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Food Chem Toxicol. 2017 Nov;109(Pt 1):95-101. doi: 10.1016/j.fct.2017.08.046. Epub 2017 Sep 1.

Permethrin decreased insulin-stimulated AKT phosphorylation dependent on extracellular signal-regulated kinase-1 (ERK), but not AMP-activated protein kinase α (AMPKα), in C2C12 myotubes.

Author information

1
Department of Food Science, United States.
2
Department of Veterinary and Animal Sciences, United States.
3
Department of Mathematics and Statistics, University of Massachusetts, Amherst, MA, 01003, United States.
4
Department of Food Science, United States. Electronic address: ypark@foodsci.umass.edu.

Abstract

Previously 10 μM permethrin (38.7% cis and 59.4% trans isomers), a pyrethroid insecticide widely used in agriculture and household products for pest control, was reported to reduce insulin-stimulated glucose uptake and phosphorylation of protein kinase B (p-AKT) in C2C12 mouse myotubes. The underlying mechanisms on how permethrin decreases insulin-stimulated AKT phosphorylation, however, are unknown. Thus, the goal of this study was to determine the possible mechanism(s) through which permethrin reduced insulin-stimulated AKT phosphorylation in C2C12 myotubes. Permethrin treatment, at 10 μM, decreased insulin-stimulated membrane glucose transporter type 4 (GLUT4) and AKT phosphorylation, and increased insulin receptor substrate 1 (IRS1) Ser307 phosphorylation in the presence of insulin. The inactivation of AKT by permethrin was independent of AMPKα. ERK inactivation by U0126, however, restored insulin-stimulated AKT phosphorylation, which was decreased by permethrin treatment. These results suggest that permethrin decreased insulin-stimulated AKT phosphorylation via ERK activation, but not by AMPKα inactivation.

PMID:
28866332
DOI:
10.1016/j.fct.2017.08.046
[Indexed for MEDLINE]

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