Ask about this productRelated genes to: PYGM antibody
- Gene:
- PYGM NIH gene
- Name:
- glycogen phosphorylase, muscle associated
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 11q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-13
Related products to: PYGM antibody
Related articles to: PYGM antibody
- The association of perturbed skeletal muscle metabolism with ICU acquired weakness (ICUAW) is not clear. The objective of the present study was to characterise temporal changes in skeletal muscle mitochondrial function, ATP concentration, and substrate utilisation during and up to 6 months post ICU admission in critically ill patients, and to delineate mechanisms underpinning ICUAW by comparing the expression of genes involved in skeletal muscle mitochondrial function and substrate utilisation in the critically ill patients to control groups that had either undergone elective surgery or leg immobilisation (i.e. muscle disuse). The study design was a randomised controlled trial of functional electrical stimulation-assisted cycle ergometry (FESCE) vs. standard care, with skeletal muscle mitochondrial respirometry defined in a nested sub-group of patients as the primary outcome. Mitochondrial respirometry did not change 7 days or 6 months after ICU admission and was not impacted by FESCE. However, a 20% reduction in muscle ATP content by day 7 of ICU stay persisted after 6 months and tended to associate with ICUAW (=0.078, R=0.582). Moreover, a 40% lower muscle glycogen and 2.5-fold greater muscle lactate were observed earlier at day 1 compared to elective surgery patients. These changes reflected expression of genes related to glycogen metabolism when disuse was accounted for, and of which a greater expression of the gene encoding glycogen phosphorylase (PYGM) was predictive of mortality. We conclude that muscle glycogen metabolism is rapidly dysregulated in critical illness, which may have implications for muscle ATP resynthesis and ICUAW. - Source: PubMed
Publication date: 2026/04/29
Jameson Tom S OWall Benjamin TUrban TomášKrajčová AdélaBakalář BobFric MichalJiroutková KateřinaDžupa ValérGojda JanPorter CraigMiznerová BarboraDuška FrantišekStephens Francis B - McArdle disease (McA) is a rare metabolic disorder of autosomal recessive inheritance caused by pathogenic variants in the PYGM gene, which lead to a deficiency of the myophosphorylase enzyme. This enzymatic defect impairs muscle glycogenolysis, typically resulting in exercise intolerance, premature fatigue, and exertional cramps triggered by anaerobic or high-intensity physical activity starting in childhood or adolescence. However, the diagnosis is frequently delayed due to the heterogeneous and non-specific presentation of these symptoms. The authors report a case of a 61-year-old woman with a lifelong history of exercise intolerance and disproportionate muscle fatigue that restricted her physical activity since her youth. She presented with persistent, idiopathic elevations of creatine kinase (CK) over several years. The patient had no history of myoglobinuria and showed preserved renal function and no evidence of acute rhabdomyolysis, despite marked hyperCKemia. Cardiac involvement was also excluded. After excluding more common secondary causes of hyperCKemia, such as statin-induced myopathy and inflammatory conditions, the persistence of marked hyperCKemia and specific exercise-induced symptoms suggested a metabolic myopathy, such as McArdle disease. Molecular analysis was performed, identifying the homozygous pathogenic variant c.280C>T (p.Arg94Trp) in the PYGM gene and confirming the diagnosis of McArdle disease. - Source: PubMed
Publication date: 2026/02/10
Valente LeandroSantos GabrielleVelho RicardoSantos José FilipeDuarte OdeteCorreia Lurdes - Persistent toe walking (TW) in children is often idiopathic but may conceal subtle neuromuscular or metabolic causes. This cross-sectional, retrospective study investigated clinical and genetic characteristics of children carrying PYGM variants to explore potential subclinical phenotypes among heterozygous carriers. - Source: PubMed
Pomarino DavidFregien BastianRostásy Kevin M - Hepatic steatosis is the most prevalent and earliest pathological change in alcoholic hepatitis and represents a critical initiating event in alcohol-associated liver disease (ALD). However, the molecular mechanisms underlying alcohol-induced hepatic lipid dysregulation remain incompletely understood. Here, we investigated the role of glutathione S-transferase Mu 3 (GSTM3) in hepatic lipid metabolism during ALD and explored its underlying mechanism. Using an ALD mouse model and ethanol (EtOH)-treated AML-12 cells, we examined the functional interaction between GSTM3 and glycogen phosphorylase, muscle associated (PYGM), which was identified as a downstream candidate through RNA sequencing (RNA-seq). We found that GSTM3 expression was markedly upregulated in primary hepatocytes isolated from ALD mice and EtOH-treated AML-12 cells, whereas GSTM3 deficiency significantly exacerbated hepatic lipid accumulation both in vivo and in vitro. Mechanistically, GSTM3 knockdown resulted in increased PYGM expression at both the mRNA and protein levels. Importantly, rescue experiments revealed that concomitant silencing of PYGM partially alleviated the enhanced lipid accumulation induced by GSTM3 deficiency, indicating that PYGM contributes to the steatotic phenotype downstream of GSTM3 loss. Collectively, these findings identify GSTM3 as a critical protective regulator of alcohol-induced hepatic steatosis and reveal a previously unrecognized GSTM3-PYGM axis that modulates lipid metabolism in ALD, suggesting GSTM3 as a potential therapeutic target for the treatment of ALD. - Source: PubMed
Publication date: 2026/02/20
Xia RanWang LuZhao Chen-ChenZhao Yu-XinLv Jun-JieYang Rui-FengZhang Yi-YinLei YuWei WeiSun Ying-Yin - Tauopathies are characterized by hyperphosphorylated tau accumulation and neurodegeneration. Although astrocytic metabolism is known to support neuronal health, the role of astrocytic glycogen metabolism, particularly the glycogenolytic enzyme PYGM (glycogen phosphorylase, muscle associated), in tauopathies remains unclear. - Source: PubMed
Cao JingMeng JianChen YiqingTang ZiqianWang YongLi KunZhang XianLuo HongLi HuihuiWang ZhanxiangZhang Yun-Wu