THE DYNAMICS OF UPTAKE, TRANSPORT AND CLEARANCE OF HORSERADISH PEROXIDASE (HRP) CONJUGATES OF CHOLERA TOXIN (CTHRP) AND WHEAT GERM. AGGLUTININ (WGHRP)

1982 ◽  
Vol 41 (3) ◽  
pp. 350 ◽  
Author(s):  
X. -C. S. Wan ◽  
J. Q. Trojanowski ◽  
J. O. Gonatas
Keyword(s):  
Horseradish Peroxidase ◽  
Cholera Toxin ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ

scholarly journals The use of lectins and cholera toxin for the detection of surface carbohydrates of cultured neurons and neuroblastoma.

1979 ◽  
Vol 27 (8) ◽  
pp. 1165-1166 ◽  
Author(s):  
N K Gonatas
Keyword(s):  
Horseradish Peroxidase ◽  
Cholera Toxin ◽  
Wheat Germ Agglutinin ◽  
Wheat Germ ◽  
Neuroblastoma Cells ◽  
Cultured Neurons ◽  
Plasma Membrane Receptor ◽  
Surface Carbohydrates ◽  
Adsorptive Endocytosis

Conjugates of horseradish peroxidase with the lectins ricin (d-galactose), wheat germ agglutinin (N-acetylglucosamine), phytohemagglutinin (N-acetylgalactosamine), and with cholera toxin (GM1 ganglioside) were used for a cytochemical detection of corresponding termin al carbohydrates, or glycolipids on cell surfaces of cultured neurons and neuroblastoma cells. Cells were labeled at 4 degrees C with the above ligands and their adsorptive endocytosis was studied after incubations at 37 degrees C in a medium free of ligand. Peroxidase was detected by the method of Graham and Karnovsky (J. Histochem. Cytochem. 14:291, 1966). Lectins and cholera toxin underwent endocytosis in cisternae and vesicles of GERL (Golgi-Endoplasmic Reticulum-Lysosome). We suggest that GERL is the primary ercipieint of adsorptively endocytosed plasma membrane "receptor"-ligand complexes which are thus degraded or possibly reutilized (recycling). Wheat germ agglutinin-horseradish peroxidase conjugates used in vivo for studies of retrograde axonal transport were significantly more sensitive than free horseradish peroxidase.

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