The Biochemistry of glycoproteins and proteoglycans

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The Biochemistry of glycoproteins and proteoglycans

edited by William J. Lennarz

Plenum Press, c1980

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Includes bibliographies and index

内容説明・目次

内容説明

Although glycoproteins and proteoglycans have been a subject of re- search for many years, it is only during the last five or so years that they have aroused the interest of a very broad cross section of investigators in the biological sciences. The reason for this expanded interest in these molecules is simple: not only are glycoproteins and proteoglycans ubiq- uitous, but many are molecules with well-defined and important biological functions. The list of molecules that fall into this category grows daily; interferon, immunoglobulins, certain hormones, many cell surface recep- tors, and viral coat proteins are but a few examples. Thus, investigators with interests as diverse as viral replication. cell-cell interactions. poly- isoprenoid synthesis, secretory processes, hormone responses, embryonic development, and immunology have become concerned with glycopro- teins and proteoglycans. The objective of this book is to summarize the current state of knowledge on the biochemistry of these molecules. Coverage is by no means encyclopedic; rather the thrust is to emphasize the recent ad- vances. The first chapter deals primarily with structural work on the oligosaccharide chains of glycoproteins, but it will be apparent in it and in the succeeding two chapters on biosynthesis that not only do structural studies aid biosynthetic investigations, but that studies on biosynthesis often playa major role in elucidation of structure.

