High impact information on Slc26a2

• None of the compounds of this group interact with contraluminal succinate transport, and only the multiring-substituted compounds 2,4 D, 2,4,5 T, ethacrynic and tienilic acid interact slightly with the sulfate transporter [1].
• Among the seven diphosphonates tested, only etidronate and clodronate have a moderate affinity to the sulfate transporter, whereas the aminodiphosphonates have no (or low) affinity to any of the contraluminal anion transporters [2].
• Sulfate transporter: 2-Naphthylmethylphosphonate and 2-naphthylmethyldifluorophosphonate have a good affinity (app.Ki </= 0.5 mmol/l), whereas Cl-F-methylphosphonate, 2OH-5NO2-benzyl-phosphonate, 2-naphthylhydroxymethylphosphonate, phosphonoacetate etidonate and clodronate have only a moderate affinity (app.Ki approximately 3 mmol/l) [2].
• Heavy metals mercury, cadmium, and chromium inhibit the activity of the mammalian liver and kidney sulfate transporter sat-1 [3].
• We have studied the effects of several heavy metals, including mercury, lead, cadmium, and chromium (at concentrations of 1 to 1000 microM), on the activity of the mammalian sulfate transporter sat-1(2) in Xenopus oocytes. sat-1 encodes a sulfate/bicarbonate anion exchanger expressed in the rat liver and kidney [3].

Anatomical context of Slc26a2

• An interaction between selenate and a sulfate transporter in the lactating rat mammary gland [4].
• Sodium-dependent sulfate transporter (NaSi-1) mRNA and protein levels were significantly lower in the kidney cortex from hypothyroid rats [5].

References