Ask about this productRelated genes to: PGM1 antibody
- Gene:
- PGM1 NIH gene
- Name:
- phosphoglucomutase 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 1p31.3
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-05
Related products to: PGM1 antibody
Related articles to: PGM1 antibody
- This case report expands the limited literature on phosphoglucomutase-1 deficiency (GSD XIV), a rare disorder that combines features of glycogen storage disease and congenital disorders of glycosylation. Given its wide clinical spectrum and often subtle early signs, under-recognition remains common. We report this case to highlight its multisystem involvement, emphasize diagnostic challenges, and reinforce the need for early consideration of GSD XIV in patients with unexplained hepatic, metabolic, and neuromuscular abnormalities. - Source: PubMed
Publication date: 2026/09/09
Al Dojan Khalid AdelSulaiman Samia AzizAlaarag Abdallah - Type 2 diabetes mellitus (T2DM) is a metabolic disorder characterized by glycolipid dysregulation and hepatic steatosis. Centella asiatica (CA) and its triterpenoid constituents exert metabolic benefits. In addition, previous metabolomics study found that asiatic acid regulated pyrimidine metabolism in obese mice, while the key target and pathway were undefined. This study investigated the regulatory effects of CA and its active constituents on T2DM-related glycolipid disorders, focusing on the pyrimidine metabolism pathway. T2DM mice were established using a high-fat diet combined with streptozotocin (STZ) and treated with Centella asiatica ethanolic extract or asiatic acid (AA), with glibenclamide as a positive control. Then, glycolipid metabolism, hepatic function, pyrimidine metabolites, and related mechanisms were assessed using biochemical assays, LC-MS/MS, cellular experiments, molecular analyses, and molecular docking. CAE and AA significantly reduced FBG (decreased by 51.01% and 53.01%), improved glucose intolerance, corrected dyslipidemia, alleviated hepatic steatosis, and attenuated insulin resistance in T2DM mice. They elevated hepatic uridine, cytidine, and UDP-glucose (UDPG) levels, promoted glycogen synthesis, inhibited uridine phosphorylase 1 (UPP1) activity, upregulated UDPG synthesis genes (PGM1, UGP2), and downregulated lipogenic genes (ACACA, Fasn, SREBP1/2). Molecular docking indicated specific binding of AA and asiaticoside to UPP1. This work distinguishes from our prior research by identifying UPP1 as a functional target and elucidating the detailed molecular mechanism. CA improves T2DM-associated glycolipid disorders and hepatic injury by modulating the pyrimidine metabolism-UDPG-glycogen synthesis pathway and targeting UPP1, highlighting its therapeutic potential for metabolic diseases. - Source: PubMed
Publication date: 2026/06/27
Shen YunjiaoYao YuanyuanLiu ZhihuiLi YiCao ShijieFeng Xinchi - The impact of the metabolic microenvironment on epigenetically plastic cancer cells underpins phenotypic heterogeneity, a major cause of metastasis and therapy resistance. Nutrient limitation is a key microenvironmental stress, and can cause cells to transition from proliferative to invasive phenotypes, however, whether cancer cells have the capacity to delay phenotype switching remains unknown. Here, using melanoma as a model, we reveal that the ability to buffer glucose availability by accumulating and mobilizing glycogen can determine cancer cell phenotypic transitions. While proliferating cells contain high levels of glycogen, invasive cells are marked by depleted glycogen stores. Accordingly, the inability to store and metabolize glycogen leads to phenotype instability and a switch from proliferation to invasion. The amount of stored glycogen inversely correlates with tissue invasion depth in primary melanomas, and reduced expression of the glycogen phosphorylases PYGB/L and phosphoglucomutase 1 (PGM1) is associated with worse patient survival. Together, we identify metabolic glucose buffering as a determinant of invasive phenotype transitions in skin cancer, suggesting similar paradigms in other cancer types. - Source: PubMed
Publication date: 2026/07/15
Ramírez-Sánchez AnaJociles-Ortega MiguelGarcía-Martínez José ManuelTorrens-Martínez IreneMartínez-Useros JavierLouphrasitthiphol PakavarinSweeney Mollie IMorente-Carrasco AnaRuiz-Reyes SergioRedondo-Díaz NereaOlmos-De Blas TeresaFernández-Aceñero María JesúsRodriguez-López José NSoga TomoyoshiWhite Richard MGoding Colin RSanchez-Del-Campo LuisGarcía-Jiménez CustodiaChocarro-Calvo Ana - This study explored the effects of dietary riboflavin supplementation on breast meat quality, muscle fiber characteristics, metabonomics, transcriptomics, and phosphoproteomics of Pekin ducks. A total of 96 14-day-old ducks were randomly allotted to two treatment groups, each with 8 replicates of 6 birds, and were fed diets supplemented with 0 or 10 mg/kg riboflavin for 28 days. Compared to the control group without riboflavin supplementation, dietary riboflavin supplementation significantly increased breast muscle shear force, myofiber diameter, perimeter, and cross-sectional area, as well as myofibril diameter. Dietary riboflavin supplementation increased gene expression involved in myogenic differentiation of breast muscle in Pekin ducks, including MYOD, MRF4, and MYF5. Breast muscle metabolomics revealed that riboflavin stimulated fatty acid beta oxidation, as most carnitine-related metabolites were upregulated. Transcriptomics analysis revealed that riboflavin upregulated seven genes involved in muscle contraction (MYO3A, MYO5B, MYH11, MYBPC1, TNNI1, TNNT2, A2M), and ten genes involved in fatty acid synthesis, oxidation, and transport processes, which may contribute to enhanced intramuscular fat content. Furthermore, phosphoproteomics analysis indicated dietary riboflavin supplementation altered the phosphorylation levels of proteins involved in muscle contraction and glycolysis (PGM1, ENO1, and TPI1), which may lead to an increase in pH. In conclusion, riboflavin supplementation in the diet improved the breast meat quality and fiber development of ducks probably by activating fatty acid beta oxidation, synthesis, and transport, as well as muscle contraction, while simultaneously depressing glycolysis process. - Source: PubMed
Publication date: 2026/06/22
Wu QingyiShao QingZhou WeiZhuang LeiJin YongyanZhou ZhengkuiXie MingHou ShuishengTang Jing - The phosphoglucomutase 1 (PGM1) enzyme plays a critical role in metabolism and glycosylation in the human body. PGM1 has been linked to multiple disease phenotypes, including the inherited metabolic disorder known as congenital disorders of glycosylation (CDGs). Numerous clinical studies have shown that mutations in key regions of the PGM1 gene affect catalytic activity and induce folding defects of the enzyme. To delve into molecular changes at the supramolecular level, the structural, stability, and other features of PGM1 variants (T19A, N38Y, and D62H) were studied in the present work. To this end, molecular dynamics (MD) simulation at a long timescale (500 ns) was carried out. Parameters such as root-mean-square deviation (RMSD), root-mean-square fluctuations (RMSF), radius of gyration (Rg), solvent-accessible surface area (SASA), hydrogen bonds, and free energy landscape (FEL) were studied and compared with those of the wild-type PGM1. It was noted that mutations 19 A, N38Y, and D62H significantly alter the protein's structural behavior, causing increased flexibility, reduced stability, and compactness. - Source: PubMed
Publication date: 2026/07/07
Abdullah Almuqri Eman