Unknown

Dataset Information

0

Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I.


ABSTRACT: This study describes the discovery of a new inherited disorder of glycosylation named "CDG-Ik." CDG-Ik (congenital disorder of glycoslyation type Ik) is based on a defect of human mannosyltransferase I (MT-I [MIM 605907]), an enzyme necessary for the elongation of dolichol-linked chitobiose during N-glycan biosynthesis. Mutations in semiconserved regions in the corresponding gene, HMT-1 (yeast homologue, Alg1), in two patients caused drastically reduced enzyme activity, leading to a severe disease with death in early infancy. One patient had a homozygous point mutation (c.773C-->T, S258L), whereas the other patient was compound heterozygous for the mutations c.773C-->T and c.1025A-->C (E342P). Glycosylation and growth of Alg1-deficient PRY56 yeast cells, showing a temperature-sensitive phenotype, could be restored by the human wild-type allele, whereas only slight restoration was observed after transformation with the patients' alleles.

SUBMITTER: Kranz C 

PROVIDER: S-EPMC1182267 | biostudies-literature | 2004 Mar

REPOSITORIES: biostudies-literature

altmetric image

Publications

Congenital disorder of glycosylation type Ik (CDG-Ik): a defect of mannosyltransferase I.

Kranz Christian C   Denecke Jonas J   Lehle Ludwig L   Sohlbach Kristina K   Jeske Stefanie S   Meinhardt Friedhelm F   Rossi Rainer R   Gudowius Sonja S   Marquardt Thorsten T  

American journal of human genetics 20040217 3


This study describes the discovery of a new inherited disorder of glycosylation named "CDG-Ik." CDG-Ik (congenital disorder of glycoslyation type Ik) is based on a defect of human mannosyltransferase I (MT-I [MIM 605907]), an enzyme necessary for the elongation of dolichol-linked chitobiose during N-glycan biosynthesis. Mutations in semiconserved regions in the corresponding gene, HMT-1 (yeast homologue, Alg1), in two patients caused drastically reduced enzyme activity, leading to a severe disea  ...[more]

Similar Datasets

| S-EPMC1182261 | biostudies-literature
| S-EPMC1763046 | biostudies-other
| S-EPMC3509812 | biostudies-literature
| S-EPMC1718926 | biostudies-other
2008-07-11 | GSE8440 | GEO
| S-EPMC200991 | biostudies-literature
| S-EPMC1222867 | biostudies-other
| S-EPMC3509848 | biostudies-literature
| S-EPMC377427 | biostudies-literature
| S-EPMC9813274 | biostudies-literature