Identification of co-chaperone Cdc37 in Penaeus monodon: coordination with Hsp90 can reduce cadmium stress-induced lipid peroxidation

• Published in: Ecotoxicology and environmental safety Vol. 209; p. 111800
• Main Authors: Zhao, Chao, Peng, Chao, Wang, Pengfei, Fan, Sigang, Yan, Lulu, Qiu, Lihua
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier Inc 01.02.2021; Elsevier
• Subjects: Animals; Cadmium - metabolism; Cadmium - toxicity; Cadmium stress; Cell Cycle Proteins - metabolism; Cell division cycle 37; Heat shock protein 90; Hemolymph - metabolism; Hepatopancreas - metabolism; HSP90 Heat-Shock Proteins - genetics; HSP90 Heat-Shock Proteins - metabolism; Lipid Peroxidation - physiology; Malondialdehyde content; Penaeidae - metabolism; Penaeidae - physiology; Penaeus monodon; Superoxide dismutase enzyme; Malondialdehyde content; Cell division cycle 37; Cadmium stress; Superoxide dismutase enzyme; Penaeus monodon; Heat shock protein 90
• ISSN: 0147-6513; 1090-2414
• DOI: 10.1016/j.ecoenv.2020.111800

Cell division cycle 37 (Cdc37) is an important cytoplasmic phosphoprotein, which usually functions as a complex with heat shock protein 90 (Hsp90), to effectively reduce the damage caused by heavy metals, such as cadmium (Cd), in aquatic animals. The high toxicity of Cd in aquatic systems generally has a deleterious effect on healthy farming of shrimps. In the present study, a novel Cdc37 gene from Penaeus monodon was identified and designated as PmCdc37. Following exposure to Cd stress, the expression levels of PmCdc37 were upregulated at the transcriptional level in both the hepatopancreas and hemolymph. RNA interference and recombinant protein injection experiments were carried out to determine the function of PmCdc37 in P. monodon following Cd exposure. To clarify the correlations between PmCdc37 and PmHsp90, the respective recombinant proteins were expressed in vitro, and the ATPase activity of PmHsp90, with or without PmCdc37, was assessed. Moreover, a pull-down assay was conducted to detect the correlation between PmCdc37 and PmHsp90. After analyzing the expression patterns of PmHsp90 following Cd challenge, whether PmHsp90 can promote the ability of PmCdc37 to resist Cd stress or not was investigated. The results showed that formation of a PmHsp90/PmCdc37 complex protected shrimp against Cd stress-induced damage. Moreover, we also confirmed that PmSOD is involved in Cd stress, and that the PmHsp90/PmCdc37 complex can regulate SOD enzymatic activity. PmSOD was involved in decreasing the MDA content in shrimp hemolymph caused by Cd stress. We concluded that during exposure to Cd, the PmHsp90/PmCdc37 complex increases SOD enzyme activity, and in turn decreases the MDA content, thereby protecting shrimp against the damage caused by Cd stress. The present studies contribute to understanding the molecular mechanism underlying resistance to Cd stress in shrimp. •The full-length cDNA sequence of a novel Cdc37 gene (PmCdc37) was firstly cloned from Penaeus monodon.•PmCdc37 can interact directly with PmHsp90 to inhibit the ATPase activity of PmHsp90.•Hsp90/Cdc37 can decrease the MDA content caused by Cd stimulation by regulating SOD enzyme activity.