| Acknowledgements | p. xi |
| Abbreviations | p. xii |
| Glossary of terms | p. xiv |
| Foreword | p. xvii |
| Preface | p. xix |
| Plate 1 | p. xx |
| An introduction to carbohydrate chemistry | p. 1 |
| Introduction | p. 1 |
| What are carbohydrates? | p. 1 |
| Monosaccharides are aldoses and ketoses | p. 2 |
| A carbon atom may be asymmetric - the concept of chirality | p. 2 |
| Monosaccharide 'family trees' | p. 4 |
| D-Forms and l-forms of carbohydrates | p. 5 |
| Numbering the carbon atoms in a monosaccharide molecule | p. 7 |
| (+) and (-) forms of carbohydrates | p. 8 |
| The concept of epimerization | p. 8 |
| Monosaccharides form ring structures | p. 9 |
| How the rings are formed - the formation of hemiacetals and hemiketals | p. 11 |
| Monosaccharide [alpha]- and [beta]-anomers | p. 14 |
| Equilibrium between different structures | p. 15 |
| Examples of some biologically important monosaccharides | p. 15 |
| Examples of some important monosaccharide derivatives | p. 17 |
| The linking together of monosaccharides to form chains | p. 22 |
| [alpha]- and [beta]-glycosidic bonds | p. 24 |
| Different linkages | p. 25 |
| Conventions for describing oligosaccharides | p. 26 |
| Reducing sugars | p. 27 |
| Examples of biologically important disaccharides | p. 28 |
| Ways of illustrating oligosaccharide chains | p. 29 |
| The complex carbohydrate structure database (CCSD) | p. 30 |
| Further reading | p. 30 |
| Enzymes of glycosylation - the glycosyltransferases | p. 31 |
| Introduction | p. 31 |
| Enzymes of glycosylation - glycosidases and glycosyltransferases | p. 31 |
| Nomenclature of glycosyltransferases | p. 33 |
| Initiation of glycosylation by glycosyltransferases | p. 33 |
| Building oligosaccharides - transglycosylation reactions | p. 34 |
| Sugar donors | p. 34 |
| The 'one enzyme-one linkage' rule - and exceptions to it | p. 34 |
| Cation and pH requirements of glycosyltransferases | p. 35 |
| Localization of glycosyltransferases along the secretory pathway | p. 35 |
| Substrate recognition by glycosyltransferases | p. 36 |
| Glycosyltransferase 'families' | p. 37 |
| The molecular structure and organization of glycosyltransferases | p. 42 |
| Cell-surface and secreted forms of glycosyltransferases | p. 43 |
| Regulation of glycosyltransferase expression and activity | p. 44 |
| Evidence for the function of glycans derived from glycosyltransferase mutants | p. 45 |
| Further reading | p. 47 |
| Polysaccharides | p. 49 |
| Introduction - how are polysaccharides defined? | p. 49 |
| Structural polysaccharides | p. 52 |
| Gums, mucilages and other plant polysaccharides | p. 65 |
| Storage polysaccharides | p. 67 |
| Further reading | p. 72 |
| N-Linked glycoproteins | p. 73 |
| What are N-linked glycoproteins? | p. 73 |
| Biosynthesis of N-linked oligosaccharides | p. 73 |
| Common structural features of N-linked oligosaccharides and the generation of structural diversity | p. 82 |
| Functions of N-linked oligosaccharides | p. 86 |
| Further reading | p. 88 |
| O-Linked (mucin-type) glycoproteins | p. 89 |
| What are O-linked glycoproteins? | p. 89 |
| The relationship between N-linked and O-linked glycoproteins | p. 89 |
| Types of O-linked glycoproteins | p. 89 |
| Structure of O-linked mucin-type glycoproteins | p. 90 |
| An overview of the biosynthesis of O-linked glycoproteins | p. 92 |
| Synthesis of O-linked glycans | p. 93 |
| Glycosyltransferase enzymes involved in O-linked oligosaccharide synthesis | p. 102 |
| Regulation of O-glycan synthesis | p. 102 |
| Where does O-glycosylation take place? | p. 103 |
| The MUC family of mucin genes | p. 105 |
| Other membrane-bound mucin-like glycoproteins | p. 109 |
| Trefoil factor family (TFF) domain peptides and their relationship with mucins | p. 109 |
| Other cell membrane-associated mucin molecules | p. 110 |
| Functions of O-linked mucins | p. 111 |
