Disease relevance of Slc26a1

• In the countries of Southern Africa, types SAT 1, SAT 2 and SAT 3 (SAT: Southern African Territories) of foot and mouth disease (FMD) virus are the most widely represented, especially the SAT 2 virus [1].

High impact information on Slc26a1

• Drugs found earlier to interact with sulfate transport in vivo have not yet been tested with sat-1 [2].
• Molecular characterization of the murine Slc26a6 anion exchanger: functional comparison with Slc26a1 [3].
• Functional comparison with murine Slc26a1, the basolateral oxalate exchanger of the proximal tubule, reveals a number of intriguing differences [3].
• In contrast, SO and oxalate transport by Slc26a1 are mutually cis-inhibited but activated significantly by extracellular halides, lactate, and formate [3].
• Also, the expression of mRNA for GlnT (SAT1), a system A isoform specific for Gln, was only expressed in neurons derived from both structures, while an alanine (Ala)-preferring system A transporter, SAT2, was expressed in neurons and astrocytes from either region [4].

Biological context of Slc26a1

• The mouse sulfate anion transporter gene Sat1 (Slc26a1): cloning, tissue distribution, gene structure, functional characterization, and transcriptional regulation thyroid hormone [5].
• The Sat1 gene (~6 kb) consists of 4 exons [5].

Anatomical context of Slc26a1

• Whereas Slc26a6 is capable of Cl(-), SO, formate, and oxalate uptake when expressed in Xenopus laevis oocytes, Slc26a1 transports only SO and oxalate [3].
• This suggests that tissue-specific nuclear matrix proteins other than topoisomerase II, including SATP-1 in the thymus, should also be considered [6].

Analytical, diagnostic and therapeutic context of Slc26a1

• Site-directed mutagenesis identified an imperfect T(3)RE at -454-bp in the Sat1 promoter to be responsible for this activity [5].

References