| In vivo differential effects of fasting, re-feeding, insulin and insulin stimulation time course on insulin signaling pathway components in peripheral tissues. | |
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MedLine Citation:
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PMID: 20833131 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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BACKGROUND: Components of the insulin receptor signaling pathway are probably some of the best studied ones. Even though methods for studying these components are well established, the in vivo effects of different fasting regimens, and the time course of insulin receptor phosphorylation and that of its downstream components in insulin-sensitive peripheral tissues have not been analyzed in detail. RATIONALE: When assessing insulin signaling, it may be beneficial to drive insulin levels as low as possible by performing an overnight fast before injecting a supra-physiological dose of insulin. Recent studies have shown however that 5 or 6 h fast in mice is sufficient to assess physiological responses to insulin and/or glucose in glucose tolerance tests, insulin tolerance tests and euglycemic hyperinsulinemic clamp studies. Moreover, mice are nocturnal feeders, with ∼70% of their daily caloric intake occurring during the dark cycle, and their metabolic rate is much higher than humans. Therefore, an overnight fast in mice is closer to starvation than just food withdrawal. Thus our aim was to assess insulin signaling components from the insulin receptor to downstream targets IRS1, Akt/PKB, GSK3, Erk1/2 and ribosomal protein S6 in muscle, liver and adipose tissue in 5 h versus 16 h (overnight) fasted mice, and the time course (0-30 min) of these phosphorylation events. We also assessed whether re-feeding under 5 h and 16 h fasting conditions was a more robust stimulus than insulin alone. CONCLUSIONS: Our study determines that a short food withdrawal from mice, for a period of 5 h, results in a similar insulin-stimulated response in phosphorylation events as the long overnight fast, presenting a more physiological experimental set up. We also demonstrate that in vivo, insulin-stimulated phosphorylation of its signaling components is different between different peripheral tissues, and depending on the tissue(s) and protein(s) of interest, an appropriate time course should be chosen. |
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Authors:
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Abdelali Agouni; Carl Owen; Alicja Czopek; Nimesh Mody; Mirela Delibegovic |
Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-09-15 |
Journal Detail:
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Title: Biochemical and biophysical research communications Volume: 401 ISSN: 1090-2104 ISO Abbreviation: Biochem. Biophys. Res. Commun. Publication Date: 2010 Oct |
Date Detail:
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Created Date: 2010-10-11 Completed Date: 2010-11-30 Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 0372516 Medline TA: Biochem Biophys Res Commun Country: United States |
Other Details:
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Languages: eng Pagination: 104-11 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier Inc. All rights reserved. |
Affiliation:
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IBES, College of Life Sciences and Medicine, Integrative Physiology, University of Aberdeen, Aberdeen AB242TZ, UK. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adipose Tissue
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drug effects,
metabolism* Animals Blood Glucose / drug effects Eating Fasting / blood, metabolism* Glycogen Synthase Kinase 3 / metabolism Insulin / metabolism*, pharmacology Insulin Receptor Substrate Proteins / metabolism Liver / drug effects, metabolism* Male Mice Mice, Inbred C57BL Mitogen-Activated Protein Kinase 1 / metabolism Mitogen-Activated Protein Kinase 3 / metabolism Muscle, Skeletal / drug effects, metabolism* Phosphorylation Proto-Oncogene Proteins c-akt / metabolism Receptor, Insulin / metabolism* Ribosomal Protein S6 / metabolism Signal Transduction |
| Grant Support | |
ID/Acronym/Agency:
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//Biotechnology and Biological Sciences Research Council; //British Heart Foundation |
| Chemical | |
Reg. No./Substance:
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0/Blood Glucose; 0/Insulin Receptor Substrate Proteins; 0/Irs1 protein, mouse; 0/Ribosomal Protein S6; 11061-68-0/Insulin; EC 2.7.10.1/Receptor, Insulin; EC 2.7.11.1/Proto-Oncogene Proteins c-akt; EC 2.7.11.24/Mitogen-Activated Protein Kinase 1; EC 2.7.11.24/Mitogen-Activated Protein Kinase 3; EC 2.7.11.26/Glycogen Synthase Kinase 3 |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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