| Further reading | p. 115 |
| O-GlcNAc glycosylation of nuclear and cytosolic proteins | p. 117 |
| Introduction - O-GlcNAc protein glycosylation | p. 117 |
| The functions of O-GlcNAc modification and its interrelationship with phosphorylation | p. 117 |
| Synthesis and cleavage of the O-GlcNAc linkage | p. 119 |
| Functions of the O-GlcNAc modification | p. 120 |
| Further reading | p. 127 |
| Species-specific and unusual types of glycoprotein glycosylation | p. 129 |
| Introduction | p. 129 |
| Glycosylation of prokaryotic glycoproteins | p. 129 |
| Glycosylation of yeast and fungal proteins | p. 133 |
| Glycosylation in plants | p. 135 |
| Protein glycosylation in insects | p. 143 |
| Unusual vertebrate glycosylation: the glycohormones | p. 146 |
| Glycosylation of nuclear and cytoplasmic glycoproteins and proteoglycans | p. 149 |
| Unusual types of O-linked glycosylation | p. 150 |
| Glycogen synthesis and glycogenin | p. 154 |
| Glc([alpha]1[right arrow]2)Gal[beta]-O-hydroxylysine | p. 154 |
| N-Linked Glc[beta]-Asn | p. 154 |
| C-Mannosylation | p. 154 |
| The Gal([alpha]1[right arrow]3)Gal antigen and xenotransplantation | p. 154 |
| Further reading | p. 155 |
| Glycoconjugates of the extracellular matrix of animals | p. 157 |
| Introduction - definition of the extracellular matrix | p. 157 |
| The fibroblast - producer of the extracellular matrix | p. 158 |
| Proteoglycans and glycosaminoglycans of the extracellular matrix | p. 160 |
| The protein backbone of glycosaminoglycans | p. 166 |
| Biosynthesis of proteoglycans | p. 167 |
| Functions of the glycosaminoglycans | p. 167 |
| Glycoproteins of the extracellular matrix | p. 169 |
| Basal lamina | p. 170 |
| Further reading | p. 173 |
| Glycosphingolipids | p. 175 |
| Introduction | p. 175 |
| Structure of GSL | p. 175 |
| Location of GSL | p. 175 |
| Biosynthesis of GSL | p. 176 |
| Nomenclature | p. 180 |
| Degradation | p. 181 |
| The distribution of GSL | p. 181 |
| Function of GSL | p. 184 |
| GSL receptors for pathogens | p. 185 |
| Further reading | p. 185 |
| Glycan chain extension and some common and important glycan structures | p. 187 |
| Introduction | p. 187 |
| Type 1 to 6 chains | p. 187 |
| Polylactosamines | p. 188 |
| Histo-blood group sugars | p. 188 |
| The ABO blood group system | p. 189 |
| The Lewis system | p. 193 |
| The I and i antigens | p. 198 |
| P[superscript k], P and P[subscript 1] antigens | p. 199 |
| 'Abnormal' blood group sugars: T, Tn, Cad and Tk | p. 200 |
| Fucosylation | p. 201 |
| Sialylation | p. 201 |
| Further modification | p. 202 |
| Further reading | p. 202 |
| Sialic acids | p. 203 |
| Occurrence | p. 203 |
| Types, modifications and linkages of sialic acids | p. 203 |
| Biosynthesis and metabolism of sialic acids | p. 205 |
| Sialylation of oligosaccharides: the sialyltransferases and regulation of their activity | p. 206 |
| Desialylation | p. 207 |
| Methods for analysing sialic acids | p. 208 |
| Sialic acid-binding lectins | p. 209 |
| General functions of sialic acids | p. 209 |
| Polysialic acid | p. 218 |
| Functional consequences of disrupted sialylation | p. 220 |
| Further reading | p. 220 |
| Glycosylphosphatidylinositol (GPI)-anchored proteins | p. 221 |
| Prevalence | p. 221 |
| Structure | p. 221 |
| Models for studying the biosynthesis of GPI-anchored proteins | p. 222 |
| Biosynthetic steps | p. 223 |
| Glycosylation of GPI-anchored proteins | p. 224 |
| The function of GPI anchors | p. 225 |
| Further reading | p. 226 |
| Carbohydrate-binding proteins (lectins) | p. 227 |
| What are lectins? | p. 227 |
| A brief history | p. 227 |
| Nomenclature | p. 229 |
| Lectin families | p. 230 |
| Carbohydrate-binding specificity | p. 232 |
| Blood group-specific lectins | p. 233 |
| Distribution and function of lectins | p. 233 |
| Occurrence and functions of plant lectins | p. 234 |
| Bacterial, viral and protozoan lectins | p. 236 |
