These authors contributed equally to this work
Hyperphosphorylation of microfilament-associated proteins is involved in microcystin-LR-induced toxicity in HL7702 cells
Article first published online: 21 FEB 2014
Copyright © 2014 Wiley Periodicals, Inc.
How to Cite
Zeng, J., Tu, W.-w., Lazar, L., Chen, D.-n., Zhao, J.-s. and Xu, J. (2014), Hyperphosphorylation of microfilament-associated proteins is involved in microcystin-LR-induced toxicity in HL7702 cells. Environ. Toxicol.. doi: 10.1002/tox.21974
- Article first published online: 21 FEB 2014
- Manuscript Accepted: 9 FEB 2014
- Manuscript Revised: 5 FEB 2014
- Manuscript Received: 26 SEP 2013
- National Nature Science Foundation of China. Grant Number: 30901216
- Zhejiang Natural Science Foundation. Grant Number: LY12B07002
- K.C. Wong Magna Fund in Ningbo University.
- mitogen-activated protein kinase;
Microcystin-LR (MC-LR) has been regarded as a hepatotoxin, which can cause cytoskeletal reorganization, especially of the actin filaments. However, the underlying mechanisms remain unclear. In this study, whether MC-LR could induce microfilaments disruption was verified in the normal human liver cell line HL7702; and then the transcription, translation, and phosphorylation levels of major microfilament-associated proteins were measured; finally, the underlying mechanisms was investigated. After treatment with MC-LR, the actin filaments lost their characteristic filamentous organization in the cells, demonstrating increased actin depolymerization. The mRNA and protein levels of ezrin, vasodilator-stimulated phosphoprotein (VASP), actin-related protein2/3, and cofilin remained unchanged. However, the phosphorylation levels of ezrin and VASP were increased, when treated with 10 μM MC-LR. Moreover, P38 and ERK1/2 were involved in MC-LR-induced hyperphosphorylation of microfilament-associated proteins. In summary, this study demonstrates that MC-LR can cause disruption of actin filaments in HL7702 cells due to MC-LR-induced mitogen-activated protein kinase pathway activation and hyperphosphorylation of different types of microfilament-associated proteins. © 2014 Wiley Periodicals, Inc. Environ Toxicol, 2014.