Glycoproteins of myelin sheaths

被引：72

作者：

Quarles, RH

机构：

[1] NINDS,Myelin and Brain Development Section, Laboratory of Molecular and Cellular Neurobiology

[2] NIH,undefined

来源：

JOURNAL OF MOLECULAR NEUROSCIENCE | 1997年 / 8卷 / 01期

关键词：

adhesion; carbohydrate; cell-cell interactions; glycoprotein; HNK-1; myelin; oligodendrocyte; oligosaccharide; P0; protein; Schwann cell;

D O I：

10.1007/BF02736858

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

A growing number of glycoproteins have been identified and characterized in myelin and myelin-forming cells. Ln addition to the major PO glycoprotein of compact PNS myelin and the myelin-associated glycoprotein (MAG) in the periaxonal membranes of myelin-forming oligodendrocytes and Schwann cells, the list now includes peripheral myelin protein-22 (PMP-22), a 170 kDa glycoprotein associated with PNS myelin and Schwann cells (P170k/SAG), Schwann cell myelin protein (SMP), myelin/oligodendrocyte glycoprotein (MOG), and oligodendrocyte-myelin glycoprotein (OMgp). Many of these glycoproteins are members of tho immunoglobulin superfamily and express the adhesion-related HNK-1 carbohydrate epitope. This review summarizes recent findings concerning the structure and function of these glycoproteins of myelin sheaths with emphasis on the physiological roles of oligosaccharide moieties.

引用

页码：1 / 12

页数：12

共 96 条

[1] The N-terminal domain of the myelin oligodendrocyte glycoprotein (MOG) induces acute demyelinating experimental autoimmune encephalomyelitis in the Lewis rat [J].