Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie
Autore:
Imbach, T; Schenk, B; Schollen, E; Burda, P; Stutz, A; Grunewald, S; Bailie, NM; King, MD; Jaeken, J; Matthijs, G; Berger, EG; Aebi, M; Hennet, T;
Indirizzi:
Univ Zurich, Inst Physiol, CH-8057 Zurich, Switzerland Univ Zurich Zurich Switzerland CH-8057 siol, CH-8057 Zurich, Switzerland Swiss Fed Inst Technol, Inst Microbiol, CH-8092 Zurich, Switzerland Swiss Fed Inst Technol Zurich Switzerland CH-8092 92 Zurich, Switzerland Catholic Univ Louvain, Ctr Human Genet, B-3000 Louvain, Belgium Catholic Univ Louvain Louvain Belgium B-3000 et, B-3000 Louvain, Belgium Childrens Hosp, Dept Neurol, Dublin 1, Ireland Childrens Hosp Dublin Ireland 1 ens Hosp, Dept Neurol, Dublin 1, Ireland Katholieke Univ Leuven Hosp, Dept Pediat, B-3000 Louvain, Belgium Katholieke Univ Leuven Hosp Louvain Belgium B-3000 3000 Louvain, Belgium
Titolo Testata:
JOURNAL OF CLINICAL INVESTIGATION
fascicolo: 2, volume: 105, anno: 2000,
pagine: 233 - 239
SICI:
0021-9738(200001)105:2<233:DODSCC>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOMANNOSE ISOMERASE DEFICIENCY; GLYCOPROTEIN SYNDROME; SACCHAROMYCES-CEREVISIAE; MAMMALIAN-CELLS; EXPRESSION; GENE; OLIGOSACCHARIDES; BIOSYNTHESIS; MUTATIONS; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
34
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., "Deficiency of dolichol-phosphate-mannose synthase-1 causes congenital disorder of glycosylation type Ie", J CLIN INV, 105(2), 2000, pp. 233-239

Abstract

Congenital disorders of glycosylation (CDG), formerly known as carbohydrate-deficient glycoprotein syndromes, lead to diseases with variable clinicalpictures. We report the delineation of a novel type of CDG identified in 2children presenting with severe developmental delay seizures, and dysmorphic features. We detected hypoglycosylation on serum transferrin and cerebrospinal fluid beta-trace protein. Lipid-linked oligosaccharides in the endoplasmic reticulum of patient fibroblasts showed an accumulation of the dolichyl pyrophosphate Man(5)GlcNAc(2) structure, compatible with the reduced dolichol-phosphate-mannose synthase (DolP-Man synthase) activity detected in these patients. Accordingly, 2 mutant alleles of the DolP-Man synthase DPM1gene, 1 with a 274C>G transversion, the other with a 628delC deletion, were detected in both siblings. Complementation analysis using DPM1-null murine Thy1-deficient cells confirmed the detrimental effect of both mutations on the enzymatic activity. Furthermore, mannose supplementation failed to improve the glycosylation status of DPM1-deficient fibroblast cells, thus precluding a possible therapeutic application of mannose in the patients. Because DPM1 deficiency, Like other subtypes of CDG-I, impairs the assembly of N-glycans, this novel glycosylation defect was named CDG-Ie.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 10:01:42