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This book presents the latest knowledge and the most recent research results on glycobiology of innate immunology. Innate immunity is the crucial part of the immunological defense system that exerts their distinct functions through binding to certain functional glycoproteins. They play a role in various human diseases and also function against microbial invaders and self-associated molecular patterns. Co-regulated expression of glycan-binding is associated with many biological components such as cellular oncotransformation, phenotype change, neuronal or embryonic development, regulation of cell division, cell–cell interaction, cell attachment, adhesion, and motility, and intracellular signaling via protein–carbohydrate or carbohydrate–carbohydrate interactions.This book opens by providing the key background on glycans in innate immunity and its mechanisms behind the Dendritic cell interactions during infection and inflammation are examined in depth, and the concluding chapteris devoted to signaling tumor immunotherapy. Up-to-date information is then presented on all aspects of glycan structure-recognizing signaling. The book should assist in the further development of new strategies against emerging infectious agents and intractable diseases.

This book presents the latest knowledge and the most recent research results on glycosphingolipid (GSL)-mediated signaling. GSLs are important constituents of the plasma membrane that exert their distinct functions through binding to certain functional proteins. They play a role in various human diseases and also function as human alloantigens. Cellular GSLs are associated with many biological functions such as cellular oncotransformation, phenotype change, neuronal or embryonic development, regulation of cell division, cell–cell interaction, cell attachment, adhesion, and motility, and intracellular signaling via protein–carbohydrate or carbohydrate–carbohydrate interactions. This book opens by providing the key background on GSL glycan–receptor interactions and mammalian GSL synthesis. Up-to-date information is then presented on all aspects of GSL-dependent signaling. Viral protein and bacterial toxin protein interactions with host cell GSLs are examined in depth, and the concluding chapter is devoted to signaling regulation. The book should assist in the further development of new strategies against emerging infectious agents and intractable diseases.

This book presents the latest knowledge and the most recent research results in the field of ganglioside biochemistry. The early chapters cover all relevant background on sialic acids and their biosynthesis, on N-glycolylneuraminic acid (Neu5Gc), which cannot be synthesized by humans, and on general aspects of ganglioside research. Ganglioside adsorption, disorders of ganglioside degradation, and the regulation of gangliosides are thoroughly discussed. A major focus of the book is the role of gangliosides in cancer. Here, the discussion encompasses, for example, the biological importance, antigenicity, and immunological actions of tumor-associated gangliosides (TAGs), the significance of different glycolipids and gangliosides as TAGs, and emerging anti-cancer vaccine strategies. The ability of sialic acids and TAGs of tumor cells to escape immunosurveillance and immunoediting also receives detailed attention. The significance of sialic acids in regulation ofthe complement system is explained, and the closing chapter focuses especially on the role of sialyl T antigen in cancer. The book will be of value for all who are interested in functional glycobiology and glycomic studies.

This book reviews recent progress in understanding of the signaling and biochemistry of GM3 ganglioside in eukaryotic cells. GM3 is the simplest of the gangliosides and the precursor of other gangliosides. It is expressed in the outer leaflet of plasma cell membranes and has roles in the recognition, interaction, binding, adhesion, and motility of cells. In addition, GM3 has been documented to have functional roles in cell migration, proliferation, senescence, and apoptosis. The full range of topics of interest are addressed in the book. The early chapters discuss the synthesis of GM3, its molecular localization in cells, and its basic function as an interacting molecule. The ways in which GM3 exerts its effects via various growth factor receptors are fully explored. Current knowledge of the part played by GM3 in health and disease is discussed in depth. For example, its roles in preventing inflammation, inhibiting tumor angiogenesis and tumor growth, and suppressing arthritis arehighlighted, and attention drawn to the significance of GM3 as a driver of impaired wound healing in diabetics. The book will be of interest to all who want a comprehensive update on research in this field.

Carbohydrate antigens on glycoconjugates of mammalian cells play crucial roles in various biological processes and are epitopes recognized by the immune system, as glycobiology has hugely been progressed during the past two decades. The book focuses on sialic acid–based xenoantigenes. In pig to human xenotransplantation, exposure of pig organs to human blood results in hyper acute rejection (HAR), caused by differences in carbohydrate epitopes between human and pig vascular endothelia. Although Gal-antigen as major antigen was eliminated, the remaining non-Gal antigens are considered to be xenoantigens. Sialosyl-Tn or Hanganutziu-Deicher (HD), are non-Gal antigens specific to natural antibodies in human. To overcome rejection responses such as HAR, studies of genes involved in carbohydrate antigens, causing xenoantigenicity, are necessary. Knowledge of pig glycosyltransferases are also useful to apply to xenoantigen masking or identification of the xenoantigenic sialylglycan(s). In the first chapter the screening for pig glycosyltransferase genes for xenoantigens is presented. In the chapter II to IV the cloning, characterization, and investigation of the regulatory mechanism of the pig CMAH gene in NeuGc biosynthesis is shown. Lastly, the effects of an alteration of pig glycosylation patterns on human serum-mediated cytotoxicity, caused by human sialyltransferases including hST6GalNAc IV is presented.