Cell adhesion activity for murine carcinoma cells of a wheat germ 55-kDa protein with binding affinity for animal extracellular matrix proteins.

Y Shoji, Y Aoyagi, T Kawakami, S Isemura, M Isemura

School of Food and Nutritional Sciences, University of Shizuoka, Yada, Shizuoka 422-8526, Japan.

Biochimica et biophysica acta 1999 Feb 2

filter terms:

A wheat germ 55-kDa protein was isolated by affinity chromatography with Matrigel immobilized on agarose, followed by preparative gel electrophoresis. This Matrigel-binding protein designated as WG-55 had an amino-terminal amino acid sequence which is identical to that of a putative mature form of wheat storage protein Gbl 1. WG-55 reacted with concanavalin A, indicating its glycoprotein nature as expected from the amino acid sequence of Gbl 1. As expected, similarly, WG-55 exhibited RGD-dependent cell adhesion activity for murine carcinoma cells. These data suggest that WG-55 or mature Gbl 1 protein may play a role in plant cell adhesion.

Citation

Y Shoji, Y Aoyagi, T Kawakami, S Isemura, M Isemura. Cell adhesion activity for murine carcinoma cells of a wheat germ 55-kDa protein with binding affinity for animal extracellular matrix proteins. Biochimica et biophysica acta. 1999 Feb 2;1426(3):498-504