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Cadmium favors F-actin depolymerization in rat renal mesangial cells by site-specific, disulfide-based dimerization of the CAP1 protein.

Arch Toxicol.. 2017-12; 
Liu Y, Xiao W, Shinde M, Field J, Templeton DM.
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… Anti-cofilin (Ab134963) was from abcam (Cambridge, MA). Anti-His antibody (H-3 sc-8036) for Western blotting was purchased from Santa Cruz (Dallas, TX). Anti-His antibody (A00186) for immu- nofluorescent staining was purchased from GenScript (Pis- cataway, NJ) …

摘要

Cadmium is a toxic metal that produces oxidative stress and has been shown to disrupt the actin cytoskeleton in rat renal mesangial cells (RMC). In a survey of proteins that might undergo Cd2+-dependent disulfide crosslinking, we identified the adenylyl cyclase-associated protein, CAP1, as undergoing a dimerization in response to Cd2+ (5-40 µM) that was sensitive to disulfide reducing agents, was reproduced by the disulfide crosslinking agent diamide, and was shown by site-directed mutagenesis to involve the Cys29 residue of the protein. Reactive oxygen species are not involved in the thiol oxidation, and glutathione modulates background levels of dimer. CAP1 is known to enhance cofilin's F-actin severing acti... More

关键词

Actin filaments; CAP1 protein; Cadmium; Cofilin; Mesangial cell