| RRC ID |
62141
|
| 著者 |
Ogikubo O, Maeda T, Yamane T, Ohtsuka T, Ohkubo I, Takahashi S, Ohnishi S, Matsui N.
|
| タイトル |
Regulation of Zn-alpha2-glycoprotein-mediated cell adhesion by kininogens and their derivatives.
|
| ジャーナル |
Biochem Biophys Res Commun
|
| 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.
|
| 巻・号 |
252(1)
|
| ページ |
257-62
|
| 公開日 |
1998-11-9
|
| DOI |
10.1006/bbrc.1998.9614
|
| PII |
S0006291X98996140
|
| PMID |
9813179
|
| MeSH |
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
|
| IF |
2.985
|
| リソース情報 |
| ヒト・動物細胞 |
MC3T3-E1(RCB1126) |
