A7. The results in C and D were modified from Dorwart et al. (2007) and show Cl− channel activity in Hepes- and in HCO3−-buffered media (C) and the minimal Cl−/HCO3− exchange activity (D) by SLC26A9.

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