Binding of lectins (Con-A, lens, helix, PHA) to binding sites induced in Tetrahymena by insulin and lectins.
Concanavalin-A (Con-A) gave rise to a moderate aggregation in untreated (control) Tetrahymena pyriformis GL populations. The cells pretreated (imprinted) with insulin or lectins underwent aggregation earlier and to a greater degree than the untreated control cells. Lens lectin, although of the same sugar specificity as Con-A, was considerably less active than the latter. Helix lectin and phytohaemagglutinin (PHA), although of similar sugar specificity, accounted for a dissimilar extent of cell aggregation, in that Helix lectin was comparable in activity to Con-A. Pretreatment (imprinting) with insulin enhanced the aggregation inducing effect of those lectins which were capable of overlapping on the insulin receptor owing to similar specificity.
Csaba
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G
Department of Biology, Semmelweis University Medical School, Budapest, Hungary.
Kovács
P
P
D000818:Animals; D001665:Binding Sites; D002449:Cell Aggregation; D002478:Cells, Cultured; D003208:Concanavalin A / Q000378:metabolism; D007328:Insulin / Q000494:pharmacology*; D037102:Lectins / Q000378:metabolism*; D010835:Phytohemagglutinins / Q000378:metabolism; D037121:Plant Lectins; D011972:Receptor, Insulin / Q000378:metabolism; D011975:Receptors, Mitogen / Q000378:metabolism*; D013769:Tetrahymena pyriformis / Q000187:drug effects* / Q000378:metabolism
C038095:Helix lectin; D007328:Insulin; D037102:Lectins; D010835:Phytohemagglutinins; D037121:Plant Lectins; D011975:Receptors, Mitogen; C033619:lentil lectin; D003208:Concanavalin A; D011972:Receptor, Insulin