Complex carbohydrate-lectin interaction at the interface: a model for cellular adhesion. II. Reactivity of both the oligosaccharide chain and sugar-binding domain of a glycoprotein lectin

Chakrabarti, Abhijit and Podder, Sunil K (1992) Complex carbohydrate-lectin interaction at the interface: a model for cellular adhesion. II. Reactivity of both the oligosaccharide chain and sugar-binding domain of a glycoprotein lectin. In: Journal of Molecular Recognition, 5 (2). pp. 69-73.

Preview

PDF page63.pdf Download (463kB)

Abstract

We describe studies of a new model cell adhesion system involving liposomes bearing lectins and the glycosphingolipid, asialomonosialoganglioside (asialoGM1). The model provides a simple analysis of experimental data to elucidate the mechanism of heterophilic cell-cell adhesion mediated by multiple protein-carbohydrate interactions. Phospholipid vesicles bearing the fatty acid conjugate of a glycoprotein lectin from Ricinus communis (RCAI vesicle) are shown to react with vesicles bearing the fatty acid conjugate of Concanavalin A (Con A) and asialoGM1 (Con A vesicle). The kinetics of aggregation and monosaccharide-induced disaggregation of the two types of vesicles were followed by monitoring the time-dependent change in turbidity. Depending on the surface density of the asialoGM1, 40-60% of the resulting precipitin complex was dissociable only in the presence of both RCAI-specific galactose and Con A-specific ?-methyl-D-mannoside. Results indicate simultaneous participation of both the saccharide-binding domain and carbohydrage sequence of RCAI, a model cell adhesion molecule, to stabilize the encounter complex by two types of interactions. These findings support the possibility of stable cell-cell adhesion in vivo occurring via interactions between cell adhesion molecules on apposing cell-surface membranes.

Item Type:	Journal Article
Publication:	Journal of Molecular Recognition
Publisher:	John Wiley & Sons, Ltd.
Additional Information:	The copyright belongs to John Wiley & Sons Ltd.
Department/Centre:	Division of Biological Sciences > Biochemistry
Date Deposited:	21 Nov 2005
Last Modified:	19 Sep 2010 04:21
URI:	http://eprints.iisc.ac.in/id/eprint/4045

Actions (login required)

View Item