The carboxy terminal 110 amino acid portion of the insulin receptor is important for insulin signalling to pyruvate dehydrogenase
| Autor: | Reiner Lammers, Axel Ullrich, W. Kirby Gottschalk |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Glucose uptake
medicine.medical_treatment Biophysics Pyruvate Dehydrogenase Complex Biology Transfection Biochemistry Cell Line Receptor IGF Type 1 Mice Insulin receptor substrate medicine Animals Humans Insulin Insulin-Like Growth Factor I Receptor Molecular Biology Insulin-like growth factor 1 receptor chemistry.chemical_classification 3T3 Cells Cell Biology Pyruvate dehydrogenase complex Receptor Insulin Recombinant Proteins Amino acid Kinetics Insulin receptor Glucose chemistry biology.protein |
| Zdroj: | Biochemical and Biophysical Research Communications. 189:906-911 |
| ISSN: | 0006-291X |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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