Ask about this productRelated genes to: G6pc antibody
- Gene:
- G6PC NIH gene
- Name:
- glucose-6-phosphatase catalytic subunit
- Previous symbol:
- G6PT
- Synonyms:
- GSD1a, G6PC1
- Chromosome:
- 17q21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-05
- Date modifiied:
- 2019-04-23
Related products to: G6pc antibody
Related articles to: G6pc antibody
- Metformin is the first-line oral anti-diabetic agent. Metformin concentrations in the intestine can reach up to 1.3 mM, while those in the portal vein are approximately 0.075 mM. It is unclear whether this metformin concentration difference contributes to metformin's antidiabetic effects. Here, we showed that high metformin concentrations upregulate G6PC expression through AMP-activated protein kinase (AMPK) activation to prevent glucose release in intestinal epithelial cells (IECs). The inhibition of mitochondrial activity by high metformin concentrations leads to drastically increased glucose utilization through glycolysis, along with lactate overproduction in the IECs. Subsequently, glycolytic metabolite lactate is released from IECs into portal vein and delivered to the liver. In the liver, low concentrations of metformin activate AMPK to promote mitochondrial fission and mitophagy to maintain a healthy mitochondrial population, resulting in increased lactate utilization in the mitochondria. These coordinated actions of metformin in the intestine and liver improve hyperglycemia in diabetes and obesity. - Source: PubMed
Publication date: 2026/08/05
He LingAn HongyingRamirez KarinaRadovick SallyWondisford Fredric E - Linn. contains abundant free phenolic (PEFP) and bound phenolic (PEBP), both of which have demonstrated potential antidiabetic activities. However, their comparative hypoglycemic effects and underlying mechanisms remain unclear. This study investigated the effects of PEFP and PEBP using insulin-resistant HepG2 (IR-HepG2) cells and a high-fat diet/streptozotocin (HFD/STZ)-induced type 2 diabetes mellitus (T2DM) mouse model. PEFP and PEBP showed no cytotoxicity toward HepG2 cells and significantly enhanced glucose consumption, glycogen synthesis, and hexokinase and pyruvate kinase activities in IR-HepG2 cells. Treatment with 160 μg mL PEFP and PEBP increased glucose consumption in IR-HepG2 cells to 7.13 ± 0.30 and 6.73 ± 0.37 mmol L, respectively, restoring levels comparable to control cells (7.23 ± 0.69 mmol L). In HFD/STZ-induced T2DM mice, PEFP and PEBP significantly improved glucose homeostasis, insulin sensitivity, dyslipidemia, oxidative stress, and inflammatory responses after 10 weeks of intervention. High-dose PEFP and PEBP reduced fasting blood glucose from 13.02 ± 1.19 mmol L in diabetic mice to 7.47 ± 1.18 and 9.87 ± 0.93 mmol L, respectively. At the molecular level, both treatments were associated with upregulation of insulin signaling-related genes (, , , , and ) and suppression of gluconeogenic genes (, , and ) in the liver. Notably, distinct functional patterns were observed. PEFP, particularly at high doses, showed stronger associations with restoration of insulin signaling and inhibition of gluconeogenesis, whereas PEBP was more closely associated with glucose utilization and glycogen storage. In addition, PEFP and PEBP inhibited jejunal α-glucosidase and α-amylase activities and altered gut microbiota composition. These findings demonstrate that PEFP and PEBP exert multifaceted antidiabetic effects, which were closely associated with the modulation of hepatic insulin signaling-related gene expression, intestinal carbohydrate digestion, and gut microbiota composition, highlighting their potential as functional food ingredients for T2DM management. - Source: PubMed
Publication date: 2026/08/03
