Structure, organization, and function of glycosphingolipids in membrane
Structure, organization, and function of glycosphingolipids in membrane
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DOI：
10.1097/00062752-200301000-00004
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发表时间：
2003-01-01
影响因子：
3.2
通讯作者：
Hakomori, S
中科院分区：
文献类型：
--
作者：
Hakomori, S
大量的糖基化模式与鞘糖脂中不同的神经酰胺结构相结合，为膜中细胞类型特异性鞘糖脂模式提供了基础，这基本上反映了富含鞘糖脂的微结构域的组成。鞘糖脂作为抗原、细胞粘附介质和信号转导调节剂的功能都基于这种组织。特别重要的是鞘糖脂与信号转导子和其他膜蛋白的组装，以形成称为糖突触的功能单元，通过糖突触发生糖基化依赖性细胞粘附与信号转导。通过相互作用的细胞的界面糖突触形成的微环境在定义细胞粘附后的表型变化中起着核心作用，如发生在个体发育和癌症进展中。鞘糖脂在膜中的这些基本功能特征也可以被认为是中性粒细胞、髓细胞和其他血细胞的鞘糖脂和神经节苷脂的特征性作用。一系列不含唾液酸-Le（x）表位的唾液酸岩藻糖基聚-N-乙酰半乳糖胺神经节苷脂，统称为髓聚糖，已显示在具有生理剪切应力条件的动态流动下介导E-选择素依赖性滚动和束缚。中性粒细胞在炎症过程中髓聚糖的功能作用进行了讨论。(C)2003年利平科特威廉姆斯威尔金斯公司
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-Le(x) 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. (C) 2003 Lippincott Williams Wilkins, Inc.