Inhibition of insulin receptor binding by dimethyl sulfoxide |
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Authors: | Emmanuel Van Obberghen Pierre De Meyts Jesse Roth |
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Affiliation: | Diabetes Branch, National Institute of Arthritis, Metabolism and Digestive Diseases, National Institutes of Health, Bethesda MD 20014 U.S.A. |
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Abstract: | Little is known of the effects of the solvent on hormone-receptor interactions. In the present study the effect of the polar solvent dimethyl sulfoxide on the binding of insulin to its surface receptors on cultured human lymphocytes of the IM-9 line was investigated. At concentrations exceeding 0.1% (v/v), dimethyl sulfoxide produced a dose-related inhibition of 125I-labeled insulin binding. Insulin binding was totally abolished in 20% dimethyl sulfoxide. This inhibition was immediately present and was totally reversible. Analysis of the data of binding at steady state indicated that the decrease in binding of 125I-labeled insulin was due to a reduced affinity of the insulin receptor without noticeable change in the concentration of receptor sites. Kinetic studies showed that the decreased affinity could largely be accounted for by a decreased association rate constant; effects on dissociation and negative cooperativity of the insulin receptor were affected to a much lesser extent. |
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Keywords: | Insulin Receptor binding Dimethyl sulfoxide (Negative cooperativity) bound/free total concentration of receptor sites per cell average affinity limiting high affinity state limiting low affinity state |
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