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    The decapeptide RNIAEIIKDI derived from domain I of the laminin B2 chain possesses neurite outgrowth-promoting activity at nanomolar concentrations for primary central and peripheral neurons. It also competes with laminin for neuronal attachment and neurite outgrowth. 

来自层粘连蛋白B2链I结构域的十肽RNIAEIIKDI在纳摩浓度下对初级中枢和周围神经元具有促进神经突生长的活性。它也与层粘连蛋白竞争神经元附着和神经突生长。

Laminins are the protein network that is the foundation for most cells and organs. They are large trimeric proteins, also in the family of glycoproteins that contain an alpha chain, a beta chain and a gamma chain which are found in five, three and three genetic variants. As a family of glycoproteins, laminins are an integral part of the structural scaffolding in almost every tissue of an organism. This makes the laminin a vital part of the maintenance and survival of the tissues. Consequently, defective laminins cause muscular dystrophy, junctional epidermolysis bullosa and defects of the kidney a defect.

Recently, publications have shown that laminins can be used to culture cells that are difficult to culture on other substrates. These trimeric glycoproteins form a similar structure to a cross, giving it a structure that has the ability to bind to other cell membrane and extracellular molecules. The three shorter arms of the laminin are particularly efficient at binding to other laminin molecules, which allows them to form larger sheets. The long arm is capable of binding to cells, which then helps anchor organized tissue cells to the membrane. These laminins are an important and biologically active part of the basal lamina, influenincing cell differentiation, migration and adhesion.