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Studies on the localization and activities of Concanavalin-A-reactive glycoproteins on the cell surface of sea urchin embryos

✍ Scribed by Matsumoto, Emiko ;Tonegawa, Yasuto ;Ishihara, Katsutoshi

Publisher
John Wiley and Sons
Year
1984
Tongue
English
Weight
701 KB
Volume
232
Category
Article
ISSN
0022-104X

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✦ Synopsis

Inhibitory effects of Concanavalin A (con A) on sea urchin development were analyzed. Con A inhibited gastrulation at lower concentrations and disturbed cell association a t higher concentrations. This cell-dissociating effect was due to the binding of con A to specific sugar residues on the cell surface. By autoradiographic study on sectioned embryos, con A binding sites were shown to be mostly localized on cell membranes. The grain number increased during development, especially at the time of hatching, when functional cell association is known to be established. By dissociating embryos with Ca-,Mg-deficient artificial seawater (CMF-SW), con A was shown to react with cell aggregation factor and with surfaces of dissociated cells. These results suggest that con-A-reactive materials on the cell surface are directly involved in the cell adhesion mechanism of sea urchin embryos.

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