GLUT4 Blocking peptide (Mouse)
- Known as:
- GLUT4 Blocking short protein sequence (Mouse)
- Catalog number:
- 30r-ag010
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Fitzgerald industries international
- Gene target:
- GLUT4 Blocking peptide (Mouse)
Related genes to: GLUT4 Blocking peptide (Mouse)
- 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 Blocking peptide (Mouse)
Related articles to: GLUT4 Blocking peptide (Mouse)
- 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 - Clinically prior hyperglycemia may lead to long-lasting adverse cardiovascular effects, a process referred to as 'glycemic memory.' Epigenetic modifications, specifically DNA methylation changes, may play a key role in this phenomenon. This study investigated if prior high glucose delivery to cardiomyocytes, led to worsened cardiovascular effects upon pressure overload and to ascertain the gene expression and corresponding DNA methylation signatures linked to glycemic memory. Using inducible and cardiomyocyte-specific glucose transporter 4 (GLUT4) overexpressing mice. We induced glucose delivery for 2 weeks, then returned to basal uptake for 2 weeks, followed by sham or transverse aortic constriction (TAC) surgery as a secondary stress. Mice were followed for an additional 8 weeks and assessed for contractile function, cellular remodeling, and molecular changes. TAC led to an exacerbated hypertrophic response and cardiac dysfunction in the transgenic mice. Subsequent analysis identified molecular changes akin to heart failure, worsened cardiac fibrosis, and oxidative stress. Using bulk RNA-sequencing and reduced representation bisulfite sequencing, we discovered differential gene expression and DNA methylation signatures that persisted even after cellular glucose levels reverted to normal. Significant changes across both expression and methylation-identified enriched pathways related to adverse cardiac events, supporting a glycemic memory response. Glycemic memory led to cardiac structural and functional exacerbation, mimicking heart failure, when subjected to a secondary stress. Our data identified transcriptome, and preliminary DNA methylome changes which may potentially be molecular signatures of future therapeutic targets associated with this heart failure susceptibility resulting from enhanced glucose delivery. - Source: PubMed
Publication date: 2026/03/04
Bakshi SayanChang Samuel FPotter Luke ASun ZhihuanHa Chae-MyeongPreuss KerstinReddy Mahima SHarrell Caitlin AChatham John CWende Adam R - PERM1 has been identified as a key regulator of muscle energy metabolism, contractile function, and mitochondrial biogenesis. To investigate the impact fasting and acute and chronic high-intensity exercise on p38MAPK, pCaMKII, and and on PERM1 target genes (, and ) in human skeletal muscle. We performed secondary analyses of muscle biopsy samples from two previously published studies, and from one unpublished study. Muscle biopsies were analyzed from the following protocols: (1) nine men pre-, during, and post- an 8 h fast with or without 2 h of arm ergometer exercise; (2) nine men and eight women pre- and 3 h post-acute high-intensity interval cycling exercise (HIIE); and (3) eleven men and eight women pre- and post- a 6-week period of high-intensity interval training (HIIT) or nonexercise control. We used RT-PCR and Western blotting to determine the and protein levels, respectively. Immunolabelling, microscopy, and subcellular fractionation were also performed to assess PERM1 cellular localization. Fasting did not induce detectable changes in the PERM1-related pathways. HIIE significantly increased p-p38MAPK ( < 0.05, = 1.27) protein, and ( < 0.05, = 0.781) and ( < 0.05, = 1.51) mRNA. Six weeks of HIIT increased the protein levels of PERM1 isoform 2 ( < 0.05, ƞ= 0.168) and CKMT2 ( < 0.05, ƞ= 0.226). PERM1 was localized in the perinuclear region and enriched in the mitochondria. Our results suggest that only some components of PERM1-related pathways are preserved in human skeletal muscle, highlighting the importance of future studies examining PERM1 function in humans. - Source: PubMed
Menezes E SIslam HArhen B BWu ZPacitti L JLyrae Silva N MChiarot ANg S YWilkinson J ANederveen JSimpson C AMcGlory CDe Felice F GGurd B J - There is evidence demonstrating the risk of developing diabetes mellitus because of SARS-CoV-2 infection. Therefore, further research is needed to determine pathological mechanisms at which SARS-CoV-2 induces diabetes mellitus. This study therefore aims to understand the effect of SARS-CoV-2 Main protease (M) on glucose uptake and GLUT-4 translocation as well as AKT, GLUT-4, and IL-6 expression in skeletal muscle (C2C12). - Source: PubMed
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