PMID: 6989266Mar 1, 1980Paper

Effects of wheat germ agglutinin on insulin binding and insulin sensitivity of fat cells

The American Journal of Physiology
J N Livingston, B J Purvis


The plant lectin (wheat germ agglutinin, WGA) produces several alterations in the ability of fat cells to bind and respond to insulin. Although WGA markedly stimulated glucose oxidation, it caused only a modest stimulation of glucose transport. WGA (0.25-20 micrograms/ml) increased the binding of insulin by adipocytes, apparently by increasing the binding affinity of the insulin receptor. With low WGA concentrations (0.25-2.5 micrograms/ml), the elevation in binding was accompanied by an increase in the sensitivity of the adipocytes to insulin stimulation of glucose transport. However, the sensitivity of these cells to vitamin K5 and H2O2 was not altered. With higher WGA concentrations (5-20 micrograms/ml), stimulation of the glucose transport system by insulin, vitamin K5, or H2O2 was markedly inhibited, an effect that is reversed by the addition of ovomucoid. These findings suggest that low WGA concentrations increase the affinity of the insulin receptor and the insulin sensitivity of the cells. At higher concentrations, the lectin appears to act at another site(s) to inhibit the activation of the transport system by insulin or other agents.


Jun 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·M N Krupp, J N Livingston
Sep 1, 1978·Proceedings of the National Academy of Sciences of the United States of America·C R KahnJ S Flier
Jun 1, 1976·The Journal of Clinical Investigation·M P Czech
Jul 12, 1976·Biochemical and Biophysical Research Communications·J M Olefsky
Oct 27, 1975·Biochemical and Biophysical Research Communications·P De Meyts, J Roth
Feb 1, 1973·Proceedings of the National Academy of Sciences of the United States of America·P Cuatrecasas, G P Tell
Feb 28, 1973·Biochimica Et Biophysica Acta·M P Czech, W S Lynn

Related Concepts

Fat Pad
Dose-Response Relationship, Drug
Glucose, (beta-D)-Isomer
Insulin Receptor beta Subunit
Animal Lectins
Plant Lectins

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