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Titolo:
Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation
Autore:
Westphal, V; Murch, S; Kim, S; Srikrishna, G; Winchester, B; Day, R; Freeze, HH;
Indirizzi:
Burnham Inst, La Jolla, CA 92037 USA Burnham Inst La Jolla CA USA 92037Burnham Inst, La Jolla, CA 92037 USA Univ London, Royal Free & Univ Coll Sch Med, Dept Paediat Gastroenterol, London, England Univ London London England Dept Paediat Gastroenterol, London, England Univ Coll London, Inst Child Hlth, London, England Univ Coll London London England ondon, Inst Child Hlth, London, England St Marks Hosp, Harrow, Middx, England St Marks Hosp Harrow Middx EnglandSt Marks Hosp, Harrow, Middx, England
Titolo Testata:
AMERICAN JOURNAL OF PATHOLOGY
fascicolo: 6, volume: 157, anno: 2000,
pagine: 1917 - 1925
SICI:
0002-9440(200012)157:6<1917:RHSAIE>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEFICIENT GLYCOPROTEIN SYNDROME; SYNDROME TYPE-I; PHOSPHOMANNOSE ISOMERASE DEFICIENCY; GLOMERULAR BASEMENT-MEMBRANE; N-LINKED GLYCOSYLATION; QUALITY-CONTROL; BINDING GLOBULIN; MOLECULAR-BASIS; SURFACE-CHARGE; FED RATS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Clinical Medicine
Life Sciences
Citazioni:
50
Recensione:
Indirizzi per estratti:
Indirizzo: Freeze, HH Burnham Inst, 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., "Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation", AM J PATH, 157(6), 2000, pp. 1917-1925

Abstract

intestinal biopsy in a boy with gastroenteritis-induced protein-losing enteropathy (PLE) showed loss of heparan sulfate (HS) and syndecan-1 core protein from the basolateral surface of the enterocytes, which improved after PLE subsided. Isoelectric focusing analysis of serum transferrin indicated acongenital disorder of glycosylation (CDG) and subsequent analysis showed three point mutations in the ALG6 gene encoding an alpha1,3-glucosyltransferase needed. for the addition of the first glucose to the dolichol-linked oligosaccharide. The maternal mutation, C998T, causing an A333V substitution, has been shown to cause CDG-Ic, whereas the two paternal mutations, TS91C(Y131H) and C924A (S308R) have not previously been reported. The mutationswere tested for their ability to rescue faulty N-linked glycosylation of carboxypeptidase Y in an ALG6-deficient Saccharomyces cerevisiae strain. Normal human ALG6 rescues glycosylation and A333V partially rescues, whereas the combined paternal mutations (Y131H and S308R) are ineffective. Underglycosylation resulting from each of these mutations is much more severe in rapidly dividing yeast, Similarly, incomplete protein glycosylation in the patient is most severe in rapidly dividing enterocytes during gastroenteritis-induced stress. Incomplete N-linked glycosylation of an HS core protein and/or other biosynthetic enzymes may explain the selective localized loss of HS and PLE.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 24/09/20 alle ore 05:11:16