Taylor & Drickamer: Introduction to Glycobiology: 2e 
Key Reading References
Answers to ProblemsTaylor & Drickamer: Introduction to Glycobiology: 2e
Chapter 12
Key References:
Brockhausen, I. (1999) Pathways of O-glycan biosynthesis in cancer cells. Biochimica et Biophysica Acta 1473, 67–95. This is a detailed review of how O-glycan biosynthesis is altered in different types of cancer.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T1W-3XYG691-7-C&_cdi=4901&_user=217827&_orig=search&_coverDate=12%2F17%2F1999&_qd=1&_sk=985269998&view=c&wchp=dGLbVtb-zSkWz&md5=e9c3d6d5efd18a3225a34fef78ffe479&ie=/sdarticle.pdf]
Bucala, R. and Cerami, A. (1992) Advanced glycosylation: chemistry, biology and implications for diabetes and aging. Advances in Pharmacology 23, 1–34. Glycation is reviewed in detail. Not available online.
Dennis, J.W., Granovsky, M., and Warren, C.E. (1999) Glycoprotein glycosylation and cancer progression. Biochimica et Biophysica Acta 1473, 21–34. The evidence that increased branching of the 1,6 arm of N-linked glycans contributes to cancer progression is reviewed.
[You must have a username and password to access the full article at http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6T1W-3XYG691-4-3&_cdi=4901&_user=217827&_orig=search&_coverDate=12%2F17%2F1999&_qd=1&_sk=985269998&view=c&wchp=dGLbVtz-zSkWA&md5=ec545bd4b639c2c84b91279f02aef5c6&ie=/sdarticle.pdf]
Dennis, J.W., Granovsky, M., and Warren, C.E. (1999) Protein glycosylation in development and disease. BioEssays 21, 412–421. This paper provides a good overview of protein glycosylation in health and disease.
[Your institution will need to be a subscriber to access this article online at: http://www3.interscience.wiley.com/cgi-bin/fulltext/61006932/PDFSTART]
Freeze, H.H. and Westphal, V. (2001) Balancing N-linked glycosylation to avoid disease. Biochimie 83, 791–799. This paper reviews congenital disorders of glycosylation and speculates on possible selective advantages of mutations in the N-linked glycosylation pathway.
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Galili, U. (2001) The a -gal epitope (Gal a 1-3Gal b 1-4GlcNAc-R) in xenotransplantation. Biochimie 83, 557–563. The characteristics of the a -gal epitope, the antibodies that recognize it, and how this interaction causes xenograft rejection are reviewed.
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Kim, Y.J. and Varki, A. (1997) Perspectives on the significance of altered glycosylation of glycoproteins in cancer. Glycoconjugate Journal 14, 569–576. This review gives details of the different glycosylation changes seen in cancer and speculates on how these changes might be linked to cause or progression of tumours.
[Your institution will need to be a subscriber to access this article online at: http://www.metapress.com/media/6a86bnrvql4upahruj3y/contributions/h/3/u/1/h3u1090k16624h2w.pdf]
Krapp, S., Mimura, Y., Jefferis, R., Huber, R. and Sondermann, P. (2003) Structural analysis of human IgG-Fc glycoforms reveals a correlation between glycosylation and structural integrity. Journal of Molecular Biology 325, 979-989. Experiments showing that glycosylation affects the conformation of IgG and thus indirectly modulates complement-fixation activity are presented.
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Michele, D.E. and Campbell, K.P. (2003) Dystrophin-glycoprotein complex: post-translational processing and dystroglycan function. Journal of Biological Chemistry 278, 15457-15460. This brief review and the paper by Schachter et al. (2004, see below) summarise the genetics and biochemistry of dystroglyan glycosylation defects.
http://www.jbc.org/cgi/reprint/278/18/15457.pdf
Mohlke, K.L., Purkayastha, A.A., Westrick, R.J., Smith, P.L., Petryniak, B., Lowe, J.B., and Ginsburg, D. (1999) Mvwf, a dominant modifier of murine von Willebrand factor, results from altered lineage-specific expression of a glycosyltransferase. Cell 96, 111–120. Experiments showing that misexpression of a GalNAc transferase causes von Willebrand factor deficiency are described.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSN-41GP6VJ-F-H&_cdi=7051&_user=217827&_orig=search&_coverDate=01%2F08%2F1999&_qd=1&_sk=999039998&view=c&wchp=dGLbVzz-zSkWW&md5=ccb2d0f129c93fa97954a1c92ce1fd7f&ie=/sdarticle.pdf
Schachter, H. (2001) Congenital disorders involving defective N-glycosylation of proteins. Cellular and Molecular Life Sciences 58, 1085–1104. These disorders are reviewed in detail.
