PubMed:11159919 JSONTXT

{"target":"http://pubannotation.org/docs/sourcedb/PubMed/sourceid/11159919","sourcedb":"PubMed","sourceid":"11159919","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/11159919","text":"Defect in N-glycosylation of proteins is tissue-dependent in congenital disorders of glycosylation Ia.\nThe biochemical hallmark of Congenital Disorders of Glycosylation (CDG) including type Ia is a defective N-glycosylation of serum glycoproteins. Hypoglycosylated forms of alpha1-antitrypsin have been detected by Western blot in serum from CDG Ia patients. In contrast we were not able to detect hypoglycosylation in alpha1-antitrypsin synthesized by fibroblasts, keratinocytes, enterocytes, and leukocytes. Similarly no hypoglycosylation was detectable in a membrane-associated N-linked glycoprotein, the facilitative glucose transporter GLUT-1 and also in serum immunoglobulin G isolated from sera of CDG Ia patients. We conclude that the phenotypic expression of CDG Ia is 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