Regulation of Zn-alpha2-glycoprotein-mediated cell adhesion by kininogens and their derivatives

Biochem Biophys Res Commun. 1998 Nov 9;252(1):257-62. doi: 10.1006/bbrc.1998.9614.

Abstract

MC3T3-E1 (mouse osteoblast-like) cells adhered to a tissue culture plate coated with human Zn-alpha2-glycoprotein (Znalpha2gp). The adhesion of MC3T3-E1 cells to Znalpha2gp was inhibited by synthetic peptides such as RGDS and ELRGDV, and by antibody against vitronectin receptor. These findings suggested that the RGD region of Znalpha2gp interacts with the vitronectin receptor (alphavbeta3) on the MC3T3-E1 cell surface. Furthermore, we found that the common heavy chain of both HMW- and LMW-kininogens accelerated the Znalpha2gp-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, N334AEVYVVPWEKKIYPTVN351 accelerated in a dose-dependent manner the Znalpha2gp- 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 3T3 Cells
  • Amino Acid Sequence
  • Animals
  • Blood Proteins / physiology*
  • Cell Adhesion / drug effects
  • Cell Adhesion / physiology*
  • Flow Cytometry
  • Humans
  • Kinetics
  • Kininogens / chemistry
  • Kininogens / pharmacology
  • Kininogens / physiology*
  • Macromolecular Substances
  • Mice
  • Molecular Sequence Data
  • Peptide Fragments / chemical synthesis
  • Peptide Fragments / chemistry
  • Peptide Fragments / pharmacology*
  • Protein Conformation
  • Vitronectin / physiology
  • alpha-2-HS-Glycoprotein

Substances

  • AHSG protein, human
  • Ahsg protein, mouse
  • Blood Proteins
  • Kininogens
  • Macromolecular Substances
  • Peptide Fragments
  • Vitronectin
  • alpha-2-HS-Glycoprotein