Carbohydrate-deficient glycoprotein syndrome type V: Deficiency of dolichyl- P -Glc:Man 9 GlcNAc 2 - PP -dolichyl glucosyltransferase
| Autor: | Roland Knauer, Ludwig Lehle, K von Figura, Christian Körner, U Holzbach, Folker Hanefeld |
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| Rok vydání: | 1998 |
| Předmět: |
chemistry.chemical_classification
0303 health sciences Multidisciplinary Methionine biology Mannose Mannose-6-Phosphate Isomerase Molecular biology 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Glucosyltransferases chemistry Biochemistry Transferrin biology.protein Glucosyltransferase Glycoprotein 030217 neurology & neurosurgery Phosphomannomutase 030304 developmental biology |
| Zdroj: | Proceedings of the National Academy of Sciences. 95:13200-13205 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.95.22.13200 |
| Popis: | Deficiency of dolichyl- P -Glc:Man 9 GlcNAc 2 - PP -dolichyl glucosyltransferase is the cause of an additional type of carbohydrate-deficient glycoprotein syndrome (CDGS type V). Clinically this type resembles the classical type Ia of CDGS caused by the deficiency of phosphomannomutase. As a result of the glucosyltransferase deficiency in CDGS type V nonglucosylated lipid-linked oligosaccharides accumulate. The defect is leaky and glucosylated oligosaccharides are found on nascent glycoproteins. The limited availability of glucosylated lipid-linked oligosaccharides explains the incomplete usage of N - glycosylation sites in glycoproteins. This finding is reflected in the presence of transferrin forms in serum that lack one or both of the two N - linked oligosaccharides and the reduction of mannose incorporation to about one-third of control in glycoproteins of fibroblasts. |
| Databáze: | OpenAIRE |
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