1;Foreword;6 2;Preface;8 3;Contents;12 4;Chapter 1: Heparan Sulfate Proteoglycan in Inflammation and Angiogenesis;14 4.1;1.1 Introduction;14 4.2;1.2 The Anti-inflammatory Function of Heparin;15 4.2.1;1.2.1 Leukocyte Trafficking and Inflammation;15 4.2.2;1.2.2 Heparin Inhibits Inflammation Mainly Through Blockage of L- and P-Selectin-Mediated Leukocyte Recruitment;16 4.2.3;1.2.3 The Anti-inflammatory Effect of Heparin Does Not Correlate with Its Anticoagulant Activity and Critically Depends on the Presence of 6-O-Sulfate of Glucosamine Residues;18 4.3;1.3 The Role of Heparan Sulfate in Leukocyte Recruitment in Inflammation;20 4.3.1;1.3.1 Generation of Endothelial- and Leukocyte-Specific Ndst1-Deficient Mice;21 4.3.2;1.3.2 Endothelial Heparan Sulfate Critically Modulates Inflammatory Responses In Vivo;22 4.3.3;1.3.3 Endothelial Heparan Sulfate Interacts with L-Selectin to Mediate Leukocyte Rolling During Inflammation;24 4.3.4;1.3.4 Endothelial Heparan Sulfate Presents Chemokines on Luminal Surfaces to Mediate Leukocyte Firm Adhesion During Inflammation;27 4.3.5;1.3.5 Endothelial Heparan Sulfate Participates in Abluminal-to-Luminal Transcytosis of Chemokine During Inflammation;28 4.3.6;1.3.6 Endothelial Heparan Sulfate Directs Intraluminal Crawling of Neutrophils by Retaining a Chemotactic Chemokine Gradient;30 4.4;1.4 The Role of Heparan Sulfate in Angiogenesis;31 4.4.1;1.4.1 Deficiency of Endothelial Ndst1 Does Not Affect Physiological Angiogenesis In Vivo;31 4.4.2;1.4.2 Deficiency of Endothelial Ndst1 Disturbs Tumor Angiogenesis In Vivo;32 4.4.3;1.4.3 Deficiency of Endothelial Ndst1 Disturbs VEGF Signaling Which Correlates with Enhanced Endothelial Apoptosis in Tumor Vasculature;33 4.5;1.5 Conclusions and Prospective;35 4.6;References;37 5;Chapter 2: Heparan Sulfate Proteoglycans in Infection;43 5.1;2.1 Primer on HSPG Biology;44 5.2;2.2 Methods for HSPG Studies in Infectious Diseases;46 5.3;2.3 HSPGs in Microbial Attachment and Internalization;47 5.3.1;2.3.1 Papillomaviruses;50 5.3.2;2.3.2 Dengue Virus;53 5.3.3;2.3.3 Listeria monocytogenes;54 5.4;2.4 HSPG as a Receptor for Virulence Factors;54 5.5;2.5 HSPGs in Tissue Tropism of Pathogens;56 5.6;2.6 Multiple Roles of HSPG in the Pathogenesis of a Single Pathogen;57 5.7;2.7 HSPG Shedding in Bacterial Pathogenesis;59 5.7.1;2.7.1 Pseudomonas aeruginosa;59 5.7.2;2.7.2 Staphylococcus aureus;60 5.7.3;2.7.3 Streptococcus pneumoniae;62 5.8;2.8 Future Perspectives;63 5.9;References;64 6;Chapter 3: Glycans in Cancer;75 6.1;3.1 Introduction;75 6.2;3.2 Glycosylation During Cancer;76 6.2.1;3.2.1 Synthesis of Glycans;76 6.2.2;3.2.2 Alteration of Glycosylation During Cancer;77 6.2.3;3.2.3 Alterations of N-Linked Glycosylation in Cancer;78 6.2.3.1;3.2.3.1 N-Linked Glycosylation;78 6.2.3.2;3.2.3.2 Biosynthesis of N-Glycans;78 6.2.3.3;3.2.3.3 N-Glycan Branching: The Role of GnT-V;79 6.2.3.4;3.2.3.4 GnT-III Versus GnT-V;80 6.2.4;3.2.4 Alterations of O-Linked Glycosylation in Cancer;81 6.2.4.1;3.2.4.1 O-Linked Glycosylation and Carcinoma Mucins;81 6.2.4.2;3.2.4.2 Biosynthesis of O-Glycans;81 6.2.4.3;3.2.4.3 Carcinoma-Associated Alterations of O-Glycans;82 6.2.4.4;3.2.4.4 Carcinoma Mucins and Cancer Progression;84 6.2.4.5;3.2.4.5 MUC1;84 6.2.4.6;3.2.4.6 MUC2;85 6.2.4.7;3.2.4.7 MUC4;85 6.2.5;3.2.5 Altered Glycosylation Affects Biology of Cancer;86 6.2.5.1;3.2.5.1 Altered Glycosylation and Metastasis;86 6.2.5.2;3.2.5.2 Cell-Cell Interactions During Metastasis;87 6.3;3.3 Conclusions and Perspective;88 6.4;References;88 7;Chapter 4: Glycosaminoglycans in Atherosclerosis and Thrombosis;94 7.1;4.1 The Vascular System;94 7.2;4.2 Atherosclerosis;96 7.3;4.3 Diabetes and Hyperglycemia;98 7.4;4.4 Glycosaminoglycans and Proteoglycans in Atherosclerosis;98 7.4.1;4.4.1 Heparan Sulfate;101 7.4.2;4.4.2 Chondroitin/dermatan Sulfate Proteoglycans;103 7.4.3;4.4.3 Hyaluronic Acid;106 7.5;4.5 Glycosaminoglycans and Thrombosis;106 7.5.1;4.5.1 Heparin;108 7.5.2;4.5.2 Heparan Sulfate;109 7.5.3;4.5.3 Dermatan Sulfate;110 7