Abstract

PREVIOUS studies on embryonic chick neural retina cells1 have demonstrated that cells in intact tissues or single cells prepared by mechanical dispersion have relatively little ability to redistribute their surface receptors into caps. In contrast, cells prepared by trypsinisation and dissociation of intact tissues were found to exhibit lateral redistribution of surface receptors even in the absence of a multivalent ligand. After 4 h culture, however, cells dissociated by trypsinisation have lost the capability for both spontaneus and lectin-induced rearrangements of surface components. Mobility of cell-surface receptors thus seems to be related to, or determined by, trypsin-labile components at the cell surface. One kind of component which seems to be trypsin labile is also important in intercellular recognition and adhesion2,3. We now report that the binding of tissue-type specific cell-surface ligands which seem to mediate recognition and adhesion causes inhibition of directed rearrangement of plant lectin receptors in the plane of the membrane.

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