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Background：
Laminins are large molecular weight glycoproteins constituted by the assembly of three disulfide-linked polypeptides, the α, β and γ chains. The human genome encodes 11 genetically distinct laminin chains. Structurally, laminin chains differ by the number, size and organization of a few constitutive domains, endowing the various members of the laminin family with common and unique important functions. In particular, laminins are indispensable building blocks for cellular networks physically bridging the intracellular and extracellular compartments and relaying signals critical for cellular behavior, and for extracellular polymers determining the architecture and the physiology of basement membranes. Laminins are glycoproteins with both common and specific functions. One common and most important function of laminins is to interact with receptors anchored in the plasma membrane of cells adjacent to basement membranes. In doing so laminins regulate multiple cellular activities and signaling pathways. There are more than 50 theoretically possible heterotrimeric associations between all the a, β and c chains. laminins 511 and 521, are the most ubiquitous isoforms in the adult organism.
