SLC10A6 Membrane Protein Introduction

Introduction of SLC10A6

Solute carrier family 10 member 6 (SLC10A6), also known as sodium-dependent organic anion transporter (SOAT in man and Soat in mice) represents a plasma membrane uptake carrier for sulfated steroid hormones. It belongs to the solute carrier family 10. SLC10A6 shows transport activity for estrone sulfate (E1S), estradiol sulfate (E2S), pregnenolone sulfate (PregS), dehydroepiandrosterone sulfate (DHEAS), 16α-hydroxydehydroepiandrosterone sulfate (16-OH-DHEAS), and androstenediol sulfate (AnDiolS). However, SLC10A6 does not accept other steroid compounds as substrates including bile acids such as taurocholic acid and chenodeoxycholic acid, cardiac glycosides such as ouabain and digoxin, or steroid glucuronides such as estrone-3-D-glucuronide and estradiol-17-D-glucuronide.

Function of SLC10A6 Membrane Protein

SOAT is a plasma membrane transporter for sulfated steroids which is highly expressed in germ cells of the testis. SLC10A6 can transport biologically inactive sulfated steroids into specific target cells, where they can be reactivated by the steroid sulfatase (STS) to biologically active, unconjugated steroids known to regulate spermatogenesis. Significantly reduced SLC10A6 mRNA expression is previously found in different forms of impaired spermatogenesis in man. It is supposed that SLC10A6 plays a role for the local supply of steroids in the testis and consequently for spermatogenesis and fertility.

Fig.1 Identification of novel inhibitors of the steroid sulfate carrier SOAT by pharmacophore modeling. (Grosser, 2016)

Application of SLC10A6 Membrane Protein in Literature

1. Geyer J., Cloning and functional characterization of human sodium-dependent organic anion transporter (SLC10A6). J Biol Chem. 2007, 282(27):19728-41. PubMed ID: 17491011
   
   

   This article shows that SOAT exhibits a seven-transmembrane domain topology with an outside-to-inside orientation of the N-terminal and C-terminal ends. SOAT mRNA is most highly expressed in testis. In placenta and pancreas, SOAT shows extremely high expression. Several nonsteroidal organosulfates also strongly inhibit SOAT, including 1-(omega-sulfooxyethyl) pyrene, bromosulfophthalein, 2- and 4-sulfooxymethylpyrene, and alpha-naphthylsulfate.

2. Grosser G., et al. Transport of steroid 3-sulfates and steroid 17-sulfates by the sodium-dependent organic anion transporter SOAT (SLC10A6). The Journal of Steroid Biochemistry and Molecular Biology. 2018, 179:20-25. PubMed ID: 28951227
   
   

   This article indicates the characteristics of SOAT substrates from the group of sulfated steroids and identifies 17β-estradiol-3,17-disulfate is not transported by SOAT.

3. Bakhaus K., et al. Sodium-dependent organic anion transporter (Slc10a6-/-) knockout mice show normal spermatogenesis and reproduction, but elevated serum levels for cholesterol sulfate. J Steroid Biochem Mol Biol. 2018, 179:45-54. PubMed ID: 28743544
   
   

   This article suggests that Soat is not essential for reproduction because the Slc10a6-/- knockout mice show normal fertile, produce normal litter sizes, and have normal spermatogenesis and sperm vitality.

4. Bakhaus K., et al. The polymorphism L204F affects transport and membrane expression of the sodium-dependent organic anion transporter SOAT (SLC10A6). J Steroid Biochem Mol Biol. 2018, 179:36-44. PubMed ID: 28951225
   
   

   The article shows polymorphism L204F of the SOAT significantly reduces transport function for DHEAS. Besides, it is also shown that SOAT-L204F polymorphism is not a cause of hypospermatogenesis.

5. Bennien J., et al. Rare genetic variants in the sodium-dependent organic anion transporter SOAT (SLC10A6): Effects on transport function and membrane expression. J Steroid Biochem Mol Biol. 2018, 179:26-35. PubMed ID: 28893621
   
   

   In this article, the SLC10A6 gene is analyzed for rare genetic variants which might affect transport function or membrane expression of SOAT. Results show that L44P, Q75R, P107L, G109S, S112F, N113K, S133F, G241D, G263E, G294R, and Y308N have no transport activity for DHEAS at all among 31 analyzed SOAT variants.

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Reference

1. Grosser G, et al. Identification of novel inhibitors of the steroid sulfate carrier 'sodium-dependent organic anion transporter' SOAT (SLC10A6) by pharmacophore modeling. Molecular & Cellular Endocrinology. 2016, 428:133-141.

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