Taylor & Drickamer: Introduction to Glycobiology: 2e 
Key Reading References
Answers to ProblemsTaylor & Drickamer: Introduction to Glycobiology: 2e
Chapter 11
Key References:
Ai, X., Do, A.-T., Lozynska, O., Kusche-Gullberg, M. Lindahl, U. and Emerson, C.P., Jr. (2003) QSulf1 remodels the 6-O sulfation states of cell sruface heparan sulphate proteoglycans to promote Wnt signaling. Journal of Cell Biology 162, 341-351. This paper describes a recently identified sulphatase the remodel glycosaminoglycans.
http://www.jcb.org/cgi/reprint/162/2/341.pdf
Blair, S.S. (2000) Notch signaling: fringe really is a glycosyltransferase. Current Biology 10, R608–R612. The evidence that glycosylation of notch by fringe modulates notch signalling is reviewed.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VRT-411G2MX-F-7&_cdi=6243&_user=217827&_orig=search&_coverDate=08%2F14%2F2000&_qd=1&_sk=999899983&view=c&wchp=dGLbVzb-zSkWz&md5=5eb0ff41f3d691c12e3a9f4ca2a3fd7b&ie=/sdarticle.pdf
Bruses, J.L. and Rutishauser, U. (2001) Roles, regulation and mechanism of polysialic acid function during neural development. Biochimie 83, 635–643. This is a detailed review of polysialic acid.
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Coetzee, T., Fujita, N., Dupree, J., Shi, R., Blight, A., Suzuki, K., Suzuki, K., and Popko, B. (1996) Myelination in the absence of galactocerebroside and sulfatide: normal structure with abnormal function and regional instability. Cell 86, 209–219. This paper describes the phenotype of knockout mice that cannot synthesize galactocerebroside or sulphatide.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSN-4195BWM-7-F&_cdi=7051&_user=217827&_orig=search&_coverDate=07%2F26%2F1996&_qd=1&_sk=999139997&view=c&wchp=dGLbVzb-zSkWA&md5=d537e3f8039ff504c6bddf11bc5c08a8&ie=/sdarticle.pdf
Collins, B.E., Ito, H., Sawada, N., Ishida, H., Kiso, M., and Schnaar, R.L. (1999) Enhanced binding of the neural siglecs, myelin-associated glycoprotein and schwann cell myelin protein, to Chol-1 (alpha-series) gangliosides and novel sulfated Chol-1 analogs. Journal of Biological Chemistry 274, 37637–37643. Experiments that define the extended carbohydrate binding specificity of MAG are described.
http://www.jbc.org/cgi/reprint/274/53/37637.pdf
Gascoigne, N.R.J. (2002) T-cell differentiation: MHC class I’s sweet tooth lost on maturity. Current Biology 12, R99–R101. A new model is proposed for how cell surface glycans modulate lymphocyte activation.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VRT-454B91B-B-5&_cdi=6243&_user=217827&_orig=search&_coverDate=02%2F05%2F2002&_qd=1&_sk=999879996&view=c&wchp=dGLbVzb-zSkzS&md5=5dd5873c03fb3fb641ffcb4ad5238aa1&ie=/sdarticle.pdf
Kreuger, J., Salmivirta, M., Sturiale, L., Gimenez-Gallego, G., and Lindahl, U. (2001) Sequence analysis of heparan sulphate epitopes with graded affinities for fibroblast growth factors 1 and 2. Journal of Biological Chemistry 276, 30744–30752. Key experiments defining the sequence of heparan sulphate saccharides that bind to growth factors are presented.
http://www.jbc.org/cgi/reprint/276/33/30744.pdf
Lander, A.D. and Selleck, S.B. (2000) The elusive functions of proteoglycans: in vivo veritas. Journal of Cell Biology 148, 227-232. Drospophila and mammalian mutations affecting proteoglycans are compared in a thoughtful review.
http://www.jcb.org/cgi/reprint/148/2/227.pdf
Lowe, J.B. and Marth, J.D. (2003) A genetic approach to mammalian glycan function. Annual Review of Biochemistry 72, 643-691. Most of the knockout mice that have been created in the glycan biosynthesis pathways and summarised in a well-organised and critical review.
