Identification of four novel PMM2 mutations in congenital disorders of glycosylation (CDG) Ia French patients

We screened 11 unrelated French patients with congenital disorders of glycosylation (CDG) Ia for PMM2 mutations. Twenty one missense mutations on the 22 chromosomes (95%) including four novel mutations were identified: C9Y (G26A) in exon 1, L32R (TA95GC) in exon 2, and T226S (C677G) and C241S (G722C...

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Bibliographic Details
Published in:Journal of medical genetics 2000-08, Vol.37 (8), p.579-580
Main Authors: VUILLAUMIER-BARROT, S, HETET, G, BARNIER, A, DUPRE, T, CUER, M, DE LONLAY, P, CORMIER-DAIRE, V, DURAND, G, GRANDCHAMP, B, SETA, N
Format: Article
Language:English
Subjects:
Biological and medical sciences
Carbohydrates (enzymatic deficiencies). Glycogenosis
Congenital Disorders of Glycosylation - etiology
Congenital Disorders of Glycosylation - genetics
Errors of metabolism
France
Humans
Medical sciences
Metabolic diseases
Mutation
Original
Phosphotransferases (Phosphomutases) - genetics
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Summary:We screened 11 unrelated French patients with congenital disorders of glycosylation (CDG) Ia for PMM2 mutations. Twenty one missense mutations on the 22 chromosomes (95%) including four novel mutations were identified: C9Y (G26A) in exon 1, L32R (TA95GC) in exon 2, and T226S (C677G) and C241S (G722C) in exon 8. We studied the PMM activity of these four novel mutant proteins and of the R141H mutant protein in an E coli expression system. The T226S, C9Y, L32R, and C241S mutant proteins have decreased specific activity (23 to 41% of normal), are all more or less thermolabile, and R141H has no detectable activity. Our results indicate that the new mutations identified here are less severe than the inactive R141H mutant protein, conferring residual PMM activity compatible with life.
ISSN:0022-2593
1468-6244
1468-6244
DOI:10.1136/jmg.37.8.579