SLC7A5 antibody - N-terminal region (ARP63651_P050)
- Known as:
- SLC7A5 (anti-) - N-terminal region (ARP63651_P050)
- Catalog number:
- arp63651_p050
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Aviva Systems Biology
- Gene target:
- SLC7A5 antibody - N-terminal region (ARP63651_P050)
Related genes to: SLC7A5 antibody - N-terminal region (ARP63651_P050)
- Gene:
- SLC7A5 NIH gene
- Name:
- solute carrier family 7 member 5
- Previous symbol:
- -
- Synonyms:
- LAT1, E16, D16S469E, MPE16, CD98
- Chromosome:
- 16q24.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-01-28
- Date modifiied:
- 2016-10-05
Related products to: SLC7A5 antibody - N-terminal region (ARP63651_P050)
Related articles to: SLC7A5 antibody - N-terminal region (ARP63651_P050)
- Colorectal cancer (CRC) is a leading cause of cancer-related death and is associated with high recurrence rates. Solute carrier family 7 member 5 (SLC7A5), a core transporter that facilitates the transmembrane movement of tryptophan, plays a role in various cancers. However, whether and how SLC7A5 promotes colorectal liver metastasis (CRLM) through tryptophan metabolism reprogramming and immune remodelling remain unexplored. - Source: PubMed
Luo YaohaoLi LeiLi ShanbaoWang XinshuaiHe ZepingSong FangbinQin JunZhang JinyanXu Junming - Vascular remodeling is a central pathological feature of cardiovascular diseases and is driven in part by vascular smooth muscle cell (VSMC) proliferation, migration, and phenotypic switching. The solute carrier family 7 member 5 (SLC7A5), a key amino acid transporter, has been implicated in cellular growth and metabolic regulation, but its role in vascular remodeling remains unclear. We investigated the contribution of SLC7A5 to VSMC activation and the underlying signaling mechanisms. - Source: PubMed
Publication date: 2026/07/14
Bai YuChen SixuanWang YueWu QimingYin Dechun - Head and neck squamous cell carcinoma (HNSCC) poses a significant global health challenge, characterized by low survival rates and frequent metastasis. Conventional therapies are often restricted by systemic toxicity and drug resistance, positioning natural bioactive extracts like Total Glucosides of Paeony (TGP) as promising therapeutic alternatives. While the amino acid transporter SLC7A5 is known to drive tumor proliferation by facilitating leucine uptake and activating the mTOR signaling pathway, the specific interaction between TGP and this SLC7A5/mTOR axis in HNSCC has not been fully elucidated. - Source: PubMed
Publication date: 2026/07/11
Li YuanqiangHu GaofengNiu WenyuanZhang LizhuoGe JiamingXuan JieYu XuefeiMa ShangLi MengjiaZhang ZiqiangLuo KeJia XingLi Qinglin - In this study, we discovered and optimized a novel series of L-type amino acid transporter 1 (LAT1)-selective inhibitors. Starting from compound 1, efforts to explore the structure-activity relationship and optimize selectivity over L-type amino acid transporter 2 (LAT2) revealed the importance of the orientation of the terminal aromatic ring and led to the highly potent and LAT1-selective 2-phenoxy-substituted compound 19. Pharmacokinetic studies of 19 demonstrated that it is orally bioavailable (10 mg/kg, p.o., mouse, AUC:2354 ng·h/mL). Further optimization of the aromatic ring improved its metabolic stability and resulted in highly LAT1-selective and orally bioavailable (10 mg/kg, p.o., mouse, AUC:3449 ng·h/mL) compound 26. This series of compounds should be useful for research on LAT1 inhibitors. - Source: PubMed
Publication date: 2026/03/31
Uesugi ShuheiTsunemi TomoyukiMurafuji HidenobuKadoshima-Yamaoka KumikoMurakawa MasaoMakita NaoyukiTomita UraraDoke YukikoYukiura HiroshiKoyama MakotoHayashi YasuhiroYamashiro KyokoYoshikiyo KazunoriTabata ToshikiMaruoka Hiroshi - L-type amino acid transporter 1 (LAT1) is a heterodimeric membrane protein that primarily facilitates the transport of phenylalanine, along with other amino acids such as valine, leucine, isoleucine, tryptophan, and tyrosine across the cell membrane. It is predominantly expressed at the blood-brain barrier. While LAT1 has been extensively studied in the context of drug delivery, its specific transport pathway for phenylalanine and the related conformational dynamics remains largely unexplored. Investigation of the transport pathway of phenylalanine via LAT1 is also very important, as excessive amounts of phenylalanine can cause phenylketonuria (PKU). Inhibiting LAT1's transport could reduce phenylalanine's entry into the brain, aiding in the management of its levels and alleviating the adverse effects of PKU. To investigate the phenylalanine transport mechanism and the conformational dynamics of LAT1, microsecond-long molecular dynamics (MD) as well as steered molecular dynamics (SMD) and targeted molecular dynamics (TMD) simulations were performed. The results of this study identify essential structural motifs that enable the isomerization of LAT1 among outward-facing, inward-facing, and occluded states. A significant conclusion drawn from this research is the identification of seven critical transmembrane helices that play central roles along the transport pathway, namely, TM1, TM4, TM6, TM7, TM8, TM9, and TM12. Root-mean-square deviation (RMSD) analyses across the structural models further indicate that TM1 and TM6 are consistently engaged during both extracellular and intracellular phenylalanine transitions, whereas TM9 and TM12 contribute more specifically to the outward and inward opening events, respectively. The observed conformational changes offer fresh insights into the alternating-access mechanism of LAT1 during phenylalanine transport, contrasting with conclusions from structural models based on other substrates transport through LAT1. By elucidating this transport mechanism, the study will contribute to developing LAT1 inhibitors that can selectively regulate brain phenylalanine levels without disrupting the transport of other essential amino acids. - Source: PubMed
Publication date: 2026/07/09
Islam Shahidul MHasan Md MehediShah Khushi