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Titolo:
Functional significance of PMM2 mutations in mildly affected patients withcongenital disorders of glycosylation Ia
Autore:
Westphal, V; Peterson, S; Patterson, M; Tournay, A; Blumenthal, A; Treacy, EP; Freeze, HH;
Indirizzi:
Burnham Inst, Glycobiol Program, La Jolla, CA 92037 USA Burnham Inst La Jolla CA USA 92037 cobiol Program, La Jolla, CA 92037 USA Neurol Inst, Dept Pediat Neurol, New York, NY 10032 USA Neurol Inst New York NY USA 10032 t Pediat Neurol, New York, NY 10032 USA Univ Calif Los Angeles, Los Angeles, CA USA Univ Calif Los Angeles Los Angeles CA USA s Angeles, Los Angeles, CA USA Montreal Childrens Hosp, Div Biochem & Med Genet, Montreal, PQ H3H 1P3, Canada Montreal Childrens Hosp Montreal PQ Canada H3H 1P3 al, PQ H3H 1P3, Canada McGill Univ, Dept Human Genet, Montreal, PQ, Canada McGill Univ Montreal PQ Canada v, Dept Human Genet, Montreal, PQ, Canada
Titolo Testata:
GENETICS IN MEDICINE
fascicolo: 6, volume: 3, anno: 2001,
pagine: 393 - 398
SICI:
1098-3600(200111/12)3:6<393:FSOPMI>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEFICIENT GLYCOPROTEIN SYNDROME; PHOSPHOMANNOSE ISOMERASE DEFICIENCY; SYNDROME TYPE 1A; ENDOPLASMIC-RETICULUM; CDG-IA; MANNOSE; YEAST; GENE; GLUCOSYLATION; SEC53;
Keywords:
congenital disorders of glycosylation; phosphomannomutase; genotype-phenotype; oligosaccharide;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Freeze, HH Burnham Inst, Glycobiol Program, 10901 N Torrey Pines Rd, La Jolla, CA 92037 USA Burnham Inst 10901 N Torrey Pines Rd La Jolla CA USA 92037 USA
Citazione:
V. Westphal et al., "Functional significance of PMM2 mutations in mildly affected patients withcongenital disorders of glycosylation Ia", GENET MED, 3(6), 2001, pp. 393-398

Abstract

Purpose: Congenital disorders of glycosylation (CDG) result from mutationsin N-glycan biosynthesis. Mutations in phosphomannomutase (PMM2) cause CDG-la. 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 severemutation 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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 19/10/17 alle ore 11:10:34