| Slime mould lectins | p. 237 |
| Invertebrate lectins | p. 237 |
| Vertebrate lectins | p. 237 |
| Lectins as tools in carbohydrate analysis | p. 247 |
| Lectins in the diagnosis of infections, drug targeting and toxic conjugates for directed cell killing | p. 247 |
| Further reading | p. 248 |
| Tools for carbohydrate analysis | p. 249 |
| Introduction - the range of tools and methods available | p. 249 |
| The use of lectins | p. 249 |
| Analysis of glycoproteins by SDS-PAGE and Western electroblotting | p. 258 |
| Proteome analysis | p. 261 |
| Preparation of glycoproteins for oligosaccharide analysis | p. 262 |
| Release of glycans | p. 262 |
| Detecting oligosaccharides | p. 264 |
| Oligosaccharide separation and mapping by HPLC | p. 265 |
| Separation and mapping of oligosaccharides by fluorophore-assisted carbohydrate electrophoresis (FACE) | p. 266 |
| Separation and mapping of oligosaccharides by capillary electrophoresis | p. 266 |
| Oligosaccharide analysis by nuclear magnetic resonance | p. 267 |
| Determining the mass of an oligosaccharide using mass spectrometry | p. 267 |
| Methods for determining the linkage position of monosaccharides in oligosaccharides | p. 268 |
| Thin-layer chromatography of glycolipids | p. 269 |
| Further reading | p. 269 |
| Modulation of glycan expression using inhibitors of N- and O-linked glycoconjugate processing, and transgenic technology | p. 271 |
| Introduction | p. 271 |
| Complete deglycosylation by chemical and enzymatic methods | p. 271 |
| Complete deglycosylation by expression in bacterial systems | p. 271 |
| Lectin-resistant cell lines | p. 271 |
| Glycosylation inhibitors | p. 272 |
| Inhibitors of N-linked glycosylation | p. 272 |
| O-Linked glycoprotein inhibitors | p. 280 |
| Glycosylation engineering | p. 281 |
| Experimental addition and deletion of glycosyltransferase genes in cell culture | p. 281 |
| Transgenic animals | p. 282 |
| Further reading | p. 285 |
| Disease processes in which carbohydrates are involved | p. 287 |
| Introduction | p. 287 |
| Infectious diseases | p. 287 |
| Leukocyte recruitment in inflammation | p. 291 |
| Changes in glycosylation of leukosialin with differentiation, immune deficiency and malignancy | p. 293 |
| Glycosylation and HIV infection | p. 294 |
| Cancer metastasis | p. 295 |
| Altered glycoforms of IgG in rheumatoid arthritis | p. 303 |
| Inherited disorders in glycan biosynthesis | p. 304 |
| Inborn errors in carbohydrate catabolism: abnormal catabolism of glycoconjugates - the lysosomal storage diseases | p. 308 |
| Further reading | p. 312 |
| Carbohydrate-based therapeutics | p. 313 |
| Introduction | p. 313 |
| Carbohydrate-based drugs and therapeutic compounds | p. 313 |
| Therapeutic glycoconjugates | p. 314 |
| Carbohydrates in imaging studies | p. 315 |
| Carbohydrates in drug delivery | p. 316 |
| Genetic disorders of carbohydrate synthesis or metabolism | p. 317 |
| Anti-inflammatory therapies | p. 318 |
| Transplant rejection mediated by carbohydrates | p. 319 |
| Inhibitors of microbial, viral and parasitic infection | p. 323 |
| Anti-cancer therapies and vaccines | p. 326 |
| Further reading | p. 327 |
| Carbohydrate biotechnology | p. 329 |
| Introduction | p. 329 |
| Barriers to chemical synthesis of carbohydrate compounds - why biotechnology is so important | p. 329 |
| The current state of carbohydrate biotechnology | p. 329 |
| Use of enzymes in aqueous solution and in solid-phase systems to produce and modify carbohydrates | p. 330 |
| Expression cloning of glycosyltransferases | p. 336 |
| Glyco-mimetic peptides | p. 342 |
| Potential uses of lectins in biotechnology | p. 342 |
| Some applications of carbohydrate biotechnology in the food, pharmaceutical and related industries | p. 343 |
| Further reading | p. 345 |
| Index | p. 346 |
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