insulin receptor substrate-1

insulin receptor substrate-1

a cytoplasmic protein that is a direct substrate of the activated insulin receptor kinase. Insulin exposure results in its rapid phosphorylation at multiple tyrosine residues. Its phosphorylated sites associate with high affinity to certain cellular proteins. IRS-1 thus acts as an adaptor molecule that links the receptor kinase to various cellular activities regulated by insulin. IRS-1 is also phosphorylated after stimulation by insulinlike growth factor-1 and several interleukins.

in·su·lin re·cep·tor sub·strate-1

(IRS-1) (in'sŭ-lin rĕ-sep'tŏr sŭb'strāt)
A cytoplasmic protein that is a direct substrate of activated insulin receptor kinase. Insulin exposure results in its rapid phosphorylation at multiple tyrosine residues. Its phosphorylated sites associate with high affinity to certain cellular proteins. IRS-1 thus acts as an adaptor molecule that links the receptor kinase to various cellular activities regulated by insulin. IRS-1 is also phosphorylated after stimulation by insulinlike growth factor-1 and several interleukins.
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We studied glucose transporter-4 (GLUT-4) insulin receptor substrate-1 (IRS-1), Insulin receptor (IR), Phosphoenolpyrovate carboxykinase (PEPCK), Sterol regulatory element binding protein-1c (SREBP-1c), Fatty acid synthase (FAS), Peroxisome proliferator-activated receptor-a (PPAR-a), Peroxisome proliferator-activated receptor-g (PPAR-g) and tumor necrosis factor-a (TNF-a) in hepatic, skeletal muscle and adipose tissue.
The excess of FFA leads per se to insulin-resistance by inactivation of key enzymes such as pyruvate dehydrogenase (PDH) or by decreasing glucose transport activity, which may be a consequence of altered insulin signaling through decreased insulin receptor substrate-1 (IRS-1) associated PI3 kinase activity [27].
Moreover, CPEC and its two triterpenoids not only enhanced glucose uptake in an insulin-independent manner, but also restored insulin-mediated protein kinase B (Akt) phosphorylation by reducing the activation of IKK[beta] and regulating insulin receptor substrate-1 (IRS-1) serine/tyrosine phosphorylation.
C-reactive protein induces phosphorylation of insulin receptor substrate-1 on Ser307 and Ser612 in L6 myocytes thereby impairing the insulin signalling pathway that promotes glucose transport.
In fact, the insulin receptor substrate-1 Gly972Arg variant is widely studied in terms of its relationship to diabetes mellitus.
29] have shown that tyrosine nitration of the insulin receptor substrate-1 reduces insulin stimulated glucose uptake.
These effects were associated with significant reduction in IGF-I secretion; inhibition of IGF-I-induced cell cycle progression and insulin receptor substrate-1 (IRS-1) tyrosine phosphorylation, along with an increase in sub-G1 peak by apigenin.
Insulin stimulates PKCzeta-mediated phosphorylation of insulin receptor substrate-1 (IRS-1).
Muscular Insulin receptor, Insulin receptors phosphorylation, insulin receptor substrate-1, serine/thereonine kinase.
Insulin receptor substrate-1 gene mutations in NIDDM; implications for the study of polygenic disease.
In tissue from people with Alzheimer's disease and mild cognitive impairment (MCI), researchers found that changes to a protein called insulin receptor substrate-1 (IRS-1 pS636/639 and pS616) in brain cells were linked to the severity of memory impairments regardless of age, sex, diabetes history, or apolipoprotein E (APOE) gene status.

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