Solute carrier family 38 (SLC38) transporters are responsible for amino acid transportation. The transporters of this family are divided into two systems, one is system A and the other is system N. SLC38A3, also known as SNAT3, was the first protein identified as a system N transporter that has the ability to counter transporter both Na+ and H+. SNAT3 has high expression in the brain, where it is only found on astrocytes and endothelial cells of the blood-brain barrier. In peripheral tissues, its expression is also found in the liver (in the periportal and perivenous hepatocytes), kidney (in the proximal tubule), heart, skeletal muscle. It is able to transport glutamine, asparagine, and histidine.
|Basic Information of SLC38A3|
|Protein Name||Sodium-coupled neutral amino acid transporter 3|
|Aliases||N-system amino acid transporter 1, Na(+)-coupled neutral amino acid transporter 3, Solute carrier family 38 member 3, System N amino acid transporter 1, G17, NAT1, SN1, SNAT3|
|Organism||Homo sapiens (Human)|
In terms of physiological function and implication in pathological conditions, SLC38A3 has been reported to be involved in energy metabolism, brain physiology, gestation, ammonia detoxification, and acid-base balance. Firstly, in the liver, SLC38A3 plays a role in hepatic ammonia detoxification from the portal blood. Besides, evidence has shown that SLC38A3 is involved in glucose homeostasis. Secondly, in the kidney, SLC38A3 may play a role in the response to acidosis. In the brain, SLC38A3 is assigned a role in the glutamate/glutamine cycle, contributing to optimal neurotransmission. Besides, SLC38A3 mRNA expression has been shown to be highly up-regulated in advanced human gliomas.
Fig.1 Schematic model of the Snat3 transporter.
This study measured the Slc38a3 promoter activity and messenger RNA stability in cultured cells under different pH conditions. It had been concluded that mechanisms underlying the SNAT gene expression regulated by extracellular pH were involved in both post-translational and transcriptional regulations.
Using diet-induced obesity mice, this study investigated whether obesity and insulin resistance could contribute to deranged ammonium excretion. The results showed that obesity and glucose intolerance impaired renal ammonium excretion when fed with NH4Cl, but the stimulation of SNAT3 and ammoniagenic enzyme expression might be compensatory but futile.
Using snat3 mutant mice, this study investigated the effect of the loss of Snat3/Slc38a3 glutamine transporter on the functions of different organs. The results showed that SNAT3 was required for amino acid homeostasis and was critical for various organ functions, including the liver, brain, and kidney.
Using the established model of cultured cerebellar Bergmann glial cells, this study sought to characterize the functional and physical coupling of glutamate uptake and glutamine release. The results showed that EAAT1-induced glutamine release was mediated by SNAT3 in Bergmann glial cells, which was regarded as evidence of functional and physical coupling of glutamate uptake and release.
In this study, treatment of Xenopus laevis oocytes expressing rat SNAT3 with the phorbol ester PMA resulted in a rapid downregulation of glutamine uptake and reduced SNAT3 activity only, indicating the specificity of the regulatory system.
Creative Biolabs now provides integrated service packages of membrane protein preparation for clients across the globe. Backed by our powerful Magic™ Membrane Protein Production Platform, our scientists have successfully expressed, purified, and reconstituted a wide spectrum of difficult-to-handle membrane protein targets, including G protein-coupled receptors, ion channels, and transporters. Your targets can be obtained using both cell-based expression and cell-free expression strategies. Moreover, using our detergent screening platform and lipid screening platform, proteins can be extracted and stabilized with suitable detergents and lipids. Besides, we can also incorporate your proteins into liposomes, nanodiscs, and polymers for further applications. Moreover, virus-like particles are provided for high-density membrane protein display.
Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC38A3 antibody development services.
Contact us if you want to know more about our membrane protein preparation services.