Ask about this productRelated genes to: EPM2A antibody
- Gene:
- EPM2A NIH gene
- Name:
- EPM2A glucan phosphatase, laforin
- Previous symbol:
- -
- Synonyms:
- LDE, LD
- Chromosome:
- 6q24.3
- Locus Type:
- gene with protein product
- Date approved:
- 1998-10-01
- Date modifiied:
- 2019-01-25
Related products to: EPM2A antibody
Related articles to: EPM2A antibody
- Neuronatin (NNAT) is small transmembrane protein involved in a wide range of physiological processes, such as white adipose tissue browning and neuronal plasticity, as well as pathological ones, such as Lafora disease caused by the formation of NNAT aggregates. However, its 3D structure is unknown, and its mechanism of action is still unclear. In this study the two most well-known NNAT isoforms (α and β) were modelled and the interaction with the SERCA2b calcium pump was assessed using computational methods. First, molecular docking identified the same binding region as the one described for phospholamban, a thoroughly described SERCA inhibitor. Then, analyses of the flux of water molecules during molecular dynamics simulations highlighted significant similarities between the behavior of SERCA2b when in complex with phospholamban, and when in complex with either NNAT isoform. These results suggest that NNAT could be considered a "regulin-like" protein. Additional all-atom and coarse-grained simulations of multiple copies of NNAT highlighted a significant aggregation potential of both NNAT isoforms, supporting experimental data. - Source: PubMed
Publication date: 2026/04/09
Ben Mariem OmarCoppi LaraDe Fabiani EmmaEberini IvanoCrestani Maurizio - Lafora disease is a rare, autosomal recessive neurodegenerative disorder characterized by the progressive accumulation of abnormal, insoluble, and hyperphosphorylated forms of glycogen, known as Lafora bodies, in the brain and other tissues. The disease typically manifests during early adolescence with myoclonus, seizures, and rapidly progressive cognitive decline, ultimately leading to severe neurological deterioration and death within a decade of onset. Mutations in the EPM2A or EPM2B genes, which encode the proteins laforin and malin-key regulators of glycogen metabolism-are the underlying cause of Lafora disease. Current research focuses on understanding the molecular mechanisms of the disease and exploring potential therapeutic approaches, including gene therapy, antisense oligonucleotides, enzyme-based therapies, and pharmacological interventions aimed at mitigating glycogen accumulation and alleviating disease symptoms. Multiple mouse models have been generated to advance our understanding of disease pathogenesis and facilitate treatment development. These include models deficient in Epm2a or Epm2b gene expression, the Epm2a and Epm2b mouse models, and a knock-in mouse model harboring the most frequent mutation in the Epm2a gene, the R240X mutation. Recently, we developed two new knock-in mouse models with Epm2b gene mutations. In this work, we describe the generation and characterization of these malin knock-in mice and compare their phenotype with Epm2b mice. These new models exhibit distinct neurological alterations, including motor and cognitive impairments, epileptic-like activity and altered synaptic plasticity. Based on these results, they can serve as valuable models for studying specific aspects of Lafora disease, providing more suitable tools for future research. - Source: PubMed
Publication date: 2026/04/03
Iglesias-Cabeza NereaZafra-Puerta LuisWorby Carolyn AFernández-Burgos DanielSciaccaluga MiriamImperatore ValentinaFermont LéaSánchez-Martín GemaSharmistha MitraGentry Matthew SCosta CinziaSerratosa José MSánchez Marina P - Lafora disease is a fatal and progressive neurodegenerative disorder characterized by the accumulation of insoluble polyglucosan inclusions, known as Lafora bodies, due to impaired glycogen metabolism. Therapeutic strategies aimed at reducing intracellular glycogen accumulation represent a promising approach to mitigating disease progression. This study aimed to evaluate the feasibility of promoting Lafora body degradation by increasing the protein levels of human pancreatic amylase, a glycogen-degrading enzyme, through the SINEUP approach. Two SINEUP constructs specifically targeting human pancreatic amylase were designed and tested in continuous tumor-derived cell lines of central nervous system origin, as well as in primary fibroblasts obtained from a patient with Lafora disease. Human pancreatic amylase protein and mRNA levels were assessed to determine the specificity of SINEUP-mediated regulation. Enzymatic activity assays were performed to evaluate functional protein upregulation, and intracellular glycogen content was measured in patient-derived fibroblasts. Both SINEUP constructs significantly increased human pancreatic amylase protein expression without affecting mRNA levels, confirming a post-transcriptional mechanism of action. The elevated protein levels were associated with a significant increase in enzymatic activity. In primary fibroblasts derived from a Lafora disease patient, enhanced amylase expression correlated with a marked reduction in intracellular glycogen content. These findings provide proof of concept that SINEUP-mediated upregulation of glycogen-degrading enzymes may represent a viable therapeutic strategy to counteract Lafora body accumulation. Further studies are warranted to assess the efficacy, safety, and translational potential of this approach, particularly in relevant animal models of Lafora disease. - Source: PubMed
Publication date: 2026/03/16
Allegri LorenzoBaldan FedericaMio CatiaImperatore ValentinaCosta CinziaProntera PaoloBisulli FrancescaMuccioli LorenzoDamante Giuseppe - To explore the novel mutations associated with asthma in core family lines of Han Chinese children by using GWAS and transmission disequilibrium test. - Source: PubMed
Publication date: 2026/03/17
Su XingyueWang BeileiWei XiaolingXue MinWang JingLiu GuohuaMa Xiang - - Source: PubMed
Publication date: 2026/03/15
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