ArticleEndocrine2002
Regulation of IRS-1/SHP2 interaction and AKT phosphorylation in animal models of insulin resistance.
Article in Endocrine, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
11 citing papers in PubMed, 30 citations in OpenAlex.
- Glucose Metabolism in Burns-What Happens?International journal of molecular sciences · 2021Review
- Trilobatin ameliorates insulin resistance through IRS-AKT-GLUT4 signaling pathway in C2C12 myotubes and ob/ob mice.Chinese medicine · 2020Article
- Making sense of gut feelings in the traumatic brain injury pathogenesis.Neuroscience and biobehavioral reviews · 2019Review
- MicroRNA-1225-5p behaves as a tumor suppressor in human glioblastoma via targeting of IRS1.OncoTargets and therapy · 2018Article
- Gestational Protein Restriction Impairs Glucose Disposal in the Gastrocnemius Muscles of Female Rats.Endocrinology · 2017Article
- Neuroenergetics of traumatic brain injury.Concussion (London, England) · 2016Review
- A Cross-Species Study of PI3K Protein-Protein Interactions Reveals the Direct Interaction of P85 and SHP2.Scientific reports · 2016Article
- Developmental programming in response to intrauterine growth restriction impairs myoblast function and skeletal muscle metabolism.Journal of pregnancy · 2012Review
- Insulin-like growth factor-I-stimulated insulin receptor substrate-1 negatively regulates Src homology 2 domain-containing protein-tyrosine phosphatase substrate-1 function in vascular smooth muscle cells.The Journal of biological chemistry · 2010Article
- Insulin signalling downstream of protein kinase B is potentiated by 5'AMP-activated protein kinase in rat hearts in vivo.Diabetologia · 2005Article
- High-throughput proteomic-based identification of oxidatively induced protein carbonylation in mouse brain.Pharmaceutical research · 2003Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Insulin stimulates tyrosine kinase activity of its receptor, resulting in phosphorylation of its cytosolic substrate, insulin receptor substrate-1, which, in turn, associates with proteins containing SH2 domains, including phosphatidylinositol 3-kinase (PI 3-kinase) and the phosphotyrosine phosphatase SHP2. The regulation of these associations in situations of altered insulin receptor substrate-1 (IRS-1) phosphorylation was not yet investigated. In the present study, we investigated insulin-induced IRS-1/SHP2 and IRS-1/PI 3-kinase associations and the regulation of a downstream serine-kinase AKT/PKB in liver and muscle of three animal models of insulin resistance: STZ diabetes, epinephrine-treated rats, and aging, which have alterations in IRS-1 tyrosine phosphorylation in common. The results demonstrated that insulin-induced IRS-1/PI 3-kinase association has a close correlation with IRS-1 tyrosine phosphorylation levels, but insulin-induced IRS-1/SHP2 association showed a modulation that did not parallel IRS-1 phosphorylation, with a tissue-specific regulation in aging. The integration of the behavior of IRS-1/PI 3-kinase and with IRS-1/SHP2 associations may be important for insulin signaling downstream as AKT phosphorylation. In conclusion, the results of the present study demonstrated that insulin-induced IRS-1/SHP2 association can be regulated in insulin-sensitive tissues of animal models of insulin resistance and may have a role in the control of AKT phosphorylation, which may be implicated in the control of glucose metabolism.
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