Ask about this productRelated genes to: GLUT4 antibody
- Gene:
- SLC2A4 NIH gene
- Name:
- solute carrier family 2 member 4
- Previous symbol:
- GLUT4
- Synonyms:
- -
- Chromosome:
- 17p13.1
- Locus Type:
- gene with protein product
- Date approved:
- 1989-03-06
- Date modifiied:
- 2016-10-05
Related products to: GLUT4 antibody
Related articles to: GLUT4 antibody
- High-fat diets (HFDs) are a key contributor to obesity and promote oxidative stress and inflammation, which are associated with muscle atrophy and insulin resistance (IR). Passiflora edulis exhibits anti-obesity, antioxidant, and anti-inflammatory effects. The study aimed to investigate the potential benefit of P. edulis f. flavicarpa (PF) extract in preventing obesity-associated muscle atrophy and IR. The PF extract effectively inhibited cholesterol micelle solubility with an IC of 3431 µg/mL and decreased fat accumulation in 3T3-L1 adipocytes. Furthermore, this study investigated a model of HFD-induced IR and muscle atrophy in rats. Thirty-five male Sprague-Dawley (SD) rats were induced with obesity by HFD and were administered 250 and 500 mg/kg/day of PF extract. Rats fed with an HFD were associated with fat accumulation and oxidative stress, which promoted inflammation, muscle damage, muscle atrophy, and IR in obese rats. However, administration of PF extract effectively mitigated these effects. The PF extract decreased fat accumulation in white adipose tissues and gastrocnemius (GAS) muscle by inhibiting fat absorption and synthesis, particularly Cd36 and Hmgcr. The PF extract also notably reduced oxidative stress-induced muscle inflammation and damage via elevating nuclear factor erythroid 2-related factor 2 (Nrf2) and reducing nuclear factor kappa B (NF-κB) expressions. Additionally, PF extract was found to mechanistically prevent muscle atrophy by inhibiting Fbxo32, Trim63, and B-cell lymphoma 2 (BCL2)-associated X (Bax) expressions, while enhancing Bcl2 expression. We also found that PF extract mitigated muscle IR by upregulation of the insulin receptor substrate-1/phosphatidylinositol-3 kinase/protein kinase B (IRS-1/PI3K/AKT) pathway and Slc2a4 expression. The findings indicate that PF extract can prevent skeletal muscle loss and IR in obesity by modulating oxidative stress, inflammation, and activating IRS-1/PI3K/AKT signaling pathway. - Source: PubMed
Chobsuay NraratChonpathompikunlert PennapaSrivilai JukkarinMalakul WachirawadeeLimpeanchob NanteetipAimjongjun SathidTunsophon Sakara - Glucose transporter type 4 (GLUT4), encoded by the gene, is the final effector of insulin-stimulated glucose uptake in insulin-sensitive tissues: skeletal muscle, adipose tissue, and cardiac muscle. Its dynamic localization, retained intracellularly under basal conditions and extensively translocated to the plasma membrane upon stimulation, makes it a master regulator of glycemic homeostasis. While the canonical insulin pathway (PI3K/Akt/TBC1D4) is the most potent and specific mechanism in the postprandial state, its dysfunction is centrally associated with insulin resistance and type 2 diabetes mellitus (T2DM). Crucially, robust alternative signaling networks function completely independently of insulin to regulate GLUT4 synthesis and translocation. Prominent among these are contraction-mediated pathways in skeletal muscle, which employ calcium signaling (via CaMKII), mechanical/metabolic stress sensors (via p38 MAPK γ/δ), and AMP-activated protein kinase (AMPK). This review critically integrates current knowledge, linking the molecular architecture and post-translational modifications of GLUT4 to the complex, tissue-specific signaling networks that govern its vesicular trafficking. We emphasize the hierarchy, redundancy, and interdependence of these pathways, highlighting differences between acute translocation and chronic transcriptional adaptations. Finally, we discuss how deciphering insulin-independent mechanisms offers promising therapeutic opportunities, particularly in identifying pharmacological targets that mimic the metabolic benefits of physical exercise. - Source: PubMed
Publication date: 2026/04/13
