Concanavalin A and ricinus communis receptor sites in normal human oral mucosa.
Fluorescein conjugates of concanavalin A (Con-A) and Ricinus communis fraction 120 (RCA120) were shown to bind to the cell surfaces of basal and spinous cell layers in oral buccal mucosa. Palatal epithelium showed distinct binding to basal and spinous cells; cell membranes in the granular layer occasionally bound Con-A and always RCA120. The ultrastructural localization of Con-A binding sites on exfoliated buccal cells was detected by the Con-A peroxidase staining method. The Con-A receptors were seen on the cell surface in association with the outer leaflet of the plasma membrane. The reaction products appeared as a homogeneous, electron-dense layer containing irregularly distributed globules.
D001485:Basement Membrane / Q000648:ultrastructure; D001665:Binding Sites; D002462:Cell Membrane / Q000648:ultrastructure; D002610:Cheek; D003208:Concanavalin A / Q000378:metabolism*; D005260:Female; D006801:Humans; D008297:Male; D009061:Mouth Mucosa / Q000378:metabolism / Q000648:ultrastructure*; D037121:Plant Lectins; D010947:Plants, Toxic; D011952:Receptors, Concanavalin A; D011955:Receptors, Drug; D012278:Ricinus / Q000378:metabolism*
D037121:Plant Lectins; D011952:Receptors, Concanavalin A; D011955:Receptors, Drug; D003208:Concanavalin A