[HTML][HTML] Functional significance of PMM2 mutations in mildly affected patients with congenital disorders of glycosylation Ia
V Westphal, S Peterson, M Patterson, A Tournay… - Genetics in …, 2001 - nature.com
V Westphal, S Peterson, M Patterson, A Tournay, A Blumenthal, EP Treacy, HH Freeze
Genetics in Medicine, 2001•nature.comPurpose: 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 …
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 …
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 as 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.
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