SLC5A10 Membrane Protein Introduction

Introduction of SLC5A10

SLC5A10 (solute carrier family 5 member 10), also known as SGLT5, or SGLT-5, is a transmembrane protein with a molecular weight of 64.3 kDa that contains 596 amino acids. In humans, it is encoded by the SLC5A10 gene which mapped at the chromosome 17p11.2. SLC5A10 is a member of the sodium glucose cotransporter (SGLT) family that is responsible for actively catalyzing carbohydrate transport across the cellular membrane. It is demonstrated this gene is exclusively expressed in the kidney and there are four splice variants detected. This transporter can mediate sodium-dependent [(14)C]-α-methyl-D-glucose (AMG) transport that can be inhibited by mannose, fructose, glucose, and galactose.

Function of SLC5A10 Membrane Protein

This cotransporter is a membrane transport protein that uses the electrochemical potential gradients (Na⁺ and H⁺) to transport sugars, neurotransmitters, amino acids, and osmolytes into the cell against their concentration gradients. The Na⁺-dependent glucose SLC5 family comprises 12 human members, 6 (SGLT1 to SGLT6) of which have the capacity to bind and transport monosaccharides. For a long time, there is a little known about SLC5A10. Recently, RT-PCR analysis has indicated that SLC5A10 is mainly present in the kidney and resembles the SGLT2 expression pattern. The radiotracer uptake assays reveal it is able to transport mannose, glucose, fructose, and galactose in a Na⁺-dependent manner. And the highest uptake is measured for mannose followed by fructose, whereas, glucose and galactose show very low uptake rates. Moreover, a related pathway about SLC5A10 is glycosaminoglycan metabolism. Therefore, this transporter protein may employ as a kidney-specific, Na⁺-dependent mannose and fructose cotransporter.

Fig.1 (A) Gene structure of SGLT-5 (Ensembl Gene ENSG00000154025 [SLC5a10]); (B) Functional characterisation of SGLT-5. (Grempler, 2012)

Application of SLC5A10 Membrane Protein in Literature

1. Li M., et al. Genome-wide association study of 1,5-anhydroglucitol identifies novel genetic loci linked to glucose metabolism. Sci Rep. 2017, 7(1): 2812. PubMed ID: 28588231
   
   

   This paper conducts genome-wide association research of serum 1,5-anhydroglucitol (1,5-AG) concentrations in 7,550 European ancestry (EA) and 2,030 African American (AA) participants free of diagnosed diabetes. Seven loci in or near SLC50A1, MCM6, SI, MGAM, MGAM2, SLC5A10, and SLC5A1 have been revealed genome-wide significant correlations in EA, and five of them were novel.

2. Nakamura M., et al. Evaluation of the mRNA and protein expressions of nutritional biomarkers in the gastrointestinal mucosa of patients with small intestinal disorders. Intern Med. 2016, 55(16): 2145-2152. PubMed ID: 27522989
   
   

   This study finds a comparison of mRNA expression profile in each intestinal section that in the upper jejunum, the SGLT1 mRNA level in the tumor group and the GIP mRNA level in the Inflammation group are greatly higher than the corresponding levels in the control group.

3. Ghezzi C., et al. Fingerprints of hSGLT5 sugar and cation selectivity. Am J Physiol Cell Physiol. 2014, 306(9): C864-870. PubMed ID: 24573086
   
   

   The report confirms that hSGLT5 is a sodium/mannose transporter blocked by phlorizin. Li(+) and H(+) ions also can drive mannose transport and this transport is electrogenic. Moreover, results indicate that substrates require a pyranose ring with an axial hydroxyl group (-OH) on carbon 2 (C-2).

4. Fukuzawa T., et al. SGLT5 reabsorbs fructose in the kidney but its deficiency paradoxically exacerbates hepatic steatosis induced by fructose. PLoS One. 2013, 8(2): e56681. PubMed ID: 23451068
   
   

   There is no compensatory effect from other transporters reportedly implicated in fructose uptake in the liver and kidney at the mRNA level. The intriguing findings display a previously unknown link through SGLT5 between hepatic lipid metabolism and renal fructose reabsorption.

5. Grempler R., et al. Functional characterisation of human SGLT-5 as a novel kidney-specific sodium-dependent sugar transporter. FEBS Lett. 2012, 3586(3): 248-253. PubMed ID: 22212718
   
   

   SGLT-5 is responsible for the mediation of mannose, fructose and sodium-dependent [(14)C]-α-methyl-D-glucose (AMG) transport is weakly (μM potency) inhibited by SGLT-2 inhibitors. In conclusion, the review characterizes SGLT-5 as a kidney mannose transporter. And further studies are warranted to investigate the physiological role of SGLT-5.

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Reference

1. Grempler R, et al. (2012). Functional characterisation of human SGLT-5 as a novel kidney-specific sodium-dependent sugar transporter. FEBS Lett. 586(3), 248-253.

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