Functional sites in the laminin alpha chains
Functional sites in the laminin alpha chains
复制标题
DOI:
10.1080/03008200591008527
复制
发表时间:
2005-01-01
影响因子:
2.9
通讯作者:
Nomizu, M
中科院分区:
文献类型:
--
作者:
Suzuki, N;Yokoyama, F;Nomizu, M
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.