Functional sites in the laminin alpha chains.
Laminins, heterotrimers composed of alpha, 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 alpha 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.
Suzuki
Nobuharu
N
School of Pharmacy, Tokyo University of Pharmacy and Life Science, Tokyo, Japan.
Yokoyama
Fumiharu
F
Nomizu
Motoyoshi
M
D000818:Animals; D001485:Basement Membrane / Q000378:metabolism; D006801:Humans; D007797:Laminin / Q000737:chemistry* / Q000145:classification / Q000378:metabolism*; D010446:Peptide Fragments / Q000378:metabolism; D011485:Protein Binding; D020033:Protein Isoforms / Q000737:chemistry / Q000145:classification / Q000378:metabolism; D015398:Signal Transduction
D007797:Laminin; D010446:Peptide Fragments; D020033:Protein Isoforms