Ramos-Jiménez ArnulfoRubio-Valles MariazelGuereca-Arvizuo JaimeJuárez-Oropeza Marco ARamos-Hernández Javier AChávez-Guevara Isaac AGonzález-Rodríguez EverardoMoreno-Brito VerónicaHernández Torres Rosa P - NEGR1 (neuronal growth regulator 1) has been genetically linked to metabolic and neuropsychiatric disorders; however, its cellular function in insulin-responsive tissues remains poorly understood. Here, we investigated the role of NEGR1 in regulating actin cytoskeletal dynamics and insulin-stimulated GLUT4 trafficking in skeletal muscle. We found that loss of reduced GLUT4 abundance selectively in predominantly glycolytic skeletal muscles in vivo. Despite preserved insulin-induced Akt phosphorylation, insulin-stimulated GLUT4 translocation was markedly impaired in both Negr1-deficient and NEGR1-overexpressing muscle cells. Mechanistically, deficiency was associated with enhanced PAK-cofilin signaling and excessive intracellular F-actin accumulation that likely impedes GLUT4 vesicle trafficking. In contrast, NEGR1 overexpression did not increase total F-actin content but induced abnormal peripheral actin organization, resulting in constitutive GLUT4 surface localization and elevated basal glucose uptake. Consistent with these findings, both loss and overexpression of NEGR1 disrupted insulin-induced Rac1-dependent actin remodeling without affecting Akt signaling. Collectively, these results identify NEGR1 as a critical modulator of actin homeostasis required for proper insulin-stimulated GLUT4 trafficking and glucose uptake in skeletal muscle, providing mechanistic insight into the metabolic abnormalities associated with NEGR1 dysregulation. Neuronal growth regulator 1 (NEGR1) regulates actin cytoskeletal homeostasis required for insulin-stimulated GLUT4 trafficking in skeletal muscle. NEGR1 dysregulation alters PAK-cofilin signaling, induces aberrant F-actin organization, and impairs GLUT4 vesicle movement independent of Akt signaling. Because NEGR1 is a major genetic risk factor for major depressive disorder, these findings reveal a shared actin-based mechanism linking metabolic dysfunction and neuropsychiatric disease. - Source: PubMed
Publication date: 2026/03/28
Yun Seo-YoungLee Soojin - Myocardial ischemia-reperfusion injury (MIRI) remains a critical complication associated with cardiopulmonary bypass (CPB). This study investigated whether p38 mitogen-activated protein kinase (p38MAPK) sustains myocardial glucose uptake by controlling glucose transporter-4 (GLUT4) expression and membrane translocation through distinct myocyte enhancer factor-2 (MEF2) isoforms. - Source: PubMed
Publication date: 2026/03/20
Gao WeilongZhang DanZhang BenfaSun PengCao YingYang SiyuanChen HongjinSong Yingnan - Corneal stromal fibrosis represents a major cause of visual impairment, primarily driven in part by the TGF-β1-mediated transition of stromal fibroblasts into contractile myofibroblasts. FARP2, a mediator of Rho-GTPase signaling and cytoskeletal organization, has been proposed as a potential mediator of this phenotypic transition; however, the specific functional contribution stromal remodeling remains largely undefined) its functional role in corneal stromal remodeling remains unclear. CSFs were isolated from New Zealand rabbits and cultured under standard conditions. Myofibroblast differentiation was induced using recombinant TGF-β1 (5 and 20 ng/mL). Gene silencing of FARP2 was performed using sequence-specific siRNA. Gene expression levels of FARP2, RHOA, TLN1, SLC2A4 and the fibrotic extracellular matrix marker COL1A were quantified by Real-time PCR and expressed as log2 fold change and FARP2 protein expression was assessed by Western blotting. The alpha smooth muscle actin (α-SMA) expression was evaluated by immunocytochemistry, and cell migratory capacity was analyzed using the scratch assay. TGF-β1 treatment induced distinct myofibroblast-like morphological changes and significantly increased α-SMA expression. In parallel, TGF-β1 significantly upregulated COL1A1 expression, indicating enhanced extracellular matrix remodeling. TGF-β1 also upregulated FARP2, RHOA, TLN1, and SLC2A4 expression in a dose-dependent manner (p < 0.05). FARP2 knockdown effectively suppressed these transcriptional responses and markedly reduced FARP2 protein levels (p < 0.05). In the scratch assay, TGF-β1 significantly enhanced wound closure kinetics, whereas FARP2 silencing resulted in a pronounced reduction in cell migration and delayed wound repair (p < 0.0001). Additionally, glucose- and TGF-β-induced upregulation of SLC2A4 was substantially attenuated in the absence of functional FARP2. These findings highlight FARP2 as a potential therapeutic candidate. Targeting of FARP2 may represent a promising therapeutic approach for preventing or reducing corneal fibrosis and scar formation. - Source: PubMed
Publication date: 2026/03/03
Rad Lina MoallemiColagar Abasalt HosseinzadehHosseini AsiehDelbandi Ali-Akbar