Binding of concanavalin A to secretory epidermis in the fish Blennius sanguinolentus pallas: light microscopic and ultrastructural studies.
Concanavalin A (Con A) lectin from jack bean Canavalia ensiformis DC binds to alpha-D-glucopyranosyl and alpha-D-mannopyranosyl residues of the cuticular secretions (glycocalyx) attached to apical plasma membrane in the skin surface cells of Blennius sanguinolentus. The presence of Con A positive carbohydrate components is also observed in some secretory vesicles close under the apical cell membrane and in the goblet cell secretion spread over the surface of the skin. Other lectin labeling methods might offer a new tool for the cytochemical demonstration of glycoconjugates containing sugar residues on plasmic membranes of the epithelial cells. This can provide an insight into the functional significance of the carbohydrate moieties, attributable to the specialization of the cell membranes.
D000818:Animals; D003208:Concanavalin A / Q000378:metabolism*; D004817:Epidermis / Q000378:metabolism* / Q000648:ultrastructure; D005399:Fishes / Q000378:metabolism*; D006651:Histocytochemistry; D006735:Horseradish Peroxidase; D008854:Microscopy, Electron; D011952:Receptors, Concanavalin A / Q000032:analysis*
D011952:Receptors, Concanavalin A; D003208:Concanavalin A; D006735:Horseradish Peroxidase