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Validated All-in-One™ qPCR Primer for SLC3A2(NM_001012662.3) Search again
Powered by BiozBy default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene is a member of the solute carrier family and encodes a cell surface, transmembrane protein with an alpha amylase domain. The protein exists as the heavy chain of a heterodimer, covalently bound through di-sulfide bonds to one of several possible light chains. It associates with integrins and mediates integrin-dependent signaling related to normal cell growth and tumorigenesis. Alternate transcriptional splice variants, encoding different isoforms, have been characterized. [provided by RefSeq].
Gene References into function
- Data show that, in vitro, under physiological conditions, CD98 is constitutively associated with beta1 integrins regardless of activation status.
- the interaction of CD98/LAT2 with ICAM-1, found to be expressed to the basolateral domain, and the potential of such interaction on intracellular signal activation in Caco2-BBE cell monolayers
- Involved in process of cell fusion necessary for syncytiotrophoblast formation. During this physiologically important event, amino acid transport activity is also regulated through expression of this membrane protein.
- The heavy chain of the cell surface antigen 4F2 is induced by lysophosphatidylcholine, oxLDL and many oxidation products. It mediates increased cytokine production by endothelial cells.
- results explain how high expression of CD98hc antigen in human cancers contributes to transformation
- iRNA-induced reduction in CD98 expression suppresses cell fusion during syncytialization of placental cell line.
- CD98hc is an integrin-associated protein that mediates integrin-dependent signals, which promote tumorigenesis.
- CD98 is a scaffolding protein that interacts with basolaterally expressed amino acid transporters and beta1 integrins and can alter amino acid transport and cell adhesion, migration and branching morphogenesis
- The 15 carboxy-terminal residues of 4F2hc are required for the transport function of the heterodimer. Mutation of the conserved residue leucine 523 to glutamine in the carboxy terminus reduced the Vmax of arginine and leucine uptake.
- Results demonstrated that a reduction of Sp1 or NF-kappaB expression reduced CD98 protein expression.
- data suggest N-glycosylation of CD98 & subsequent interaction with galectin 3 is critical for aspects of placental cell biology, & provides rationale for observation that in mice truncation of CD98hc extracellular domain leads to early embryonic lethalit
- CD98hc is a bridge between multidrug resistance phenotype and tumor metastasis
- The structure of human 4F2HC ectodomain provides a model for homodimerization and electrostatic interaction with plasma membrane.
- The transmembrane domain of CD98 heavy chain has an essential role in the stimulation of alpha(v)beta(3) integrin for cell adhesion and motility.
- Altogether, our results support a model whereby CyPB induces integrin-mediated adhesion via interaction with a multimolecular unit formed by the association between CD147, CD98 and beta1 integrins.
- interaction between SLC3A2 and SAT1 suggests that these proteins may facilitate excretion of acetylated polyamines.
- Inhibition of system L (LAT1/CD98hc) reduces the growth of cultured human breast cancer cells.
- CD98 expression in primary and metastatic neoplasms is reported.
- CD98 was phosphorylated in vitro by ecto-protein kinases from Jurkat cells and by the commercial casein kinase 2 (CK2).