The contribution of glycosylation deficiency to liver pathology – an example of congenital disorders of glycosylation (CDG), galactosemia and fructosemia Maciej Adamowicz, Piotr Socha Medical Science Review - Hepatologia 2008; 8 63-71 aaICID: 862348
Article type: Review article
IC™ Value: 3.01
Abstract provided by Publisher
Glycosylation is a common modification of proteins. Sugar glycans attached to protein by N- or O-glycoside bond are responsible for many important functions of plasma, cell membrane, connective tissue and other glycoproteins. Deficit of glycosylation characterizes the group of inborn errors of metabolism named congenital disorders of glycosylation (CDG). The defects of N-glycan biosynthesis localized in different subcellular compartments within the group of 21 CDG variants, constitute the basis of complex clinical picture with prevalence of multiorgan symptoms and abnormalities of numerous laboratory parameters. The diagnosis of CDG on clinical basis is difficult due to the extreme heterogeneity of phenotypes. The biochemical hall-mark of CDG is the abnormal pattern of transferrin isoforms routinely determined in lab by isoelectric focusing (IEF) method. Deficiency of transferrin glycosylation was observed also in other inborn errors of sugar metabolism, galactosemia and hereditary fructose intolerance. Hypoglycosylation of transferrin in these diseases is transient, depends of the toxic sugars in the diet and disappears during dietary treatment. Liver disease constitutes an important part of the complex phenotypes of CDG, galactosemia and fructosemia.