SLC38A5 Membrane Protein Introduction

Introduction of SLC38A5

Sodium-coupled neutral amino acid transporter 5 (SNAT5 or SLC38A5) belongs to the system N subfamily of amino acid transporter family. SLC38A5 shares 61% sequence identity to SLC38A3, which was the first identified system N transporter. Like SLC38A3, SLC38A5 transports zwitterionic amino acids in a Na+-dependent and markedly pH-sensitive manner, displaying limited substrate specificity with a preference for glutamine > histidine > asparagine. SLC38A5 is expressed in the brain and found in astrocytes. Additionally, SLC38A5 is found in other tissues such as the stomach, with very high expression, as well as the lungs, spleen, and colon. Structurally, this protein is demonstrated to have 11 transmembrane segments.

Basic Information of SLC38A5
Protein Name Sodium-coupled neutral amino acid transporter 5
Gene Name SLC38A5
Aliases Solute carrier family 38 member 5, System N transporter 2, JM24, SN2, SNAT5
Organism Homo sapiens (Human)
UniProt ID Q8WUX1
Transmembrane Times 11
Length (aa) 472

Functions of SLC38A5 Membrane Protein

SLC38A5 is tightly associated with synapses in the brain, together with SNAT3, and participates in the function of the glutamine- GABA-glutamate cycle, being responsible for the glutamine release from the astrocytes in the intercellular space. Moreover, studies have reported that it might contribute to the regulation of glycine concentration in glutamatergic synapses and, therefore, to the functioning of the N-methyl-d-aspartate (NMDA) subtype of glutamate receptors. Besides, in periportal hepatocytes, SLC38A3 and SLC38A5 are likely to be involved in the uptake of glutamine. SLC38A5 is also expressed in the kidney where it is probably involved in ammoniagenesis especially during metabolic acidosis.

SLC38A5 Membrane Protein Introduction

Application of SLC38A5 Membrane Protein in Literature

  1. Rodríguez A., et al. Expression of the System N transporter (SNAT5/SN2) during development indicates its plausible role in glutamatergic neurotransmission. Neurochemistry international. 2014, 73: 166-171. PubMed ID: 24333324

    This study analyzed the profile of SNAT5 expression during development in comparison with that of other transporters involved in amino acid fluxes in the glutamatergic system. The results showed that the ontogenic emergence of SNAT5 in glial cells occurred in a concerted manner with other glutamate and glutamine transporters.

  2. Singh S., et al. Unique regulation of Na-glutamine cotransporter SN2/SNAT5 in rabbit intestinal crypt cells during chronic enteritis. Journal of cellular and molecular medicine. 2018, 22(3): 1443-1451. PubMed ID: 29271063

    This study sought to determine the mechanism of regulation of Na-nutrient cotransporter SNAT5 by arachidonic acid metabolites in crypt cells. The findings provided evidence that SNAT5 stimulation in crypt cells was mediated by the leukotriene pathway during chronic intestinal inflammation.

  3. Hashim M., et al. Inhibition of SNAT5 induces incretin responsive state from incretin unresponsive state in pancreatic β-cells: study of β-cell spheroid clusters as a model. Diabetes. 2018, 67(9): 1795-1806. PubMed ID: 29954738

    This study investigated the mechanism by which an incretin unresponsive state transforms into an incretin responsive state using the spheroid clusters (K20-SC) as a model. The results showed that the suppression of SNAT5 activity resulted in increased glutamate production and that enhancement of cAMP signaling endowed incretin unresponsive β-cells with incretin responsiveness.

  4. Hamdani E.H., et al. The system N transporter SN2 doubles as a transmitter precursor furnisher and a potential regulator of NMDA receptors. Glia. 2012, 60(11): 1671-1683. PubMed ID: 22821889

    This article reported that rat SNAT5 mediated electroneutral and bidirectional transport of glutamine and glycine at perisynaptic astroglial membranes. It was suggested that this transporter functioned as both a transmitter precursor furnisher and a potential regulator of NMDA receptors.

  5. Singh S., et al. Mast cell regulation of Na-glutamine co-transporters B0AT1 in villus and SN2 in crypt cells during chronic intestinal inflammation. BMC gastroenterology. 2015, 15(1): 47. PubMed ID: 25884559

    This study sought to determine the regulation of B0AT1 and SNAT5 by mast cells during chronic enteritis using male rabbit models with chronic intestinal inflammation. The results showed that mast cells probably functioned as a regulator of the B0AT1 in villus cells and SN2 in crypts cells.

SLC38A5 Preparation Options

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