Mucins Glycosylation

Chapters on the role of mucins and mucin glycosylation in bacterial adhesion (Chapter 27), and on bioengineering of glucansucrases (Chapter 28) complete the collection of topics assembled in this volume. 

The genes encoding the polypeptide backbones of a number of mucins derived from various tissues (eg, pancreas, small intestine, trachea and bronchi, stomach, and salivary glands) have been cloned and sequenced. These studies have revealed new information about the polypeptide backbones of mucins (size of tandem repeats, potential sites of N-glycosylation, etc) and ultimately should reveal aspects of their genetic control. Some important properties of mucins are summarized in Table 47-8. 

Marcaurelle LA, Mizoue LS, Wilken J, et al. Chemical synthesis of lymphotactin a glycosylated chemokine with a C-terminal mucin-like domain. Chemistry 2001 7 1129-32. 

H. C. Hang and C. R. Bertozzi, The chemistry and biology of mucin-type O-linked glycosylation, Bioorg. Med. Chem., 13 (2005) 5021-5034. 

T. A. Gerken, Kinetic modeling confirms the biosynthesis of mucin core 1 (/i-Gal (1 -3)x-Gal YAc-O-Ser/Thr) O-glycan structures are modulated by neighboring glycosylation effects, Biochemistry, 43 (2004) 4137—4142. 

T. A. Gerken, C. L. Owens, and M. Pasumarthy, Determination of the site-specific O-glycosylation pattern of the porcine submaxillary mucin tandem repeat glycopeptide, J. Biol. Chem., 272 (1997) 9709-9719. 

Karsten, U., Serttas, N., Paulsen, H., Danielczyk, A., and Goletz, S. (2004) Binding patterns of DTR-specific antibodies reveal a glycosylation-conditioned tumor-specific epitope of the epithelial mucin (MUC1). Glycobiology 14(8), 681-692. 

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