Exp Mol Med.
2005 Oct;37(5):427-435.
Heat shock protein 27 interacts with vimentin and prevents insolubilization of vimentin subunits induced by cadmium
- Affiliations
-
- 1ILCHUN Molecular Medicine Institute MRC, Department of Biochemistry and Molecular Biology, Seoul National University College of Medicine, Seoul 110-799, Korea. jeongsun@snu.ac.kr
- 2Laboratory of Functional Genomics, Korea Institute of Radiological & Medical Sciences, Seoul 139-706, Korea.
- 3School of Biological Sciences, Seoul National University, Seoul 151-742, Korea.
Abstract
- Vimentin is an intermediate filament that regulates cell attachment and subcellular organization. In this study, vimentin filaments were morphologically altered, and its soluble subunits were rapidly reduced via cadmium chloride treatment. Cadmium chloride stimulated three major mitogen-activated protein kinases (MAPKs): extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38, and led apoptotic pathway via caspase-9 and caspase-3 activations. In order to determine whether MAPKs were involved in this cadmium-induced soluble vimentin disappearance, we applied MAPK- specific inhibitors (PD98059, SP600125, SB203580). These inhibitors did not abolish the cadmium-induced soluble vimentin disappearance. Caspase and proteosome degradation pathway were also not involved in soluble vimentin disappearance. When we observed vimentin levels in soluble and insoluble fractions, soluble vimentin subunits shifted to an insoluble fraction. As we discovered that heat- shock protein 27 (HSP27) was colocalized and physically associated with vimentin in unstressed cells, the roles of HSP27 with regard to vimentin were assessed. HSP27-overexpressing cells prevented morphological alterations of the vimentin filaments, as well as reductions of soluble vimentin, in the cadmium-treated cells. Moreover, HSP27 antisense oligonucleotide augmented these cadmium-induced changes in vimentin. These findings indicate that HSP27 prevents disruption of the vimentin intermediate filament networks and soluble vimentin disappearance, by virtue of its physical interaction with vimentin in cadmium-treated SK-N-SH cells.
Keyword
- Full Text Links
-
- Actions
-
Cited
- CITED
-
- Close
- Share
-
- Similar articles
-
- The Protective Effect of Induced Heat Shock Protein in Human Corneal Epithelial Cells
- Expression of Heat Shock Protein 70 m-RNA in Rat Bladder Overdistended by Diuresis
- Heat Shock Protein Induction By An Infrared Warm Compression Device
- Environmental factors regulating the expression of Porphyromonas gingivalis heat shock protein
- Hsp27 modulation of implant-associated metal ion cytotoxicity of osteoblastic cells
