HTLV I&II Ab (screening)
- Known as:
- HTLV I&II Antibody (detection)
- Catalog number:
- HTLVAB.CE.480
- Product Quantity:
- 480 Tests n
- Category:
- -
- Supplier:
- DiaPro
- Gene target:
- HTLV & (screening)
Related genes to: HTLV I&II Ab (screening)
- Gene:
- SLC2A1 NIH gene
- Name:
- solute carrier family 2 member 1
- Previous symbol:
- GLUT1, GLUT, HTLVR, CSE
- Synonyms:
- DYT18, DYT9
- Chromosome:
- 1p34.2
- Locus Type:
- gene with protein product
- Date approved:
- 1994-11-18
- Date modifiied:
- 2019-04-23
Related products to: HTLV I&II Ab (screening)
Related articles to: HTLV I&II Ab (screening)
- Successful placentation requires coordinated regulation of trophoblast differentiation, immune tolerance, vascular remodeling, and nutrient transport during the peri-implantation period. The chemokine ligand CXCL12 and its receptor CXCR4 are expressed at the fetal-maternal interface and implicated in trophoblast migration, immune regulation, and angiogenesis, but their in vivo role in early placental functional development remains unclear. The objective of this study was to determine whether suppression of CXCL12/CXCR4 signaling during implantation alters placental programming in sheep. Ewes received intrauterine infusion of CXCR4 antagonist AMD3100 from Day 12-19 of pregnancy, and tissues were collected on Day 20. Pregnancy rates were not affected by treatment; however, pregnancy-associated glycoprotein abundance was increased in treated ewes, indicating altered trophoblast differentiation. Inhibiting CXCR4 reduced expression of angiogenic factors including vascular endothelial growth factor A, placental growth factor, fms-like tyrosine kinase-1, and angiopoietin-1 in endometrium, consistent with impaired vascular development. Suppression of CXCR4 also shifted immune signaling toward a pro-inflammatory profile, with increased interferon-gamma and interleukin-12 and decreased transforming growth factor beta. In addition, expression of glucose and amino acid transporters, including SLC2A1, SLC2A3, SLC38, and SLC7 family members, was altered in fetal membranes and endometrium, accompanied by increased autophagy marker LC3B-II, suggesting metabolic stress. These findings demonstrate that CXCL12/CXCR4 signaling is not required for conceptus attachment but is important for coordinated development of vascular, immune, and metabolic pathways during early placentation. Disruption of this axis produces molecular changes consistent with placental insufficiency, supporting a central role for CXCL12/CXCR4 in establishing functional placental capacity. - Source: PubMed
Publication date: 2026/09/24
Ashley RyanMullins MakaylaSalopek ShaylieSaucedo KylaAlvarez EmaHunt MonetBaez SamanthaKronlein NiklasValdez KassandraButler LaurenRopp Kate - Glucose is the primary energy substrate for the developing foetus, and placental glucose transport is a key element of pregnancy physiology. In early gestational diabetes mellitus, metabolic alterations may disrupt the expression of glucose transporters (GLUTs). This study evaluated the influence of physical activity, monitored using pedometers, on the expression of the SLC2A1 (GLUT-1), SLC2A3 (GLUT-3), and SLC2A4 (GLUT-4) genes in the placentas of women with early gestational diabetes, and analysed associations between GLUT expression and clinical parameters. - Source: PubMed
Publication date: 2026/09/21
Sochacki MateuszSibiak RafalMantaj UrszulaAdamczak LukaszBlatkiewicz MalgorzataRucinski MarcinWender-Ozegowska Ewa - Glucose transporter type 1 deficiency syndrome (Glut1DS) is a rare autosomal dominant genetic disorder caused by mutations in SLC2A1, which results in impaired glucose transport across the blood-brain barrier. Patients with Glut1DS present with various symptoms, including seizures, delayed development and movement disorders. The current first-line therapy - ketogenic diet - has shown variable efficacy, highlighting the need to explore alternative therapeutic strategies. This study aimed to investigate comprehensive phenotypic characteristics of the Glut1DS mouse model B6(D2)-Slc2a1/1Rbrc to establish foundational data for identifying novel therapeutic targets. The Slc2a1Rgsc200 mutant mouse was phenotypically characterized at the Japan Mouse Clinic of the RIKEN BioResource Research Center by using a phenotyping pipeline that included intraperitoneal glucose tolerance test (IPGTT) and clinical blood chemistry analyses. Heterozygous Glut1DS mutants exhibited no differences in basal plasma glucose or glycosylated hemoglobin A1c levels when compared to wild-type controls. However, female heterozygous mutants showed decreased glucose levels during IPGTT, accompanied by increased plasma insulin levels following glucose administration. These findings support recent evidence linking insulin signaling to seizure control in patients with Glut1DS, as demonstrated in human studies. - Source: PubMed
