Aspartylglucosaminuria (AGU) is an inherited lysosomal storage disorder caused by the deficiency of aspartylglucosaminidase. We have earlier reported a single missense mutation (Cys163----Ser) to be responsible for 98% of the AGU alleles in the isolated Finnish population, which contains about 90% of the reported AGU patients. Here we describe the spectrum of 10 AGU mutations found in unrelated patients of non-Finnish origin. Since 11 out of 12 AGU patients were homozygotes, consanguinity has to be a common denominator in most AGU families. The mutations were distributed over the entire coding region of the aspartylglucosaminidase cDNA, except in the carboxyl-terminal 17-kDa subunit in which they were clustered within a 46-amino acid region. Based on the character of the mutations, most of them are prone to affect the folding and stability and not to directly affect the active site of the aspartylglucosaminidase enzyme.
Pubmed ID: 1722323 RIS Download
Mesh terms: Acetylglucosamine | Adolescent | Adult | Alleles | Aspartylglucosaminuria | Aspartylglucosylaminase | Base Sequence | Cell Line | Child | Child, Preschool | Chromosome Deletion | Codon | DNA | DNA Transposable Elements | Fibroblasts | Humans | Infant | Leukocytes | Molecular Sequence Data | Mutation | Oligodeoxyribonucleotides | Polymerase Chain Reaction | Polymorphism, Genetic | RNA | RNA Splicing
Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.