Molecular and biochemical characterization of Tunisian patients with glycogen storage disease type III

• Published in: Journal of Human Genetics
• Main Authors: A. Mili, I. Ben Charfeddine, O. Mamai, W. Cherif, L. Adala, A. Amara, S. Pagliarani, S. Lucchiari, A. Ayadi, N. Tebib, A. Harbi, J. Bouguila, D. H'Mida, A. Saad, K. Limem, M. Gribaa, G. Comi
• Format: Article in Journal/Newspaper
• Language: English
• Published: 2012
• Subjects: amylo-1,6-glucosidase; AGL gene; glycogen storage disease type III; haplotype analysi; founder effect; novel mutation; Settore MED/26 - Neurologia; Faroe Islands
• Online Access: http://hdl.handle.net/2434/299188; https://doi.org/10.1038/jhg.2011.122

Glycogen storage disease type III (GSD III) is an autosomal recessive inborn error of metabolism caused by mutations in the glycogen debranching enzyme amylo-1,6-glucosidase gene, which is located on chromosome 1p21.2. GSD III is characterized by the storage of structurally abnormal glycogen, termed limit dextrin, in both skeletal and cardiac muscle and/or liver, with great variability in resultant organ dysfunction. The spectrum of AGL gene mutations in GSD III patients depends on ethnic group. The most prevalent mutations have been reported in the North African Jewish population and in an isolate such as the Faroe Islands. Here, we present the molecular and biochemical analyses of 22 Tunisian GSD III patients. Molecular analysis revealed three novel mutations: nonsense (Tyr1148X) and two deletions (3033_3036del AATT and 3216_3217del GA) and five known mutations: three nonsense (R864X, W1327X and W255X), a missense (R524H) and an acceptor splice-site mutation (IVS32-12A > G). Each mutation is associated to a specific haplotype.