Publication date: 2026/09/21
Furuse TamioKushida TomokoShinogi AkikoOzaki MaoYanagisawa RyokoTamura Masaru - This manuscript is the corrected version of a previously published paper. Glucose uptake by mammalian cells is a key mechanism to maintain cell and tissue homeostasis and relies mostly on plasma membrane-localized glucose transporter proteins (GLUTs). Two main cellular mechanisms regulate GLUT proteins in the cell: first, expression of GLUT genes is under dynamic transcriptional control and is used by cancer cells to increase glucose availability. Second, GLUT proteins are regulated by membrane traffic from storage vesicles to the plasma membrane (PM). This latter process is triggered by signaling mechanisms and is well studied in the case of insulin-responsive cells, which activate protein kinase AKT to phosphorylate TBC1D4, a RAB-GTPase-activating protein involved in membrane traffic regulation. Previously, we identified protein kinase WNK1 as another kinase able to phosphorylate TBC1D4 and regulate the surface abundance of the constitutive glucose transporter GLUT1. Here we describe that downregulation of WNK1 through RNA interference in HEK293 cells led to a two-fold decrease in cell-surface GLUT1 abundance, concomitant with a 40% decrease in glucose uptake. By mass spectrometry, we identified serine (S) 704 in TBC1D4 and also S565 in its paralogue TBC1D1 as candidate WNK1 phosphorylation sites. Transfection of the respective phosphomimetic or unphosphorylatable TBC1D mutants into cells revealed that both affected the cell-surface abundance of GLUT1. The results reinforce a regulatory role for WNK1 in GLUT1 trafficking and glucose uptake and may have potential impact for the understanding of metabolic dysregulation, as observed in many cancer cells or insulin-responsive cell types. - Source: PubMed
Publication date: 2026/08/31
Henriques Andreia F AMatos PauloCarvalho Ana SofiaAzkargorta MikelElortza FelixMatthiesen RuneJordan Peter - Canine malignant melanoma is an aggressive neoplasm with limited remedial options. Therefore, the development of novel antineoplastic agents is urgently needed. This study investigated the medicinal potential and molecular mechanisms of Roxb. essential oil (CEO) against canine melanoma. Phytochemical profiling via GC-MS identified 22 compounds, with monoterpenoids (90.99%) predominating, specifically sabinene (53.25%) and terpinen-4-ol (17.99%). CEO exhibited potent, concentration-dependent cytotoxicity across four canine melanoma cell lines, with a mean IC₅₀ of approximately 0.006% v/v. Quantitative proteomic mapping of CEO-treated M5 cells identified a total of 222 differentially expressed proteins associated with systemic cellular collapse. Key mechanisms included significant genotoxic stress (upregulation of H2AX and histone variants), endoplasmic reticulum stress (suppression of CALR and HSPB1), and the activation of a coordinated necroptosis/mitophagy axis (modulation of Drp1, VDAC, and p62). Protein-protein interaction network analysis further identified SLC2A1 as a central metabolic hub with high-confidence connectivity to conventional chemotherapies, suggesting that CEO-induced metabolic disruption converges onto core pathways targeted by 5-fluorouracil and imatinib. These findings suggest that CEO induces complex cell death signatures through coordinated nuclear and organelle stress. Ultimately, it should be considered as a promising candidate for future translational research and functional validation. - Source: PubMed
Publication date: 2026/08/26
Chongrattanameteekul PeerawitKe Chiao-HsuLin Chen-SiChuammitri PhongsakornMatchimakul PitchayaLumsangkul ChompunutOkonogi SiripornMektrirat Raktham