Redistribution and internalisation of anti-AH1e (anti-AHP)- and Concanavalin A-binding sites. 1977

J Roth, and M Wagner

The redistribution and internalisation of two different lectin-binding sites on the same cell was investigated electron microscopically on unfixed rat liver cell cultures. For these purposes an electron microscopic double labeling technique was used for visualisation of the anti-AHel-binding sites by the gold-labeled lectin and for the demonstration of the Concanavalin A-binding sites by the Concanavalin A-peroxidase technique. From the experiments it was evident that the ligand-induced redistribution of the antiAHel-binding sites effects a rearrangement of the Concanavalin A-binding sites. Both markers were found in a clustered distribution on the cell surface. Following the redistribution an internalisation of both lectin-binding sites could be observed on central and peripheral cell parts. In the lateral cell parts an accumulation of the both markers occurred on the plasma membrane.

UI MeSH Term Description Entries
D011952 Receptors, Concanavalin A Glycoprotein moieties on the surfaces of cell membranes that bind concanavalin A selectively; the number and location of the sites depends on the type and condition of the cell. Concanavalin A Binding Sites,Concanavalin A Receptors,Concanavalin A Receptor,Receptor, Concanavalin A
D011955 Receptors, Drug Proteins that bind specific drugs with high affinity and trigger intracellular changes influencing the behavior of cells. Drug receptors are generally thought to be receptors for some endogenous substance not otherwise specified. Drug Receptors,Drug Receptor,Receptor, Drug
D002460 Cell Line Established cell cultures that have the potential to propagate indefinitely. Cell Lines,Line, Cell,Lines, Cell
D002462 Cell Membrane The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells. Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D006372 Helix, Snails A genus of chiefly Eurasian and African land snails including the principal edible snails as well as several pests of cultivated plants. Helix (Snails),Snails Helix
D001665 Binding Sites The parts of a macromolecule that directly participate in its specific combination with another molecule. Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D037102 Lectins Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition. Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal

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