title: Mannose-specific binding sites for horseradish peroxidase in various cells of the rat.
abstract: Mannose-specific binding sites for horseradish peroxidase (HRP) were studied in fixed sections of various tissues by a method reported previously. Liver sinusoidal cells, mast cells of lymph nodes, and alveolar macrophages of the lung and skin fibroblasts were main cell types showing mannose-specific binding of HRP. Macrophages, fibroblasts, and mast cells in the connective tissue of other organs also showed the reaction. However, macrophages of the spleen, and cultured 3T3 cells and L-cells did not give the reaction. The specificities of the binding reaction were studied by determining the approximate concentrations of competing sugars that suppressed the specific binding of HRP. It was found that the endogenous lectins in macrophages, fibroblasts, mast cells, and liver sinusoidal cells showed similar specificities toward various carbohydrates. D-Mannose and L-fucose had the highest affinity toward the lectins (competing ability for the binding of HRP). D-Mannose-6-phosphate, N-acetyl-D-glucosamine, D-glucose, D-ribose, and D-arabinose showed intermediate affinity, whereas D-xylose and D-galactose showed low affinity. Polymerized mannose in mannan and glycoproteins rich in mannose groups (invertase and ribonuclease B) showed much higher affinity to the binding sites than free mannose.
mesh_terms: D000818:Animals; D001665:Binding Sites; D002478:Cells, Cultured; D006023:Glycoproteins / Q000378:metabolism; D006735:Horseradish Peroxidase; D037102:Lectins; D008358:Mannose / Q000378:metabolism*; D051379:Mice; D010544:Peroxidases; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains
chemical_list: D006023:Glycoproteins; D037102:Lectins; D006735:Horseradish Peroxidase; D010544:Peroxidases; D008358:Mannose