目次

1 Structure of Glycoproteins and their Oligosaccharide Units.- 1. Introduction.- 2. Isolation and Structural Analysis of Glycopeptides.- 2.1. Methods for Isolation of Glycopeptides.- 2.2. Methods Used in Determination of Oligosaccharide Structure.- 3. Glycopeptides Containing Oligosaccharides Linked O-Glycosidically to the Peptide.- 3.1. Oligosaccharides Linked through N-Acetylgalactosamine to Serine and Threonine.- 3.2. Oligosaccharides Linked to Serine and Threonine through Sugars Other Than N-Acetylgalactosamine.- 3.3. Oligosaccharides Linked to the Hydroxyl Group of Hydroxylysine and Hydroxyproline.- 4. Glycopeptides Containing the N-Acetylglucosaminyl-Asparagine Linkage.- 4.1. Structure of the Core Region.- 4.2. Structure of "Simple"-Type Oligosaccharides.- 4.3. Structure of "Complex"-Type Oligosaccharides.- 4.4. Structure of the Oligosaccharide-Lipid Intermediate.- 5. Role of Oligosaccharides in Glycoprotein Synthesis.- 6. References.- 2 The Function of Saccharide-Lipids in Synthesis of Glycoproteins.- 1. Introduction.- 2. Dolichol.- 3. Monoglycosyl Derivatives of Dolichol Phosphate.- 3.1. Mannosylphosphoryldolichol and N-Acetylglucosaminyl-pyrophosphoryldolichol.- 3.2. Other Glycosyl Polyprenol Derivatives.- 4. Assembly of Oligosaccharide-Lipids.- 5. Transfer of Oligosaccharide Chains to Endogenous Membrane Proteins.- 6. Transfer of the Oligosaccharide Chains from Oligosaccharide-Lipids to Exogenous, Soluble Proteins.- 6.1. Existence of a Tripeptide Acceptor Sequence.- 6.2. In Vitro Glycosylation of Denatured Soluble Proteins.- 7. A Model for Glycosylation of Membrane and Secretory Glycoproteins.- 8. Regulation of Glycoprotein Synthesis.- 9. Inhibitors of Glycosylation.- 9.1. In Vivo Effects of Deoxy Sugars on Protein Glycosylation.- 9.2. Effect of Deoxy Sugars on the Secretion of Glycoproteins.- 9.3. Effect of Deoxy Sugars on Virus Replication.- 9.4. In Vitro Effect of Deoxy Sugars on Protein Glycosylation.- 9.5. Fluorodeoxy Sugars.- 9.6. Amino Sugars.- 9.7. Bacitracin.- 9.8. Tunicamycin.- 10. References.- 3 Mammalian Glycosyltransferases: Their Role in the Synthesis and Function of Complex Carbohydrates and Glycolipids.- A 1. Introduction.- 1.1. Sugar Nucleotides and Transglycosylation.- 1.2. Glycosyltransferases: General Comments.- 2. Glycosyltransferases Involved in Elongation of N-Glycosidically Linked Oligosaccharides of the N-Acetyllactosamine type.- 2.1. Processing of Protein-Bound Oligosaccharide Prior to Elongation.- 2.2. N-Acetylglucosaminyltransferases and Control of Elongation.- 2.3. Fucosyltransferases.- 2.4. Galactosyltransferases.- 2.5..- 2.6. The Golgi Apparatus as the Major Subcellular Site of Elongation.- 3. Glycosyltransferases Involved in Synthesis of O-Glycosidically Linked Oligosaccharides.- 3.1. Synthesis of Serine(Threonine)-N-Acetyl-D-Galactosamine Linkage.- 3.2. Synthesis of Submaxillary Gland Mucins.- 3.3. Synthesis of Human Blood Group Oligosaccharides.- B 1. Introduction.- 2. New Gangliosides.- 3. Occurrence and Subcellular Distribution.- 4. Gangliosides as Membrane Components.- 5. Biosynthesis and Degradation.- 6. Effect of Cell Transformation on Ganglioside Synthesis.- 7. Gangliosides in Development and Differentiation.- 8. Gangliosides as Membrane Receptors for Toxins and Hormones.- 9. References.- 4 Surface Carbohydrate Alterations of Mutant Mammalian Cells Selected for Resistance to Plant Lectins.- 1. Selection of Cells with Altered Surface Carbohydrate.- 2. Biochemical Basis of a Surface Carbohydrate Alteration.- 3. Genetic and Biochemical Properties of Glt1? CHO Cells.- 3.1. Localization of the Mutated Gene Product.- 3.2. Altered Membrane Properties.- 4. Surface Carbohydrate Alterations of Other Lectin-Resistant (LecR) Cell Lines.- 4.1. Ricin-Resistant (RicR) Mouse L Cells.- 4.2. Wheat Germ Agglutinin-Resistant (WgaR) CHO Cells.- 4.3. Concanavalin A-Resistant (ConAR) CHO Cells.- 5. Membrane Properties of LecR Cells Possessing Specific Carbohydrate Alterations.- 5.1. Lectin Binding and Cytotoxicity.- 5.2. Lectin Agglutination and Capping.- 5.3. Membrane Glycoproteins and Glycolipids.- 6. Properties of Other LecR Cell Lines.- 7. Mechanisms of Lectin Cytotoxicity.- 8. Glycosylation Mutants Selected Without the Use of Lectins.- 9. Concluding Remarks.- 10. References.- 5 Alterations in Glycoproteins of the Cell Surface.- 1. Introduction.- 2. Growth-Dependent Changes in Asparagine-Linked Oligosaccharides of Membrane Glycoproteins.- 2.1. Glycopeptides of Class B.- 2.2. Glycopeptides of Class A.- 3. Transformation-Dependent Changes in Asparagine-Linked Glycopeptides.- 3.1. Comparison Systems.- 3.2. Difference in Sialoglycopeptides (Class B Glycopeptides).- 3.3. Carbohydrate Content.- 3.4. Alterations and Relation to in Vitro and in VivoTumor Cells.- 3.5. Microheterogeneity in Oligosaccharides.- 3.6. Class A Glycopeptides.- 3.7. Changes in Oligosaccharides Derived from Single Glycoproteins.- 4. Changes in Serine- (Threonine-) Linked Oligosaccharides of Membrane Glycoproteins.- 5. Alterations in Glycosaminoglycans.- 6. Use of Endoglycosidases for Detecting Alterations in Cell Surface Glycopeptides.- 6.1. Class A and B Glycopeptides.- 6.2. Endoglycosidases Useful in Structural Analysis of Class C Glycopeptides.- 7. References.- 6 Carbohydrate Recognition Systems for Receptor-Mediated Pinocytosis.- 1. Introduction.- 2. Galactose-Binding Receptor of Mammalian Hepatocytes.- 2.1. Development of the Problem.- 2.2. Binding by Plasma Membranes.- 2.3. Isolation of Binding Protein.- 2.4. Nature of the Binding Mechanism.- 2.5. Specificity of Binding.- 2.6. Circulating Asialoglycoproteins.- 2.7. Subcellular Loci of Binding Protein.- 2.8. Membrane Topology.- 2.9. Regeneration of Binding Protein.- 3. N-Acetylglucosamine-Binding Receptor of Avian Hepatocytes.- 3.1. Historical.- 3.2. Isolation of Binding Protein.- 3.3. Physical and Chemical Properties.- 3.4. Kinetics of Binding.- 3.5. Comparison of Avian N-Acetylglucosamine and Mammalian Galactose-Binding Proteins.- 4. Mannose-6-Phosphate Recognition System of Human Fibroblasts.- 4.1. Recognition of Lysosomal Enzymes-Historical.- 4.2. Recognition Signal.- 4.3. function.- 4.4. Generality.- 4.5. Binding Protein.- 5. Mannose/N-Acetylglucosamine Recognition System of Reticuloendothelial Cells.- 5.1. Clearance of Injected Lysosomal Enzymes.- 5.2. Recognition of Two Carbohydrate Termini.- 5.3. Isolation of a Binding Protein with Dual Specificity.- 5.4. Function.- 6. Fucose Recognition System of Mammalian Hepatocytes.- 7. Concluding Remarks.- 8. References.- 7 Structure and Metabolism of Connective Tissue Proteoglycans.- 1. Introduction.- 1.1. Structure of Proteoglycans and Their Polysaccharide Components.- 1.2. Mechanisms of Biosynthesis.- 1.3. Catabolic Pathways.- 2. Hyaluronic Acid.- 2.1. Structure of Hyaluronic Acid.- 2.2. Biosynthesis of Hyaluronic Acid.- 2.3. Catabolism of Hyaluronic Acid.- 3. Chondroitin Sulfate Proteoglycans.- 3.1. Structure of Chondroitin Sulfates (Linkage Units 3-10).- 3.2. Aggregates of Chondroitin Sulfate Proteoglycans.- 3.3. Biosynthesis of Chondroitin Sulfate.- 3.4. Catabolism of Chondroitin Sulfate Proteoglycans.- 4. Keratan Sulfate.- 4.1. Structure of Keratan Sulfate.- 4.2. Biosynthesis of Keratan Sulfate.- 4.3. Catabolism of Keratan Sulfate.- 5. Heparin and Heparan Sulfate Proteoglycans.- 5.1. Structure of Heparin.- 5.2. Biosynthesis of Heparin.- 5.3. Heparan Sulfate.- 5.4. Catabolism of Heparin and Heparan Sulfate.- 6. Dermatan Sulfate.- 6.1. Structure of Dermatan Sulfate.- 6.2. Biosynthesis of Dermatan Sulfate.- 6.3. Catabolism of Dermatan Sulfate.- 7. References.

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