Structure, organization, and function of glycosphingolipids in membrane

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Abstract

A large variety of glycosylation patterns in combination with different ceramide structures in glycosphingolipids provide a basis for cell type-specific glycosphingolipid pattern in membrane, which essentially reflects the composition of glycosphingolipid-enriched microdomains. Functions of glycosphingolipids as antigens, mediators of cell adhesion, and modulators of signal transduction are all based on such organization. Of particular importance is the assembly of glycosphingolipids with signal transducers and other membrane proteins to form a functional unit termed a glycosynapse, through which glycosylation-dependent cell adhesion coupled with signal transduction takes place. The microenvironment formed by interfacing glycosynapses of interacting cells plays a central role in defining phenotypic changes after cell adhesion, as occur in ontogenic development and cancer progression. These basic functional features of glycosphingolipids in membrane can also be considered roles of glycosphingolipids and gangliosides characteristic of neutrophils, myelocytes, and other blood cells. A series of sialyl fucosyl poly-N-acetylgalactosamine gangliosides without the sialyl-Lex epitope, collectively termed myeloglycan, have been shown to mediate E-selectin—dependent rolling and tethering under dynamic flow with physiologic shear stress conditions. Functional roles of myeloglycan in neutrophils during inflammatory processes are discussed

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