Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

The biochemical and biophysical properties of mucins are largely determined by extensive O-glycosylation of serine- and threonine-rich tandem repeat (TR) domains. In a number of human diseases aberrant O-glycosylation is associated with variations in the properties of the cell surface-associated and secreted mucins. To evaluate in vivo the O-glycosylation of mucin TR domains, we generated recombinant chimeric mucins with TR sequences from MUC2, MUC4, MUC5AC, or MUC5B, which were substituted for the native TRs of epitope-tagged MUC1 protein (MUC1F). These hybrid mucins were extensively O-glycosylated and showed the expected association with the cell surface and release into culture media. The presence of different TR domains within the chimeric mucins appears to have limited influence on their posttranslational processing. Alterations in glycosylation were detailed by fast atom bombardment mass spectrometry and reactivity with antibodies against particular blood-group and tumor-associated carbohydrate antigens. Future applications of these chimeras will include investigations of mucin posttranslational modification in the context of disease.

Original publication

DOI

10.1093/glycob/11.6.459

Type

Journal article

Journal

Glycobiology

Publication Date

06/2001

Volume

11

Pages

459 - 471

Keywords

Amino Acid Sequence, Antigens, Tumor-Associated, Carbohydrate, Blood Group Antigens, Carbohydrate Sequence, Glycosylation, Humans, Molecular Sequence Data, Mucin-1, Mucins, Oligosaccharides, Protein Processing, Post-Translational, Recombinant Fusion Proteins, Repetitive Sequences, Amino Acid, Spectrometry, Mass, Fast Atom Bombardment