Inhibition of PPARα attenuates vimentin phosphorylation on Ser-83 and collapse of vimentin filaments during exposure of rat Sertoli cells in vitro to DBP

• DBP leads to the collapse of vimentin filament network, while GW6471 (inhibitor of PPARα) pretreatment could attenuate this effect.
• DBP upregulates soluble vimentin in a time dependent manner, while GW6471 pretreatment does not upregulate soluble vimentin.
• PPARα is activated by DBP in Sertoli cells, while GW6471 inhibits the activity of PPARα.
• PPARα is one of the factors which lead to the phosphorylation of vimentin in Sertoli cells after DBP exposure, and phosphorylation of vimentin partially affects the solubility/assembly of vimentin.

Dibutyl phthalate (DBP) is a peroxisome proliferator which can lead to germ cell loss from Sertoli cells. Collapse of vimentin filaments occurs in Sertoli cells after DBP exposure. Peroxisome proliferator activated receptor α (PPARα) is a key receptor which could be activated by DBP. The role of PPARα in this process was investigated. Results showed that, PPARα was activated in DBP-exposed Sertoli cells, GW6471 inhibited the activity of PPARα, phosphorylation level of vimentin and concentration of soluble vimentin was higher in DBP-treated Sertoli cells than GW6471+DBP-treated cells. These results suggest that PPARα directly or indirectly mediated phosphorylation of vimentin on Ser 83, and PPARα may play an important role in regulating the reorganization of vimentin filaments during exposure of Sertoli cells to DBP.