Analysis of wheat germ agglutinin (WGA), Phaseolus vulgaris leucoagglutinin (PHA-L), and lens culinaris agglutinin (LCA) binding to isolated rat neocortical membrane glycoproteins and to brain tissue sections.
Different lectin transport directions--either anterograde or retrograde in tracing neuronal pathways--have been attributed to different sugar specificities of the lectins. To test this hypothesis, transmembrane neocortical glycoproteins were isolated to analyze their lectin-binding properties. The lectins tested exhibited a broad binding pattern to these glycoproteins. Arguing against the above-mentioned hypothesis, sugar residues of transmembranal glycoproteins probably are not exclusively responsible for the different transport directions observed in lectin tracing.
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Anatomische Anstalt, Universität München, F.R.G.
Schumacher
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D000818:Animals; D001921:Brain / Q000378:metabolism*; D002462:Cell Membrane / Q000378:metabolism; D002540:Cerebral Cortex / Q000378:metabolism*; D006651:Histocytochemistry; D037102:Lectins / Q000378:metabolism*; D008562:Membrane Glycoproteins / Q000302:isolation & purification / Q000378:metabolism*; D008970:Molecular Weight; D010835:Phytohemagglutinins / Q000378:metabolism*; D037121:Plant Lectins; D051381:Rats; D011975:Receptors, Mitogen / Q000378:metabolism*; D014909:Wheat Germ Agglutinins / Q000378:metabolism*
D037102:Lectins; D008562:Membrane Glycoproteins; D010835:Phytohemagglutinins; D037121:Plant Lectins; D011975:Receptors, Mitogen; D014909:Wheat Germ Agglutinins; C033619:lentil lectin; C100156:leukoagglutinins, plants