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HSP70 deficiency results in activation of c-Jun N-terminal Kinase, extracellular signal-regulated kinase, and caspase-3 in hyperosmolarity-induced apoptosis
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Lee, Jae-Seon | - |
dc.contributor.author | Lee, Je-Jung | - |
dc.contributor.author | Seo, Jeong-Sun | - |
dc.date.accessioned | 2010-01-12T04:25:23Z | - |
dc.date.available | 2010-01-12T04:25:23Z | - |
dc.date.issued | 2004-12-14 | - |
dc.identifier.citation | J Biol Chem. 2005 Feb 25;280(8):6634-41. Epub 2004 Dec 7. | en |
dc.identifier.issn | 0021-9258 (Print) | - |
dc.identifier.uri | http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15590690 | - |
dc.identifier.uri | https://hdl.handle.net/10371/29642 | - |
dc.description.abstract | In this study we examined the function of heat shock protein 70 (HSP70) in the hyperosmolarity-induced apoptotic pathway using hsp70.1-/-mouse embryonic fibroblasts (MEFs). When the cells were exposed to hyperosmotic stress, an absence of HSP70 negatively affected cell viability. Caspase-9 and caspase-3 were rapidly activated, and extensive cleavage occurred in focal adhesion and cytoskeletal molecules in the hsp70.1-/-MEFs. In contrast, hsp70.1+/+ MEFs exhibited no caspase-9 or caspase-3 activation and finally recovered intact cell morphology when cells were shifted back to an isosmotic state. Because HSP70 might be involved in the regulation of mitogen-activated protein kinase (MAPK) activities with regard to various cellular activities, we also monitored MAPK phosphorylation. The absence of HSP70 affected c-Jun N-terminal kinase phosphorylation. However, it had no effect on p38. Sustained phosphorylation of extracellular signal-regulated kinase (ERK) was observed during the hyperosmolarity-induced apoptosis of hsp70.1-/-MEFs. Inhibition of ERK activity by the treatment of PD98059 accelerated the apoptotic pathway. ERK phosphorylation was precisely correlated with shift of mitogen-activated protein kinase phosphatase-3 from the soluble to insoluble fraction. Our results demonstrate that the inhibitory effect of HSP70 on caspase-3 activation is sufficient to inhibit apoptosis and that HSP70 exhibits regulatory functions to c-Jun N-terminal kinase and ERK phosphorylation in hyperosmolarity-induced apoptosis. | en |
dc.language.iso | en | en |
dc.publisher | American Society for Biochemistry and Molecular Biology | en |
dc.subject | Animals | en |
dc.subject | Caspase 3 | en |
dc.subject | Caspases/antagonists & inhibitors/*metabolism | en |
dc.subject | Cells, Cultured | en |
dc.subject | Dual Specificity Phosphatase 1 | en |
dc.subject | Embryo, Mammalian/cytology | en |
dc.subject | Extracellular Signal-Regulated MAP Kinases/*metabolism | en |
dc.subject | HSP70 Heat-Shock Proteins/deficiency/genetics/*physiology | en |
dc.subject | JNK Mitogen-Activated Protein Kinases/*metabolism | en |
dc.subject | Mice | en |
dc.subject | Mice, Knockout | en |
dc.subject | Mice, Transgenic | en |
dc.subject | Phosphorylation | en |
dc.subject | Protein Phosphatase 1 | en |
dc.subject | Protein Tyrosine Phosphatases/metabolism | en |
dc.subject | Transfection | en |
dc.subject | Apoptosis | - |
dc.subject | Osmotic Pressure | - |
dc.title | HSP70 deficiency results in activation of c-Jun N-terminal Kinase, extracellular signal-regulated kinase, and caspase-3 in hyperosmolarity-induced apoptosis | en |
dc.type | Article | en |
dc.contributor.AlternativeAuthor | 이재선 | - |
dc.contributor.AlternativeAuthor | 이제중 | - |
dc.contributor.AlternativeAuthor | 서정선 | - |
dc.identifier.doi | 10.1074/jbc.M412393200 | - |
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