SLC7A2 Membrane Protein Introduction

Introduction of SLC7A2

SLC7A2 (solute carrier family 7 member 2), also known as CAT-2 or ATRC2, is a cationic amino acid transporter. Encoded by the gene SLC7A2, the transporter SLC7A2 belongs to SLC7 family, which can be divided into two major subgroups, cationic amino acid transporters (CATs, SLC7A1-4) and glycoprotein-associated amino acid transporters (gpaATs, SLC7A5-11), also called catalytic chains of the hetero(di)meric amino acid transporters (HATs). The SLC7A2 gene, containing 12 exons, is mapped to chromosome 8p22. It is reported that three transcript variants have been found for this gene and they encode different isoforms correspondingly. Similar to other members of CATs subgroup, SLC7A2 also has 14 predicted transmembrane (TM) segments and is glycosylated, the positions of the glycosylation sites vary between isoforms and between species. It is documented that N-ethylmaleimide can down-regulate the expression of SLC7A2.

Function of SLC7A2 Membrane Protein

As an important member of CATs subgroup, SLC7A2 mediates the cellular uptake of cationic amino acids such as arginine, lysine and ornithine with pH- and sodium-independence, apparently as an exchange mechanism. SLC7A2 is demonstrated to play a critical regulatory role in classical or alternative activation of macrophages via arginine transport. It is acknowledged that arginine acts as a substrate for nitric oxide synthase (NOS) which is responsible for the production of the nitric oxide (NO). NO abundance in inflammatory cells promotes the progression of diseases such as inflammatory bowel disease, cancer, arthritis, Crohn's disease, and atherosclerosis. Because of the ability to transport arginine, SLC7A2 has been implicated in immune responses to pathogens and in controlling inflammation as well as IL-17 activation in an injury model of colitis. The SLC7A2^-/- mice exhibit increased numbers of memory T cells and activated dendritic cells in the lungs, while gastric macrophage levels and iNOS/NO biosynthesis in macrophages is significantly reductive. SLC7A2 transporters are associated with the transient increase of arginine transport through system y(+) induced by phorbol esters or thymeleatoxin.

Fig.1 SLC7A2 regulates the intimate attachment of A/E pathogens to epithelial cells. (Singh, 2016)

Application of SLC7A2 Membrane Protein in Literature

1. Singh K., et al. The L-arginine transporter solute carrier family 7 member 2 mediates the immunopathogenesis of attaching and effacing bacteria. PLoS pathogens. 2016, 12(10): e1005984. PubMed ID: 27783672
   
   

   The authors used the Slc7a2 ^–/– mice infected with Citrobacter rodentium to assess the role of SLC7A2 in murine infection. They demonstrated that SLC7A2 can enhance the attachment of C. rodentium to the epithelium and thus create its ecological niche, which may increase its own pathogenicity.

2. Visigalli R., et al. Rapamycin stimulates arginine influx through CAT2 transporters in human endothelial cells. Biochimica et Biophysica Acta (BBA)-Biomembranes. 2007, 1768(6): 1479-1487. PubMed ID: 17397797
   
   

   This article demonstrated that except tumor necrosis factor-alpha (TNFα), rapamycin (an inhibitor of mTOR kinase) can also stimulate CAT2-mediated arginine uptake in human endothelial cells, indicating that mTOR activity is associated with the repression of CAT2 expression.

3. Yeramian A., et al. Arginine transport via cationic amino acid transporter 2 plays a critical regulatory role in classical or alternative activation of macrophages. The Journal of Immunology. 2006, 176(10): 5918-5924. PubMed ID: 16670299
   
   

   The authors demonstrated that Th1-type and Th2-type cytokines can activate bone marrow-derived macrophages, resulting in an increase of L-arginine transport only through the y(+) system, especially Slc7A2. Moreover, Slc7A2 knockout mice showed a decrease in L-arginine transport in response to Th1-type and Th2-type cytokines.

4. Barry D.P., et al. Cationic amino acid transporter 2 enhances innate immunity during Helicobacter pylori infection. PLoS One. 2011, 6(12): e29046. PubMed ID: 22194986
   
   

   The authors used CAT2(-/-) mice to investigate the importance of CAT2 in vivo during H. pylori infection, and they found that gastric macrophage levels, macrophage expression of iNOS, dendritic cell activation, and expression of granulocyte-colony stimulating factor in CAT2(-/-) mice were significantly suppressed, indicating that CAT2 can enhance the innate immune response during H. pylori infection.

5. Lauteala T., et al. Human cationic amino acid transporter gene hCAT-2 is assigned to 8p22 but is not the causative gene in lysinuric protein intolerance. Human genetics. 1997, 100(1): 80-83. PubMed ID: 9225973
   
   

   The authors firstly cloned cDNAs of hCAT-2A and hCAT-2B, which are most likely to the product of the same gene, hCAT-2. And they mapped the hCAT-2 gene to chromosome 8p22. Furthermore, by linkage analysis in Finnish LPI families, they revealed that hCAT-2B was involved in LPI disease.

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Reference

1. Singh K, et al. (2016). The L-arginine transporter solute carrier family 7 member 2 mediates the immunopathogenesis of attaching and effacing bacteria. PLoS pathogens. 12(10): e1005984.

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