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Titolo:
Carbohydrate-deficient glycoprotein syndrome type II
Autore:
Schachter, H; Jaeken, J;
Indirizzi:
Univ Toronto, Sch Med, Dept Biochem, Toronto, ON M5G 1X8, Canada Univ Toronto Toronto ON Canada M5G 1X8 ochem, Toronto, ON M5G 1X8, Canada Hosp Sick Children, Dept Struct Biol & Biochem, Toronto, ON M5G 1X8, Canada Hosp Sick Children Toronto ON Canada M5G 1X8 Toronto, ON M5G 1X8, Canada Katholieke Univ Leuven, Ctr Metab Dis, Louvain, Belgium Katholieke Univ Leuven Louvain Belgium Ctr Metab Dis, Louvain, Belgium
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR BASIS OF DISEASE
fascicolo: 2-3, volume: 1455, anno: 1999,
pagine: 179 - 192
SICI:
0925-4439(19991008)1455:2-3<179:CGSTI>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
UDP-N-ACETYLGLUCOSAMINE; ASPARAGINE-LINKED OLIGOSACCHARIDES; LEUKOCYTE ADHESION DEFICIENCY; PHOSPHOMANNOSE ISOMERASE DEFICIENCY; LYSOSOMAL-ENZYME N-ACETYLGLUCOSAMINE-1-PHOSPHOTRANSFERASE; MAGNETIC-RESONANCE SPECTROSCOPY; AUTOSOMAL RECESSIVE DISEASE; ALPHA-MANNOSIDASE-II; ANEMIA TYPE-II; SERUM TRANSFERRIN;
Keywords:
carbohydrate-deficient glycoprotein; N-acetylglucosaminyltransferase; N-glycan synthesis; Golgi; transferrin glycoform; psychomotor retardation;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
125
Recensione:
Indirizzi per estratti:
Indirizzo: Schachter, H Univ Toronto, Sch Med, Dept Biochem, 555 Univ Ave, Toronto, ON M5G 1X8, Canada Univ Toronto 555 Univ Ave Toronto ON Canada M5G 1X8 8, Canada
Citazione:
H. Schachter e J. Jaeken, "Carbohydrate-deficient glycoprotein syndrome type II", BBA-MOL BAS, 1455(2-3), 1999, pp. 179-192

Abstract

The carbohydrate-deficient glycoprotein syndromes (CDGS) are a group of autosomal recessive multisystemic diseases characterized by defective glycosylation of N-glycans. This review describes recent findings on two patients with CDGS type II. In contrast to CDGS type I, the type II patients show a more severe psychomotor retardation, no peripheral neuropathy and a normal cerebellum. The CDGS type II serum transferrin isoelectric focusing patternshows a large amount (95%) of disialotransferrin in which each of the two glycosylation sites is occupied by a truncated monosialo-monoantennary N-glycan. Fine structure analysis of this glycan suggested a defect in the Golgi enzyme UDP-GlcNAc:alpha-6-D-mannoside beta-1,2-N-acetylglucosaminyltransferase II (GnT II; EC 2.4.1.143) which catalyzes an essential step in the biosynthetic pathway leading from hybrid to complex N-glycans. GnT LT activity is reduced by over 98% in fibroblast and mononuclear cell extracts from the CDGS type II patients. Direct sequencing of the GnT II coding region from the two patients identified two point mutations in the catalytic domain of GnT LT, S290F (TCC to TTC) and H262R (CAC to CGC). Either of these mutations inactivates the enzyme and probably also causes reduced expression. TheCDG syndromes and other congenital defects in glycan synthesis as well as studies of null mutations in the mouse provide strong evidence that the glycan moieties of glycoproteins play essential roles in the normal development and physiology of mammals and probably of all multicellular organisms. (C) 1999 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 10:28:45