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Schachter, H., Vajsar, J. and Zhang, W. (2004) The role of defective glycosylation in congenital muscular dystrophy. Glycoconjugate Journal 20, 291-300.
[Your institution will need to be a subscriber to access this article online at: http://www.metapress.com/media/f27puhqwlj0570lxgndm/contributions/x/u/6/8/xu68350587321152.pdf]
Tretter, V., Altmann, F., Kubelka, V., Marz, L., and Becker, W.M. (1993) Fucose a 1,3 linked to the core region of glycoprotein N-glycans creates an important epitope for IgE from honeybee venom allergic individuals. International Archives of Allergy and Immunology 102, 259–266. Experiments defining a 1,3 linked fucose as a major cause of allergic responses to bee stings are presented. Not available online.
Questions
2) Describe the types of experiments used to define the molecular basis for congenital disorders of glycosylation.
References:
Kim, S., Westphal, V., Srikrishna G., Mehta, D.P., Peterson, S., Filiano, J., Karnes, P.S., Patterson, M.C. and Freeze, H.H. (2000) Dolichol phosphate mannose synthase (DPM1) mutations define congenital orders of glycosylation Ie (CDG-Ie). Journal of Clinical Investigation 105, 191-198.
http://www.jci.org/cgi/reprint/105/2/191.pdf
Burda, P., Borsig, L., de Rijk-van Andel, J., Wevers, R., Jaeken, J., Carchon, H., Berger, E.G. and Aebi, M. (1998) A novel carbohydrate-deficient syndrome characterized by a deficiency in glucosylation of the dolichol-linked oligosaccharide. Journal of Clinical Investigation 102, 647-652.
http://www.jci.org/cgi/reprint/102/4/647.pdf
4) Assess the indirect evidence that the product of the LARGE gene is a glycosyltransferase that synthesizes chains of repeating glucose-GlcNAc disaccharide units.
Reference:
Patnaik, S.K. and Stanley, P. (2005) Mouse Large can modify complex N- and mucin O-glycans on α-dystroglycan to induce laminin binding. Journal of Biological Chemistry 280, 20851-20859.
http://www.jbc.org/cgi/reprint/280/21/20851.pdf
5) Describe the experiments used to show that alterations in the glycan structures of MUC-1 on tumour cells are associated with changes in activity of glycosyltransferases.
Reference:
Dalziel, M., Whitehouse, C., McFarlane, I., Brockhausen, I., Gschmeissner S., Schwientek, T., Clausen, H., Burchell, J.M. and Taylor-Papadimitriou, J. (2001) The relative activities of the C2GnT1 and ST3Gal-1 glycosyltransferases determine O-glycan structure and expression of a tumor-associated epitope on MUC1. Journal of Biological Chemistry 276, 11007-11015.
http://www.jbc.org/cgi/reprint/276/14/11007.pdf
Box 12.1 Glycobiology of disease: Human diseases result from aberrant proteoglycan biosynthesis
Lead references:
Lead references:
Fuster, M.M., Brown, J.R., Wang, L. and Esko, J.D. (2003) A disaccharide precursor of sialyl Lewis x inhibits metastatic potential of tumor cells. Cancer Research 63, 2775-2781.
http://cancerres.aacrjournals.org/cgi/reprint/63/11/2775.pdf
Kim, Y.J., Borsig, L., Varki, N.M. and Varki, A. (1998) P-selectin deficiency attenuates tumor growth and metastasis. Proceedings of the National Academy of Sciences USA 95, 9325-9330.
http://www.pnas.org/cgi/reprint/95/16/9325.pdf
Weston, B.W., Hiller, K.M., Mayben, J.P., Manousos, G.A., Bendt, K.M., Liu, R. and Cusack, J.C., Jr. (1999) Expression of human α(1,3)fucosyltransferase antisense sequences inhibits selectin-mediated adhesion and liver metastasis of colon carcinoma cells. Cancer Research 59, 2127-2135.
http://cancerres.aacrjournals.org/cgi/reprint/59/9/2127.pdf
Brown, J.R., Fuster, M.M., Whisenant, T. and Esko, J.D. (2003) Expression patterns of a2,3-sialyltransferases and a1,3-fucosyltransferases determine the mode of sialyl Lewis x inhibition by disaccharide decoys. Journal of Biological Chemistry 278, 23352-23359.
http://www.jbc.org/cgi/reprint/278/26/23352.pdf
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