Abstract
MC3T3-E1 (mouse osteoblast-like) cells adhered to a tissue culture plate coated with human Zn-α2-glycoprotein (Znα2gp). The adhesion of MC3T3-E1 cells to Znα2gp was inhibited by synthetic peptides such as RGDS and ELRGDV, and by antibody against vitronectin receptor. These findings suggested that the RGD region of Znα2gp interacts with the vitronectin receptor (αvβ3) on the MC3T3-E1 cell surface. Furthermore, we found that the common heavy chain of both HMW- and LMW-kininogens accelerated the Znα2gp-mediated MC3T3-E1 cell adhesion. Among the three domains of the common heavy chain of both kininogens, domain 3 promoted the cell adhesion by up to 200%. Among the nine synthetic peptides covering domain 3, the peptide, N334AEVYVVPWEKKIYPTVN351accelerated in a dose-dependent manner the Znα2gp- and vitronectin (VN)-mediated MC3T3-E1 cell adhesion. These findings suggested that a defined region of domain 3 is responsible for the acceleration of cell adhesion.
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