Publications by authors named "E Pellier"
Glycogen storage disease type III (GSDIII) is an autosomal recessive disorder characterized by a deficiency of glycogen debranching enzyme (GDE) leading to cytosolic glycogen accumulation and inducing liver and muscle pathology. Skin fibroblasts from three GSDIII patients were reprogrammed into induced pluripotent stem cells (iPSCs) using non-integrated Sendai virus. All of the three lines exhibited normal morphology, expression of pluripotent markers, stable karyotype, potential of trilineage differentiation and absence of GDE expression, making them valuable tools for modeling GSDIII disease in vitro, studying pathological mechanisms and investigating potential treatments.
View Article and Find Full Text PDFGlycogen storage disease type III (GSDIII) is a rare genetic disease caused by mutations in the gene encoding the glycogen debranching enzyme (GDE). The deficiency of this enzyme, involved in cytosolic glycogen degradation, leads to pathological glycogen accumulation in liver, skeletal muscles and heart. Although the disease manifests with hypoglycemia and liver metabolism impairment, the progressive myopathy is the major disease burden in adult GSDIII patients, without any curative treatment currently available.
View Article and Find Full Text PDFLimb girdle muscular dystrophies (LGMD), caused by mutations in 29 different genes, are the fourth most prevalent group of genetic muscle diseases. Although the link between LGMD and its genetic origins has been determined, LGMD still represent an unmet medical need. Here, we describe a platform for modeling LGMD based on the use of human induced pluripotent stem cells (hiPSC).
View Article and Find Full Text PDFArticle Synopsis
- - Limb-girdle muscular dystrophy type R3 (LGMD R3) is a genetic disorder resulting from mutations in the alpha-sarcoglycan (α-SG) gene, leading to muscle weakness.
- - Researchers conducted a study to find drugs that enhance the effectiveness of the proteasome inhibitor bortezomib in degrading the misfolded R77C-α-SG protein, identifying the HDAC inhibitor givinostat as a promising candidate.
- - Givinostat's therapeutic action appears to inhibit the autophagic pathway, suggesting new insights into how misfolded SG proteins are degraded and indicating potential for treating other diseases with similar degradation issues.
Article Synopsis
- Cell organization relies on the interaction between cytoskeletal systems and organelles, with GBF1 and Arf1 playing key roles in golgi and mitochondrial structure.
- Research reveals that GBF1 and Arf1 also help regulate the positioning of mitochondria through microtubules, involving a protein called Miro.
- Inhibition of GBF1 or Arf1 causes mitochondria to cluster towards the centrosome, leading to changes in their shape and movement patterns, highlighting the coordinated transport mechanisms essential for cellular organization.