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Antibody against IRS-1 was purchased from Upstate (Lake Placid, NY) and antibody against phosphor IRS-1 was from Invitrogen (Carlsbad, CA).
Insulin-stimulated activation (phosphorylation) of IR, IRS-1, and Akt was assessed by immunoblotting and immunoprecipitation.
Furthermore, our data show that IRS-1 is a lysine-acetylated protein, a previously unidentified post-translational modification of IRS-1, and that increases in the level lysine acetylation of IRS-1 result in improved insulin signal transduction.
As shown in Figure 1, stably transfected cells showed marked increase in the protein detected by an anti-IRS-1 antibody, indicating that wild type IRS-1 or Arg IRS-1 was overexpressed in the transfected cardiomyocytes.
The IRS-1 phosphorylation pattern clearly indicated that blocking IGF-IR signaling strongly induced phosphorylation of IRS-1 at Y896.
IRS-1 is generally considered to be a unique substrate of IGF-IR, which phosphorylates IRS-1 at Y612.
Total IRS-1 levels were reduced.
The phospho-pentapeptide DGpYMP (Cblin) mimics Tyr612-phosphorylated IRS-1 and inhibits the Cbl-b-mediated ubiquitination and degradation of IRS-1 in vitro and in vivo.
Pregnancy may be a suitable condition to detect any abnormalities related to IRS-1 polymorphisms.
Insulin receptor substrate-1 (IRS-1) expression and tyrosine phosphorylation is decreased during pregnancy.
prolifer on the InsR/IRS-1/PI3K pathway and glucose metabolism in type 2 diabetic mice.
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