Regulation of PTP-1 and Insulin Receptor Kinase by Fractions from Cinnamon: Implications for Cinnamon Regulation of Insulin SignallingImparl-Radosevich J.d · Deas S.a · Polansky M.M.b · Baedke D.A.c · Ingebritsen T.S.c · Anderson R.A.b · Graves D.J.a
a Department of Biochemistry and Biophysics, Iowa State University, Ames, Iowa; b Nutrient Requirements and Functions Laboratory, Beltsville Human Nutrition Research Center, US Department of Agriculture, ARS, Beltsville, Md.; c Molecular, Cellular, Developmental Biology Program, Department of Zoology and Genetics, Iowa State University, and d ExSeed Genetics, LLC, Iowa State University, Ames, Iowa, USA
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Bioactive compound(s) extracted from cinnamon potentiate insulin activity, as measured by glucose oxidation in the rat epididymal fat cell assay. Wortmannin, a potent PI 3′-kinase inhibitor, decreases the biological response to insulin and bioactive compound(s) from cinnamon similarly, indicating that cinnamon is affecting an element(s) upstream of PI 3′-kinase. Enzyme studies done in vitro show that the bioactive compound(s) can stimulate autophosphorylation of a truncated form of the insulin receptor and can inhibit PTP-1, a rat homolog of a tyrosine phosphatase (PTP-1B) that inactivates the insulin receptor. No inhibition was found with alkaline phosphate or calcineurin suggesting that the active material is not a general phosphatase inhibitor. It is suggested, then, that a cinnamon compound(s), like insulin, affects protein phosphorylation-dephosphorylation reactions in the intact adipocyte. Bioactive cinnamon compounds may find further use in studies of insulin resistance in adult-onset diabetes.
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