Target Size for a Fibronectin-Cell Adhesion System Determined by the X-ray Inactivation Method

Cell Structure and Function

Katsumi Kobayashi²  Yasunori Miyamoto¹  Akinari Yokoya¹  Shozo Ishizaka¹ 

[1] Institute of Biological Sciences, University of Tsukuba;Photon Factory, National Laboratory for High Energy Physics

关键词: fibronectin;    target size;    X-ray inactivation method;    cell adhesion;   

DOI  :  10.1247/csf.16.17

学科分类：分子生物学，细胞生物学和基因

来源: Japan Society for Cell Biology

【 摘 要 】

References(25)In order to elucidate the mechanism of cell adhesion, the size of the functional site, both in the fibronectin molecule and in the mouse fibroblast cell, responsible for cell adhesion activity, was determined. The size was assumed to be equivalent to the target size, that can be determined from the X-ray inactivation dose. The target size of the cell-binding site in the fibronectin molecule was 32 kdalton. The molecular weight was much larger than that of the tripeptide, which has been reported to be the minimum peptides having a cell-binding activity. This suggests that submolecular regions in fibronectin other than the tripeptide are necessary for cell adhesion. The target size in the cell responsible for the adhesion to the fibronectin-coated surface was 4300 kdalton. The large molecular weight of the target could be explained by assuming that a complex protein system is involved in the cell-adhesion process in the cell.

【 授权许可】

Unknown