http://arjournals.annualreviews.org/doi/pdf/10.1146/annurev.biochem.72.121801.161809
Park, P.W., Reizes, O., and Bernfield, M. (2000) Cell surface heparan sulfate proteoglycans: selective regulators of ligand-receptor encounters. Journal of Biological Chemistry 275, 29923–29926. This is a short review covering details of interactions between heparan sulphate proteoglycans and their protein ligands and the cellular processes modulated by these interactions.
http://www.jbc.org/cgi/reprint/275/39/29923.pdf
Pellegrini, L. (2001) Role of heparan sulfate in fibroblast growth factor signalling: a structural view. Current Opinion in Structural Biology 11, 629–634. Insights gained from crystal structures of growth factors in complex with heparin are reviewed.
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Rapraeger, A.C. (2000) Syndecan-regulated receptor signaling. Journal of Cell Biology 149, 995–997. This is a short commentary reviewing evidence for roles of the cell-surface proteoglycan syndecan in modulating cell-matrix adhesion and signalling.
http://www.jcb.org/cgi/reprint/149/5/995.pdf
Schachner, M. and Bartsch, U. (2000) Multiple functions of the myelin-associated glycoprotein MAG (siglec-4a) in formation and maintenance of myelin. Glia 29, 154–165. The functions of MAG in the nervous system are reviewed in detail.
[Your institution will need to be a subscriber to access this article online at: http://www3.interscience.wiley.com/cgi-bin/fulltext/68503490/PDFSTART]
Vyas, A.A. and Schnaar, R.L. (2001) Brain gangliosides: functional ligands for myelin stability and the control of nerve regeneration. Biochimie 83, 677–682. The evidence for roles of gangliosides in maintenance of myelin and in nerve regeneration is reviewed.
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Wallis, G.A. (1995) Cartilage disorders. The importance of being sulphated. Current Biology 5, 225–227. This is a short commentary on the finding that mutations in the gene for a sulphate transporter underlie a cartilage disorder, which shows the importance of sulphation of glycosaminoglycans.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6VRT-4DCW4J9-P-5&_cdi=6243&_user=217827&_orig=search&_coverDate=03%2F31%2F1995&_qd=1&_sk=999949996&view=c&wchp=dGLbVlz-zSkWW&md5=7cc86e616fb54a1db7852426c5d418a8&ie=/sdarticle.pdf
Wassarman, P.M. (1999) Mammalian fertilisation: molecular aspects of gamete adhesion, endocytosis and fusion. Cell 96, 175–183. The data demonstrating involvement of glycans in sperm–egg interactions are summarized.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSN-4194MSC-2-H&_cdi=7051&_user=217827&_orig=search&_coverDate=01%2F22%2F1999&_qd=1&_sk=999039997&view=c&wchp=dGLbVlz-zSkzV&md5=88b30279b44b298b7a70b8e30bf4c926&ie=/sdarticle.pdf
Yamashita, T., Wada, R., Sasaki, T., Deng, C., Bierfreund, U., Sandhoff, K., and Proia, P.L. (1999) A vital role for glycosphingolipid synthesis during development and differentiation. Proceedingsof the National Academy of Sciences USA 96, 9142–9147. This paper describes the phenotype of mice in which the gene for glucosylceramide synthase has been knocked out, preventing synthesis of glycosphingolipids.
http://www.pnas.org/cgi/reprint/96/16/9142.pdf
Questions
2) Compare the findings of the following two studies that have investigated specificity of binding of heparan sulphate proteoglycans to two different families of growth factors.
References:
Kreuger, J., Jemth, P., Sanders-Lindberg, E., Eliahu, L., Ron, D., Basilico, C., Salmivirta, M. and Lindahl, U. (2005) Fibroblast growth factors share binding sites in heparan sulphate. Biochemical Journal 389, 145-150.
http://www.biochemj.org/bj/389/0145/3890145.pdf
Pankonin, M.S., Gallagher, J.T. and Loeb, J.A. (2005) Specific structural features of heparan sulfate proteoglycans potentiate neuregulin-1 signalling. Journal of Biological Chemistry 280, 383-388.
http://www.jbc.org/cgi/reprint/280/1/383.pdf
4) Knockout mice lacking enzymes involved in glycan synthesis have provided insights into the importance of glycans in development, but sometimes knockout experiments produce surprising results. Explain how the unexpectedly mild phenotype of mice lacking Golgi mannosidase II lead to the discovery of an alternate pathway for synthesis of N-linked glycans.
