Premium
Permethrin, a pyrethroid insecticide, impairs insulin‐stimulated glucose uptake in C2C12 myotubes (1142.7)
Author(s) -
Kim Jonggun,
Park Yooheon,
Yoon Kyong,
Clark John,
Park Yeonhwa
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.1142.7
Subject(s) - protein kinase b , permethrin , insect growth regulator , c2c12 , pyrethroid , phosphorylation , biology , insulin , glucose homeostasis , chemistry , medicine , endocrinology , biochemistry , myogenesis , myocyte , insulin resistance , botany , pesticide , agronomy , larva
Pyrethroids are a class of insecticides structurally derived from the naturally occurring insecticides called pyrethrins originating from Chrysanthemum flowers. Based on emerging evidence that exposures to pyrethroid insecticides were linked to altered glucose homeostasis, we investigated the role of permethrin (a pyrethroid insecticide) on glucose uptake using a C2C12 myotube model. C2C12 myoblasts were differentiated into myotubes with 0, 10, and 20 μM permethrin for 8 days. Permethrin treatment significantly reduced insulin stimulated glucose uptake in this model. Further, we found that permethrin affected insulin‐stimulated phosphorylation of Protein Kinase B (AKT) without altering total AKT levels, targeted at both Serine (Ser 473) and Threonine (Thr 308) sites. Permethrin inhibited insulin‐stimulated activation of phosphoinositide‐dependent kinase (pPDK), one upstream regulator of phosphorylation on AKT at Thr 308, without influencing activation of phosphatase and tensin homolog (pPTEN). These data suggest that permethrin impaired insulin responses by influencing AKT signaling by regulating two independent pathways, upstream of PDK/Thr 308 AKT and regulator(s) of Ser 473 AKT.