Abstract
Purpose: Congenital disorders of glycosylation (CDG) result from mutations in N-glycan biosynthesis. Mutations in phosphomannomutase (PMM2) cause CDG-Ia. Here, we report four clinically mild patients and their mutations in PMM2. Methods: Analysis of the PMM2 cDNA and gene revealed the mutations affecting the glycosylation efficiency. Results: The patients have 30% to 50% normal PMM activity in fibroblasts due to different mutations in PMM2, and we studied the effect of each mutation on the PMM activity in a Saccharomyces cerevisiae expression system. Conclusions: Each patient carried a severe mutation that decreased the PMM activity to less than 10% as well a relatively mild mutation. A new mutation, deletion of base 24, changed the reading frame. The C9Y, C241S, and L32R mutations showed 27% to 45% activity when expressed in the eukaryotic expression system, and the more severe D148N was shown to be thermolabile.
Original language | English (US) |
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Pages (from-to) | 393-398 |
Number of pages | 6 |
Journal | Genetics in Medicine |
Volume | 3 |
Issue number | 6 |
DOIs | |
State | Published - 2001 |
Keywords
- Congenital disorders of glycosylation
- Genotype-phenotype
- Oligosaccharide
- Phosphomannomutase
ASJC Scopus subject areas
- Genetics(clinical)