Reference:
Chui, D., Oh-Eda, M., Liao, Y.F., Panneerselvam, K., Lal, A., Marek, K.W., Freeze, H.H., Moreman, K.W., Fukuda, M.N. and Marth, J.D. (1997) Alpha-mannosidase-II deficiency results in dyserythropoiesis and unveils an alternate pathway in oligosaccharide biosynthesis. Cell 90, 157-167.
http://www.sciencedirect.com/science?_ob=MImg&_imagekey=B6WSN-419B8BT-K-N&_cdi=7051&_user=217827&_orig=search&_coverDate=07%2F11%2F1997&_qd=1&_sk=999099998&view=c&wchp=dGLzVzz-zSkzV&md5=181cd5dae5c0674584b25a6b36c75b49&ie=/sdarticle.pdf
5) The mechanism by which the extended glycans created by the action of the fringe glycosyltransferase modify the interactions of Notch with Delta and Serrate is not yet known. Suggest some possible mechanisms. One possible mechanism is proposed in the following paper. Assess the evidence to support this proposal.
Reference:
Xu, A., Lei, L. and Irvine, K.D. (2005) Regions of Drosophila notch that contribute to ligand binding and the modulatory influence of fringe. Journal of Biological Chemistry 280, 30158-30165.
http://www.jbc.org/cgi/reprint/280/34/30158.pdf
Box 11.1 Glycobiology of disease: Human diseases result from aberrant proteoglycan biosynthesis
Lead references:
Karniski, L.P. (2004) Functional expression and cellular distribution of diastrophic dysplasia sulphate transporter (DTDST) gene mutations in HEK cells. Human Molecular Genetics 13, 2165-2171.
http://hmg.oxfordjournals.org/cgi/reprint/13/19/2165.pdf
Zak, B.M., Crawford, B.E. and Esko, J.D. (2002) Hereditary multiple exostoses and heparan sulphate polymerization. Biochimica et Biophysica Acta 1573, 346-355.
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Song, H.H., Shi, W., Xiang, Y.-Y. and Filmus, J. (2005) The loss of glypican-3 induces alterations in Wnt signaling. Journal of Biological Chemistry 280, 2116-2125.
http://www.jbc.org/cgi/reprint/280/3/2116.pdf
Box 11.2 Glycotherapeutics: Chondroitinase treatment facilitates regeneration in the central nervous system
Lead references:
Oohira, A., Matsui, F., Tokita, Y., Yamauchi, S. and Aono, S. (2000) Molecular interactions of neuronal chondroitin sulfate proteoglycans in brain development. Archives of Biochemistry and Biophysics. 374, 24-34.
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Silver, J. and Miller, J.H. (2004) Regeneration beyond the glial scar. Nature Reviews Neuroscience 5, 146-156.
[Your institution will need to be a subscriber to access this article online at http://www.nature.com/nrn/journal/v5/n2/pdf/nrn1326.pdf]
Bradbury, E.J., Moon, L.D.F., Popat, R.J., King, V.R., Bennett, G.S., Patel, P.N., Fawcett, J.W. and McMahon, S.B. (2002) Chondroitinase ABC promotes functional recovery after spinal cord injury. Nature 416, 636-640.
[Your institution will need to be a subscriber to access this article online at http://www.nature.com/nature/journal/v416/n6881/pdf/416636a.pdf]
Caggiano, A.O., Zimber, M.P., Ganguly, A., Blight, A.R. and Gruskin, E.A. (2005) Chondroitinase ABCI improves locomotion and bladder function following contusion injury of the rat spinal column. Journal of Neurotrauma 22, 226-239.
[Your institution will need to be a subscriber to access this article online at http://www.liebertonline.com/doi/pdf/10.1089/neu.2005.22.226]
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