Laminins in basement membrane assembly

被引:331
作者
Hohenester, Erhard [1 ]
Yurchenco, Peter D. [2 ]
机构
[1] Univ London Imperial Coll Sci Technol & Med, London, England
[2] Robert Wood Johnson Med Sch, Piscataway, NJ USA
基金
美国国家卫生研究院; 英国惠康基金;
关键词
laminin; collagen IV; nidogen; agrin; perlecan; dystroglycan; ALPHA-DYSTROGLYCAN-BINDING; CELL-ADHESION MOLECULE; GLUTAMIC-ACID RESIDUE; CRYSTAL-STRUCTURE; IV COLLAGEN; EMBRYONIC LETHALITY; INTEGRIN-BINDING; GLOBULAR DOMAINS; STRUCTURAL BASIS; ACTIN-BINDING;
D O I
10.4161/cam.21831
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The heterotrimeric laminins are a defining component of all basement membranes and self-assemble into a cell-associated network. The three short arms of the cross-shaped laminin molecule form the network nodes, with a strict requirement for one alpha, one beta and one gamma arm. The globular domain at the end of the long arm binds to cellular receptors, including integrins, alpha-dystroglycan, heparan sulfates and sulfated glycolipids. Collateral anchorage of the laminin network is provided by the proteoglycans perlecan and agrin. A second network is then formed by type IV collagen, which interacts with the laminin network through the heparan sulfate chains of perlecan and agrin and additional linkage by nidogen. This maturation of basement membranes becomes essential at later stages of embryo development.
引用
收藏
页码:56 / 63
页数:8
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