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).

Aug 1, 2005 · Linear regression analysis indicated that the increased expression of p85/55/50, PKC-θ activity, phosphorylation levels of Ser 307 IRS-1 and JNK-1, and the proportion of MHC IIx fiber can predict 82% of the decrease in insulin sensitivity (glucose infusion rate values).

Aug 30, 2017 · Mechanisms for the increased macrophages in MPKCδKO/ApoE −/− were associated with elevated phosphorylation levels of prosurvival cell-signaling proteins, Akt and FoxO3a, with reduction of proapoptotic protein Bim associated with …

The classic view of p85 functions is that it has two roles in the PI3K complex. Binding of p85 to the ABD domain stabilizes p110, and binding of the nSH2 domain inhibits the catalytic activity of p110.

PERK lipid kinase activity is regulated in a phosphatidylinositol 3-kinase (PI3K) p85α-dependent manner. Moreover, PERK activity is essential during adipocyte differentiation.

Apr 2, 2009 · We describe that p85β bound to CD28 and to CBL with greater affinity than p85α. Moreover, deletion of p85β impaired CD28-induced intracellular events, including c-CBL and CBL-b down-regulation as well as PI3K pathway activation.

Class I isoforms are heterodimers composed of a p110 catalytic subunit and a regulatory subunit. p110α, -β, and -δ (class IA) engage p85-type regulatory subunits encoded by PIK3R1 (p85α, p55α, p50α), PIK3R2 (p85β), or PIK3R3 (p55γ).

Protein kinase C-theta (PKCθ) is a key enzyme in T lymphocytes, where it plays an important role in signal transduction downstream of the activated T cell antigen receptor (TCR) and the CD28 costimulatory receptor.

Phosphorylation of PI3K subunit p85 and PKC after SDF-1α induction was evaluated by Western blot. Results: The inhibition of PI3K or PKC signaling pathways significantly reduced SDF-1α-mediated migration of SCAPs.

Mar 15, 1996 · We now report that exposure of platelets to PKC-activating beta-phorbol myristate acetate (betaPMA) does not stimulate PI 3-Kgamma, but rather stimulates p85/PI 3-K, which associates with the cytoskeleton.