Xing MingxiaShen TingtingXie FanWu HaomingWang GuangqiangXia YongjunSong XinFu QiangqiangSheng YiAi Lianzhong - The endoplasmic reticulum glucose-6-phosphatase (G6Pase) system, traditionally linked to hepatic and renal glucose homeostasis, is increasingly recognized as a regulator of intracellular glucose-6-phosphate (G6P) partitioning with broad relevance to cancer biology. Emerging evidence implicates its catalytic subunits (G6PC1-3) and associated transporters, particularly SLC37A4/G6PT, in redox control, calcium homeostasis, protein quality control, glycogen metabolism, autophagy, epithelial-mesenchymal transition, stemness, immune evasion, and therapy resistance. In several non-gluconeogenic cancers, elevated G6Pase-system activity is associated with aggressive phenotypes, whereas in liver and kidney, G6PC loss promotes metabolic disruption and dedifferentiation. This Review highlights how ER-directed G6P flux, rather than glucose production itself, may shape tumour behaviour and reveal context-specific therapeutic vulnerabilities. Importantly, the clinical targeting of this system remains at an early, largely preclinical stage, and the therapeutic opportunities discussed here should be regarded as hypotheses to be tested rather than established interventions. - Source: PubMed
Publication date: 2026/07/17
Danalache Bogdan AlexandruFallah AbdallahMercier FrédéricAnnabi Borhane - Artificial dim light at night (dLAN) depresses nocturnal melatonin peak, along with disruption in sleep and metabolism. This study asked whether exogenous melatonin administration could reverse the effects of dim light at night on sleep and metabolism in a diurnal songbird. To answer this, three groups of zebra finches (Taeniopygia guttata) of both sexes (n=6/group/sex) hatched and raised in our indoor aviary were used. While a group remained on the dark night (LD control; 12L:12D, L=150 lux: D=0 lux), as before, to the other two groups the 12-h dark night was replaced with 5-lux (equivalent to 0.048 W/m²) dim light (12L:12dLAN; dLAN). Half an hour before dark onset, consecutively for the next 11 days, the birds of a dLAN group received subcutaneous injections of melatonin (10 µg/ 100 µl vehicle), while those of the other dLAN and LD groups (controls) received 100 µl vehicle alone. Exogenous melatonin mitigated dLAN-induced disruptive effects on both nocturnal sleep and metabolism. As compared to LD and vehicle-treated controls, melatonin-treated birds showed a significantly reduced nocturnal sleep frequency (fewer awakenings) and longer sleep bout as well as reduced night-time feeding and body fattening, and restoration of normal hepatic expression of genes associated with glucose and lipid metabolism. In particular, the elevated melatonin levels prevented the midnight increase in g6pc, irs1, fasn, star and egr1, and augmented the sirt1 mRNA levels under the dLAN environment. These results suggest that nocturnal melatonin levels are a crucial component of the regulatory pathways underlying nocturnal sleep and metabolism, independent of sex, in a diurnal songbird species. - Source: PubMed
Publication date: 2026/07/28
Buniyaadi AmaanKumar AshwaniBhardwaj Sanjay KumarKumar Vinod - Thioredoxin domain-containing protein 5 (TXNDC5) plays a role in diseases related to oxidative stress, energy metabolism, and cellular inflammation. This protein has also been associated with diabetes and insulin folding. To gain insight into these relationships, glucose metabolism was characterized using -deficient mice. The absence of TXNDC5 lowered glycemia, which was correlated with higher non-esterified fatty acid (NEFA) levels following an overnight fast on a chow diet in males. Several tolerance tests (pyruvate, glucose, and insulin) revealed no impairment in gluconeogenesis, but rather, higher insulin sensitivity. In vitro assays using an engineered hepatic cell line corroborated the results of increased glucose uptake. When a high-fat, high-sucrose diet was administered to induce a prediabetic state, the absence of TXNDC5 reproduced the lower glycemia and higher NEFA levels observed in mice consuming the chow diet. However, higher levels of plasma insulin were observed in -deficient mice. The insulin receptor was increased in the hepatic plasma membranes. Increased hepatic gene expression of , , and was also observed in the absence of TXNDC5. These results indicate that TXNDC5 plays a role in the hepatic sex-differential handling of glucose and lipids, and in retaining the insulin receptor on the plasma membrane. - Source: PubMed
Publication date: 2026/07/15
Sánchez-Marco JavierBarranquero CristinaMartínez-Beamonte RobertoSurra Joaquín CBidooki Seyed HesamoddinHerrera-Marcos Luis VRodríguez-Yoldi María-JesúsNavarro María ALopez-Yus MartaArbonés-Mainar Jose MOsada Jesús