Abstract
The signalling pathways by which insulin triggers protein synthesis were studied using an antisense strategy to deplete ERK1/ERK2 and rapamycin to inhibit the p70S6K pathway. The results indicated that ERK1/ERK2 principally regulated the amount of the protein synthesis machinery available in the cell while the p70S6K pathway contributed to modulating its activation in response to insulin. ERK1/ERK2 also mediated in a small proportion of insulin-stimulated protein synthesis which included the induction of c-fos protein. When c-fos induction was blocked the majority of insulin-stimulated protein synthesis still occurred and thus did not require transcriptional regulation of c-fos or its targets.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adipocytes / metabolism*
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Animals
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
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Cell Line
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Hypoglycemic Agents / metabolism
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Hypoglycemic Agents / pharmacology*
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Insulin / metabolism
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Insulin / pharmacology*
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Mice
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Mitogen-Activated Protein Kinase 1
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Mitogen-Activated Protein Kinase 3
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Mitogen-Activated Protein Kinases*
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Protein Biosynthesis
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Ribosomal Protein S6 Kinases / metabolism*
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Signal Transduction / drug effects*
Substances
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Hypoglycemic Agents
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Insulin
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Ribosomal Protein S6 Kinases
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Calcium-Calmodulin-Dependent Protein Kinases
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Mitogen-Activated Protein Kinase 1
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Mitogen-Activated Protein Kinase 3
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Mitogen-Activated Protein Kinases