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.
| Original language | English |
|---|---|
| Pages (from-to) | 427-435 |
| Number of pages | 9 |
| Journal | Experimental and Molecular Medicine |
| Volume | 37 |
| Issue number | 5 |
| Publication status | Published - 2005 Oct 31 |
| Externally published | Yes |
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Keywords
- Apoptosis
- Cadmium chloride
- Heat shock protein
- Mitogen activated protein kinases
- Molecular chaperones
- Vimentin
ASJC Scopus subject areas
- Biochemistry
- Genetics
Cite this
Heat shock protein 27 interacts with vimentin and prevents insolubilization of vimentin subunits induced by cadmium. / Lee, Jae Seon; Zhang, Mei Hua; Yun, Eun Kyung; Geum, Dongho; Kim, Kyungjin; Kim, Tae Hyung; Lim, Yun Sook; Seo, Jeong Sun.
In: Experimental and Molecular Medicine, Vol. 37, No. 5, 31.10.2005, p. 427-435.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Heat shock protein 27 interacts with vimentin and prevents insolubilization of vimentin subunits induced by cadmium
AU - Lee, Jae Seon
AU - Zhang, Mei Hua
AU - Yun, Eun Kyung
AU - Geum, Dongho
AU - Kim, Kyungjin
AU - Kim, Tae Hyung
AU - Lim, Yun Sook
AU - Seo, Jeong Sun
PY - 2005/10/31
Y1 - 2005/10/31
N2 - 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.
AB - 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.
KW - Apoptosis
KW - Cadmium chloride
KW - Heat shock protein
KW - Mitogen activated protein kinases
KW - Molecular chaperones
KW - Vimentin
UR - http://www.scopus.com/inward/record.url?scp=27744607883&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=27744607883&partnerID=8YFLogxK
M3 - Article
C2 - 16264267
AN - SCOPUS:27744607883
VL - 37
SP - 427
EP - 435
JO - Experimental and Molecular Medicine
JF - Experimental and Molecular Medicine
SN - 1226-3613
IS - 5
ER -