Glycobiology, 2000, Vol. 10, No. 5 439-449
© 2000 Oxford University Press
MUC1: the polymorphic appearance of a human mucin
Institute of Biochemistry, Medical Faculty, University of Cologne, Joseph-Stelzmann-Strasse 52, 50931 Köln, Germany
Accepted on December 1, 1999;
Key words: mucin/MUC1/O-glycosylation/tumor antigen/cancer
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Introduction |
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The term "mucin" has changed its meaning over the last decades prompted by the impressive progress made in the field of glycobiology. Up to the 1970s researchers exclusively used this term to refer to the major glycoprotein components in secreted mucus lining the surfaces of glandular epithelia. The best characterized species during that time, the mucins from ovine and bovine submaxillary glands, served as structural models for this subclass of glycoproteins, since they exhibited the features regarded as typical for mucins: a high carbohydrate content (exceeding 50% by weight) with a concomitant high buoyant density and a threonine/serine rich peptide core serving as a scaffold for the addition of uniform, simple and mainly acidic oligosaccharides. A dense hydrophilic coat of O-linked negatively charged glycans was a simple structural model, but in accord with the proposed function of mucins which was regarded to lie in the formation of a viscoelastic gel
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MUC1 expression and function |
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Polymorphism of the MUC1 protein |
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Polymorphism of MUC1 glycosylation |
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Cellular biosynthesis of MUC1 glycans
Tissue-specific glycosylation patterns
Tumor-associated alterations of MUC1 O-glycosylation
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Site-specific O-glycosylation of MUC1 |
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Site-specificity and regulation of initial O-glycosylation
Localization of O-glycosylation sites on in vivo modified MUC1
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MUC1 O-glycosylation and immunogenicity/antigenicity |
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MUC1 as B cell immunotarget
MUC1 as T cell immunotarget
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Concluding remarks and perspectives |
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Acknowledgments |
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Footnotes |
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References |
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