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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.

Basic Information of SLC7A2
Protein Name Low affinity cationic amino acid transporter 2
Gene Name SLC7A2
Aliases CAT-2, ATRC2
Organism Homo sapiens (Human)
UniProt ID P52569
Transmembrane Times 14
Length (aa) 698
Sequence MKIETSGYNSDKLICRGFIGTPAPPVCDSKFLLSPSSDVRMIPCRAALTFARCLIRRKIVTLDSLEDTKLCRCLSTMDLIALGVGSTLGAGVYVLAGEVAKADSGPSIVVSFLIAALASVMAGLCYAEFGARVPKTGSAYLYTYVTVGELWAFITGWNLILSYVIGTSSVARAWSGTFDELLSKQIGQFLRTYFRMNYTGLAEYPDFFAVCLILLLAGLLSFGVKESAWVNKVFTAVNILVLLFVMVAGFVKGNVANWKISEEFLKNISASAREPPSENGTSIYGAGGFMPYGFTGTLAGAATCFYAFVGFDCIATTGEEVRNPQKAIPIGIVTSLLVCFMAYFGVSAALTLMMPYYLLDEKSPLPVAFEYVGWGPAKYVVAAGSLCALSTSLLGSMFPLPRILFAMARDGLLFRFLARVSKRQSPVAATLTAGVISALMAFLFDLKALVDMMSIGTLMAYSLVAACVLILRYQPGLSYDQPKCSPEKDGLGSSPRVTSKSESQVTMLQRQGFSMRTLFCPSLLPTQQSASLVSFLVGFLAFLVLGLSVLTTYGVHAITRLEAWSLALLALFLVLFVAIVLTIWRQPQNQQKVAFMVPFLPFLPAFSILVNIYLMVQLSADTWVRFSIWMAIGFLIYFSYGIRHSLEGHLRDENNEEDAYPDNVHAAAEEKSAIQANDHHPRNLSSPFIFHEKTSEF

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.

SLC7A2 regulates the intimate attachment of A/E pathogens to epithelial cells. 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.

SLC7A2 Preparation Options

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find an optimal match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-SLC7A2 antibody development services.


Over years, Creative Biolabs has successfully generated massive functional membrane proteins for our customers. We are glad to provide one-stop, custom-oriented service packages regarding a variety of membrane protein targets. Please contact us for more information if you need.

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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