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- W2135036700 endingPage "152" @default.
- W2135036700 startingPage "142" @default.
- W2135036700 abstract "Laminins, heterotrimers composed of α, β, and γ 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 α 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." @default.
- W2135036700 created "2016-06-24" @default.
- W2135036700 creator A5000257639 @default.
- W2135036700 creator A5033456857 @default.
- W2135036700 creator A5090371447 @default.
- W2135036700 date "2005-01-01" @default.
- W2135036700 modified "2023-10-11" @default.
- W2135036700 title "Functional Sites in the Laminin Alpha Chains" @default.
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