ArticleThe American journal of pathology2000
Reduced heparan sulfate accumulation in enterocytes contributes to protein-losing enteropathy in a congenital disorder of glycosylation.
Article in The American journal of pathology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 98 citations in OpenAlex.
- ALG8-CDG: Molecular and phenotypic expansion suggests clinical management guidelines.Journal of inherited metabolic disease · 2022Article
- Acetazolamide treatment in late onset CDG type 1 due to biallelic pathogenic DHDDS variants.Molecular genetics and metabolism reports · 2022Article
- Nutrition interventions in congenital disorders of glycosylation.Trends in molecular medicine · 2022Review
- The role of albumin and the extracellular matrix on the pathophysiology of oedema formation in severe malnutrition.EBioMedicine · 2022Article
- The Challenge of Modulating Heparan Sulfate Turnover by Multitarget Heparin Derivatives.Molecules (Basel, Switzerland) · 2020Review
- Comparative pathophysiology and management of protein-losing enteropathy.Journal of veterinary internal medicine · 2019Review
- Article
- ALG6-CDG: a recognizable phenotype with epilepsy, proximal muscle weakness, ataxia and behavioral and limb anomalies.Journal of inherited metabolic disease · 2016Article
- Clinical Approaches to the Patient with a Failing Fontan Procedure.Current cardiology reports · 2016Review
- Reduced expression of the oligosaccharyltransferase exacerbates protein hypoglycosylation in cells lacking the fully assembled oligosaccharide donor.Glycobiology · 2015Article
- Clinical utility gene card for: ALG6 defective congenital disorder of glycosylation.European journal of human genetics : EJHG · 2015Article
- Central role of the gut epithelial barrier in the pathogenesis of chronic intestinal inflammation: lessons learned from animal models and human genetics.Frontiers in immunology · 2013Review
- Article
- Fibrotic response in fibroblasts from congenital disorders of glycosylation.Journal of cellular and molecular medicine · 2011Article
- Heparan sulfate proteoglycans.Cold Spring Harbor perspectives in biology · 2011Review
- Analysis of interactions of Salmonella type three secretion mutants with 3-D intestinal epithelial cells.PloS one · 2010Article
- Glycosylation diseases: quo vadis?Biochimica et biophysica acta · 2009Review
- Heparan sulfate and syndecan-1 are essential in maintaining murine and human intestinal epithelial barrier function.The Journal of clinical investigation · 2008Article
- New disorders in carbohydrate metabolism: congenital disorders of glycosylation and their impact on the endocrine system.Reviews in endocrine & metabolic disorders · 2003Review
- Review
Corrections and comments
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Authors and funding
7 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
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 a congenital 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, T391C (Y131H) and C924A (S308R) have not previously been reported. The mutations were 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.
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