System N/A neutral amino acid transporter (SNAT, SLC38A1) is a family of transporters involved in transferring neutral and aliphatic amino acids across the cell membrane. The SNAT family is also called SLC38 family. The transporters in this family are responsible for either system A or system N transport. SLC38A1 belongs to system A subfamily, meaning that this protein is exclusively Na+ dependent. It couples amino acid transport to the Na+ electrochemical potential gradient with 1:1 stoichiometry. Moreover, it could be inhibited by the amino acid analog 2-methylamino-isobutyric acid (MeAIB). Hydropathy analysis predicts that SLC38A1 has 11 membrane-spanning domains. The tissue distribution of this transporter includes the brain, retina, heart, placenta, adrenal gland. Primarily, it is expressed in neuronal cells of the brain, axons of ganglion cells in the nerve fiber, and optic nerves of the retina. SLC38A1 preferentially transports L-glutamine (Gln) followed by L-histidine and L-alanine.
|Basic Information of SLC38A1|
|Protein Name||Sodium-coupled neutral amino acid transporter 1|
|Aliases||Amino acid transporter A1, N-system amino acid transporter 2, Solute carrier family 38 member 1, System A amino acid transporter 1, System N amino acid transporter 1|
|Organism||Homo sapiens (Human)|
Various physiological studies and pathological studies have revealed the involvement of SLC38A1. Firstly, SLC38A1 has been postulated to play a critical role in Gln-glutamate recycling and in the generation of neurotransmitters. Additionally, the stimulation of neuronal differentiation associated with the enhancement of dendritic development by brain-derived neurotrophic factor requires the up-regulation of SLC38A1 expression. The low expression of SLC38A1 has been reported to be associated with suicidal behavior. Many studies have demonstrated that SLC38A1 played a potential role in cancer development and progression, including hepatocellular carcinoma, breast cancer, osteosarcoma, and cholangiocarcinoma. As a result, SLC38A1 might serve as a prognostic and therapeutic marker of these cancers or tumor diseases.
Fig.1 Proposed structure of human SNAT1.
This study characterized the role of SLC38A1, which was a MeCP2 target gene, in microglia to understand the mechanism of microglia dysfunction in Rett syndrome. The results suggested a therapeutic potential of mitochondria-targeted antioxidants for Rett syndrome.
This study investigated the N-glycosylation of SNAT1 and the importance of N-glycosylation for SNAT1 function. The results showed that there were three de novo glycosylation sites and this modification might play an important role in the transport of substrates across the cell membrane.
This study investigated the functional link between the SNATs, L-citrulline, and NO signaling using the siRNA technique. The results showed that SNAT1 mediated L-citrulline transport modulated eNOS coupling and thus regulated NO production in hypoxic PAECs from newborn piglets, suggesting that increasing the SNAT1-mediated L-citrulline might be potential therapeutic strategies to enhance NO production in patients with pulmonary vascular diseases.
This study investigated SNAT1 expression in breast cancers and explored the underlying mechanism of this protein in promoting breast carcinogenesis using RT-PCR, Western blotting, and tissue microarray. Results showed that the correlation of SANT1 with Akt signaling might play a critical role in the development and progression of breast cancer.
Using Hela epithelial cervical cancer cells and 143B osteosarcoma cells that expressed glutamine transporters such as SNAT1, this study investigated the role of these transporters for glutaminolysis. The results showed that the expression of SNAT1 and SNAT2 were required for glutamine uptake.
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