[HTML][HTML] Inhibition of insulin signaling in endothelial cells by protein kinase C-induced phosphorylation of p85 subunit of phosphatidylinositol 3-kinase (PI3K)
Y Maeno, Q Li, K Park, C Rask-Madsen, B Gao… - Journal of biological …, 2012 - ASBMB
The regulation of endothelial function by insulin is consistently abnormal in insulin-resistant
states and diabetes. Protein kinase C (PKC) activation has been reported to inhibit insulin
signaling selectively in endothelial cells via the insulin receptor substrate/PI3K/Akt pathway
to reduce the activation of endothelial nitric-oxide synthase (eNOS). In this study, it was
observed that PKC activation differentially inhibited insulin receptor substrate 1/2 (IRS1/2)
signaling of insulin's activation of PI3K/eNOS by decreasing only tyrosine phosphorylation of …
states and diabetes. Protein kinase C (PKC) activation has been reported to inhibit insulin
signaling selectively in endothelial cells via the insulin receptor substrate/PI3K/Akt pathway
to reduce the activation of endothelial nitric-oxide synthase (eNOS). In this study, it was
observed that PKC activation differentially inhibited insulin receptor substrate 1/2 (IRS1/2)
signaling of insulin's activation of PI3K/eNOS by decreasing only tyrosine phosphorylation of …