Glycogen storage disease type Ia in Argentina: two novel glucose-6-phosphatase mutations affecting protein stability
| Autor: | Chi Jiunn Pan, Raquel Dodelson de Kremer, Carlos E. Argaraña, Ana E. Paschini-Capra, Celia J. Angaroni, Janice Y. Chou, Roberto J. Pezza, Alicia N. Giner-Ayala |
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| Rok vydání: | 2004 |
| Předmět: |
Male
G6PC Endocrinology Diabetes and Metabolism Blotting Western DNA Mutational Analysis Argentina Mutation Missense Gene Expression Mutagenesis (molecular biology technique) Glycogen Storage Disease Type I Biochemistry Cricetulus Endocrinology Cricetinae Genetics Animals Humans Missense mutation Glycogen synthase Molecular Biology Gene DNA Primers chemistry.chemical_classification biology Molecular biology Phosphoric Monoester Hydrolases Transmembrane domain Enzyme chemistry COS Cells Glucose-6-Phosphatase Mutagenesis Site-Directed biology.protein Female Gene Deletion Glucose 6-phosphatase |
| Zdroj: | Molecular Genetics and Metabolism. 83:276-279 |
| ISSN: | 1096-7192 |
| DOI: | 10.1016/j.ymgme.2004.06.010 |
| Popis: | Glycogen storage disease type Ia (GSD-Ia) is caused by deleterious mutations in the glucose-6-phosphatase gene (G6PC). A molecular study of this gene was carried out in 11 Argentinean patients from 8 unrelated families. Four missense (p.Gln54Pro, p.Arg83Cys, p.Thr16Arg, and p.Tyr209Cys) and one deletion (c.79delC) mutations have been identified. Two novel mutations, p.Thr16Arg (c.47C > G) located within the amino-terminal domain and p.Tyr209Cys (c.626A > G) situated in the sixth transmembrane helix, were uncovered in this study. Site-directed mutagenesis and transient expression assays demonstrated that both p.Thr16Arg and p.Tyr209Cys mutations abolished enzymatic activity as well as reduced G6Pase stability. |
| Databáze: | OpenAIRE |
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