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Titolo:
Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic
Autore:
Imbach, T; Grunewald, S; Schenk, B; Burda, P; Schollen, E; Wevers, RA; Jaeken, J; de Klerk, JBC; Berger, EG; Matthijs, G; Aebi, M; Hennet, T;
Indirizzi:
Univ Zurich, Inst Physiol, CH-8057 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8057 siol, CH-8057 Zurich, Switzerland Ctr Human Genet, B-3000 Louvain, Belgium Ctr Human Genet Louvain BelgiumB-3000 an Genet, B-3000 Louvain, Belgium Swiss Fed Inst Technol, Inst Microbiol, CH-8092 Zurich, Switzerland Swiss Fed Inst Technol Zurich Switzerland CH-8092 92 Zurich, Switzerland Acad Hosp Nijmegen, Lab Neurol, NL-6525 GC Nijmegen, Netherlands Acad HospNijmegen Nijmegen Netherlands NL-6525 GC Nijmegen, Netherlands Dept Pediat, B-3000 Louvain, Belgium Dept Pediat Louvain Belgium B-3000Dept Pediat, B-3000 Louvain, Belgium Sophia Childrens Hosp, Dept Pediat, Rotterdam, Netherlands Sophia Childrens Hosp Rotterdam Netherlands iat, Rotterdam, Netherlands
Titolo Testata:
HUMAN GENETICS
fascicolo: 5, volume: 106, anno: 2000,
pagine: 538 - 545
SICI:
0340-6717(200005)106:5<538:MOOCDO>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEFICIENT GLYCOPROTEIN SYNDROME; PHOSPHOMANNOSE ISOMERASE DEFICIENCY; LIPID-LINKED OLIGOSACCHARIDE; SACCHAROMYCES-CEREVISIAE; ENDOPLASMIC-RETICULUM; GENE; GLUCOSYLATION; MUTATIONS; GLUCOSYLTRANSFERASE; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Hennet, T Univ Zurich, Inst Physiol, Winterthurerstr 190, CH-8057 Zurich, Switzerland Univ Zurich Winterthurerstr 190 Zurich Switzerland CH-8057 land
Citazione:
T. Imbach et al., "Multi-allelic origin of congenital disorder of glycosylation (CDG)-Ic", HUM GENET, 106(5), 2000, pp. 538-545

Abstract

Congenital disorders of glycosylation (CDG), formerly known as carbohydrate-deficient glycoprotein syndrome, represent a family of genetic diseases with variable clinical presentations. Common to all types of CDG characterized to date is a defective Asn-linked glycosylation caused by enzymatic defects of N-glycan synthesis. Previously, we have identified a mutation in theALG6 alpha 1,3 glucosyltransferase gene as the cause of CDG-Ic in four related patients. Here, we present the identification of seven additional cases of CDG-Ic among a group of 35 untyped CDG patients. Analysis of lipid-linked oligosaccharides in fibroblasts confirmed the accumulation of dolichyl pyrophosphate-Man(9)GlcNAc(2) in the CDG-Ic patients. The genomic organization of the human ALG6 gene was determined, revealing 14 exons spread over 55 kb. By polymerase chain reaction amplification and sequencing of ALG6 exons, three mutations, in addition to the previously described A333 V substitution, were detected in CDG-Ic patients. The detrimental effect of these mutations on ALG6 activity was confirmed by complementation of alg6 yeast mutants, Haplotype analysis of CDG-Ic patients revealed a founder effect for the ALG6 allele bearing the A333 V mutation. Although more than 80% of CDG are type Ia, CDO-Ic may be the second most common form of the disease.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 08:46:10