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- W2040771825 abstract "Insulin-like growth factor 1 (IGF-1) had no detectable effect on pyruvate dehydrogenase (PDH) in NIH 3T3 cells that stably overexpressed normal human IGF-1 receptors. Insulin stimulated PDH activity 3-4--fold in cells that overexpressed normal human insulin receptors, but not in cells expressing TMI receptors, composed of the ligand binding domain of the insulin receptor coupled to the transmembrane and intracellular components of the IGF-1 receptor, or CEX receptors, in which the carboxy terminal 110 amino acid portion of the insulin receptor was exchanged for the corresponding portion of the IGF-1 receptor. In contrast, insulin stimulated glucose uptake in the control cell line and in each of the chimeric receptor-expressing lines with similar dose-response characteristics. These findings suggest the carboxy terminal portion of the IR may play a role in mediating the stimulation of PDH activity." @default.
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- W2040771825 date "1992-12-01" @default.
- W2040771825 modified "2023-10-14" @default.
- W2040771825 title "The carboxy terminal 110 amino acid portion of the insulin receptor is important for insulin signalling to pyruvate dehydrogenase" @default.
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- W2040771825 doi "https://doi.org/10.1016/0006-291x(92)92289-a" @default.
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