Defective mucin-type glycosylation on α-dystroglycan in COG-deficient cells increases its susceptibility to bacterial proteases.

ABSTRACT: Deficiency in subunits of the conserved oligomeric Golgi (COG) complex results in pleiotropic defects in glycosylation and causes congenital disorders in humans. Insight regarding the functional consequences of this defective glycosylation and the identity of specific glycoproteins affected is lacking. A chemical glycobiology strategy was adopted to identify the surface glycoproteins most sensitive to altered glycosylation in COG-deficient Chinese hamster ovary (CHO) cells. Following metabolic labeling, an unexpected increase in GalNAz incorporation into several glycoproteins, including α-dystroglycan (α-DG), was noted in cog1-deficient ldlB cells. Western blotting analysis showed a significantly lower molecular weight for α-DG in ldlB cells compared with WT CHO cells. The underglyc

SUBMITTER: Yu SH 

PROVIDER: S-EPMC6139567 | biostudies-literature | 2018 Sep

REPOSITORIES: biostudies-literature