PMC:4572578 / 8148-8941 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/4572578","sourcedb":"PMC","sourceid":"4572578","source_url":"https://www.ncbi.nlm.nih.gov/pmc/4572578","text":"Next, we investigated whether an assumed defect in the assembly of the ER tethering complex impairs glycosylation and/or results in increased ER stress. Isoelectric focusing of transferrin, alpha-1-antitrypsin, and apolipoprotein CIII followed by in-gel immunodetection was performed in sera of a control subject, a COG6-CDG individual, and five individuals with NBAS mutations. Although the observed patterns indicated a clear deficiency in N-/O-glycosylation in the CDG individual, no differences were observed for the NBAS-mutant individuals compared to controls (Figure S2). These findings suggest that under the investigated conditions NBAS deficiency does not disturb retrograde transport between ER and Golgi to the extent that obvious changes in glycosylation patterns can be observed.","tracks":[]}