Functional sites in the laminin alpha chains

被引:90
作者
Suzuki, N
Yokoyama, F
Nomizu, M [1 ]
机构
[1] Tokyo Univ Pharm & Life Sci, Sch Pharm, Lab Clin Biochem, Tokyo 1920392, Japan
[2] Hokkaido Univ, Grad Sch Environm Earth Sci, Sapporo, Hokkaido 060, Japan
基金
日本学术振兴会;
关键词
basement membrane; integrin; laminin; syndecan;
D O I
10.1080/03008200591008527
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Laminins, heterotrimers composed of a, beta, and gamma chains, are multifunctional glycoproteins present in basement membranes. Laminins, the most important component of basement membranes during basement membrane assembly in early development, are involved in various biological activities such as cell adhesion, migration, growth, differentiation, tumor metastasis, and angiogenesis. Fully 15 laminin isoforms have been identified and are tissue- and/or developmental stage-specifically expressed. Integrins, dystroglycan, syndecans, and the other several cell surface molecules are cellular receptors for laminins. The globular domains located in the N- and C-terminus of the laminin alpha chains are critical for interactions with the cellular receptors. There are highly conserved functional sites and chain-specific functional sites among the laminin a chains. Additionally, laminins are processed by specific endogenous proteases and the processing regulates laminin functions. Binding of the functional sequences in laminins to the cellular receptors triggers intracellular signaling, followed by inducing various cell activities including cell spreading and migration. Laminins possess multifunctional sequences and are key molecules that determine cell fate.
引用
收藏
页码:142 / 152
页数:11
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