Differences between the endocytosis of horseradish peroxidase and its conjugate with wheat germ agglutinin by cultured fibroblasts.
A covalent conjugate of wheat germ agglutinin (WGA) with horseradish peroxidase (HRP) was used for a morphologic study of its adsorptive endocytosis by cultured human fibroblasts. Initial binding at 4 degrees C of the conjugate was observed over the entire plasma membrane, including "coated" and smooth pits. Endocytosis of HRP and the WGA-HRP conjugate was observed in lysosomes, but only the conjugate was seen in a cisterna of the Golgi apparatus (GERL), and in adjacent coated vesicles.
D000135:Acid Phosphatase / Q000378:metabolism; D002478:Cells, Cultured; D004705:Endocytosis; D005347:Fibroblasts / Q000378:metabolism* / Q000648:ultrastructure; D006056:Golgi Apparatus / Q000378:metabolism; D006735:Horseradish Peroxidase / Q000378:metabolism*; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D008854:Microscopy, Electron; D010544:Peroxidases / Q000378:metabolism*; D011107:Polylysine / Q000378:metabolism; D014909:Wheat Germ Agglutinins
D037102:Lectins; D014909:Wheat Germ Agglutinins; D011107:Polylysine; D006735:Horseradish Peroxidase; D010544:Peroxidases; D000135:Acid Phosphatase