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Open Access Green as soon as Postprint is submitted to ZB.
Divergent roles of IRS (Insulin receptor substrate) 1 and 2 in liver and skeletal muscle.
Curr. Med. Chem. 24, 1827-1852 (2017)
IRS1 and IRS2 are the most important representatives of the IRS protein family and critical nodes in insulin/IGF1-signaling. Although they are quite similar in their structural and functional features they show tissue-specific differences. In this review, we outline the functions of IRS1 and IRS2 in skeletal muscle and liver with regard to their importance for metabolism, growth and differentiation. Mechanisms contributing to IRS1 and IRS2 dysregulation in disease states as well as consequences thereof are discussed. IRS1 plays the dominant role in skeletal muscle. It is crucial for normal growth and differentiation of myofibers, insulin- dependent glucose uptake and glycogen synthesis. The presence of IRS2 in skeletal muscle is negligible for insulin-induced glucose uptake and the general role of IRS2 in muscle is still not fully understood. In liver IRS1 and IRS2 are important to mediate insulindependent regulation of glucose and lipid metabolism and complement each other in the diurnal regulation thereof. IRS1 in the liver is more important for signaling in the late refeeding period, whereas IRS2 signaling is mostly dominating in the period directly after food intake and during fasting. Importantly, the expression level of IRS1 and IRS2 is different within the liver lobule, which could be an explanation for the phenomenon of selective insulin resistance. Dysregulated muscular or hepatic abundance and/or phosphorylation status of IRS1 and IRS2 are important factors in the pathogenesis of insulin resistance, type 2 diabetes and muscle wasting.
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Publication type
Article: Journal article
Document type
Review
Keywords
Insulin Receptor Substrate ; Skeletal Muscle ; Liver ; Metabolism ; Insulin Resistance ; Phosphorylation ; Degradation; Glycogen-synthase Kinase-3; Forkhead Transcription Factor; Element-binding Protein-1c; Phosphatidylinositol 3-kinase Activity; Stimulated Glucose-transport; C-reactive Protein; Signal-transduction; Serine Phosphorylation; Lipid-metabolism; Nonalcoholic Steatohepatitis
ISSN (print) / ISBN
0929-8673
e-ISSN
1875-533X
Journal
Current Medicinal Chemistry
Quellenangaben
Volume: 24,
Issue: 17,
Pages: 1827-1852
Publisher
Bentham Science Publishers
Publishing Place
Sharjah
Non-patent literature
Publications
Reviewing status
Peer reviewed