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Article: Hsp20 protects neuroblastoma cells from ischemia/reperfusion injury by inhibition of apoptosis via a mechanism that involves the mitochondrial pathways

TitleHsp20 protects neuroblastoma cells from ischemia/reperfusion injury by inhibition of apoptosis via a mechanism that involves the mitochondrial pathways
Authors
Issue Date2010
PublisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/cnr/index.htm
Citation
Current Neurovascular Research, 2010, v. 7 n. 4, p. 281-287 How to Cite?
AbstractHsp20 is a chaperone protein that is highly and constitutively expressed in the brain, cardiac tissue and many other organs. Recently, it is well established that Hsp20 can enhance cardiac function and render cardioprotection. However, the potential benefits of Hsp20 and its phosphorylation form action on ischemic stroke and the underlying mechanism(s) are largely unknown. To investigate whether Hsp20 exerts protective effects on in vitro ischemia/ reperfusion (I/R) injury, mouse neuroblastoma cells were subjected to oxygen-glucose deprivation (OGD) and reoxygenation. Expressions of Hsp20 were strongly downregulated in mouse N2A cells at the 0-hour and 6-hour recovery time points following 4 hours of OGD, and returned to basal level 12 and 24 hours after OGD treatment, both at mRNA and protein levels. The ratio of phosphorylated to total Hsp20 protein was not significantly affected at the 0-hour and 6hour recovery time points following 4 hours of OGD. However, markedly higher serine phosphorylation of Hsp20 was observed 12 and 24 hours after OGD treatment. Furthermore, overexpression of Hsp20 reduced OGD-induced apoptosis by reducing the release of cytochrome c from mitochondria to cytosol. However, blockade of Hsp20 phosphorylation at Ser16 abrogated this anti-apoptotic effect. In conclusion, our data demonstrated that increased Hsp20 expression in mouse N2A neuroblastoma cells protected against I/R injury, resulting in reduced apoptosis with the decrease of the release of cytochrome c from mitochondria to cytosol. Phosphorylation of Ser16 played an important role in the neuroprotective effect of Hsp20. Thus, Hsp20 may constitute a new therapeutic target for cerebral ischemic diseases. © 2010 Bentham Science Publishers Ltd.
Persistent Identifierhttp://hdl.handle.net/10722/168496
ISSN
2015 Impact Factor: 2.123
2015 SCImago Journal Rankings: 0.695
References

 

DC FieldValueLanguage
dc.contributor.authorZeng, Len_US
dc.contributor.authorTan, Jen_US
dc.contributor.authorHu, Zen_US
dc.contributor.authorLu, Wen_US
dc.contributor.authorYang, Ben_US
dc.date.accessioned2012-10-08T03:19:39Z-
dc.date.available2012-10-08T03:19:39Z-
dc.date.issued2010en_US
dc.identifier.citationCurrent Neurovascular Research, 2010, v. 7 n. 4, p. 281-287en_US
dc.identifier.issn1567-2026en_US
dc.identifier.urihttp://hdl.handle.net/10722/168496-
dc.description.abstractHsp20 is a chaperone protein that is highly and constitutively expressed in the brain, cardiac tissue and many other organs. Recently, it is well established that Hsp20 can enhance cardiac function and render cardioprotection. However, the potential benefits of Hsp20 and its phosphorylation form action on ischemic stroke and the underlying mechanism(s) are largely unknown. To investigate whether Hsp20 exerts protective effects on in vitro ischemia/ reperfusion (I/R) injury, mouse neuroblastoma cells were subjected to oxygen-glucose deprivation (OGD) and reoxygenation. Expressions of Hsp20 were strongly downregulated in mouse N2A cells at the 0-hour and 6-hour recovery time points following 4 hours of OGD, and returned to basal level 12 and 24 hours after OGD treatment, both at mRNA and protein levels. The ratio of phosphorylated to total Hsp20 protein was not significantly affected at the 0-hour and 6hour recovery time points following 4 hours of OGD. However, markedly higher serine phosphorylation of Hsp20 was observed 12 and 24 hours after OGD treatment. Furthermore, overexpression of Hsp20 reduced OGD-induced apoptosis by reducing the release of cytochrome c from mitochondria to cytosol. However, blockade of Hsp20 phosphorylation at Ser16 abrogated this anti-apoptotic effect. In conclusion, our data demonstrated that increased Hsp20 expression in mouse N2A neuroblastoma cells protected against I/R injury, resulting in reduced apoptosis with the decrease of the release of cytochrome c from mitochondria to cytosol. Phosphorylation of Ser16 played an important role in the neuroprotective effect of Hsp20. Thus, Hsp20 may constitute a new therapeutic target for cerebral ischemic diseases. © 2010 Bentham Science Publishers Ltd.en_US
dc.languageengen_US
dc.publisherBentham Science Publishers Ltd. The Journal's web site is located at http://www.bentham.org/cnr/index.htmen_US
dc.relation.ispartofCurrent Neurovascular Researchen_US
dc.subject.meshAnimalsen_US
dc.subject.meshAnoxia - Metabolismen_US
dc.subject.meshApoptosis - Drug Effects - Physiologyen_US
dc.subject.meshCell Line, Tumoren_US
dc.subject.meshCytochromes C - Metabolismen_US
dc.subject.meshGene Expression Regulation, Neoplastic - Physiologyen_US
dc.subject.meshGlucose - Deficiencyen_US
dc.subject.meshGreen Fluorescent Proteins - Geneticsen_US
dc.subject.meshHsp20 Heat-Shock Proteins - Genetics - Metabolismen_US
dc.subject.meshMiceen_US
dc.subject.meshMitochondria - Metabolismen_US
dc.subject.meshMutationen_US
dc.subject.meshNeuroblastoma - Pathology - Ultrastructureen_US
dc.subject.meshPhosphorylation - Physiologyen_US
dc.subject.meshRna, Messenger - Metabolismen_US
dc.subject.meshTime Factorsen_US
dc.titleHsp20 protects neuroblastoma cells from ischemia/reperfusion injury by inhibition of apoptosis via a mechanism that involves the mitochondrial pathwaysen_US
dc.typeArticleen_US
dc.identifier.emailLu, W:luwei@hku.hken_US
dc.identifier.authorityLu, W=rp00754en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.2174/156720210793180783-
dc.identifier.pmid20854253-
dc.identifier.scopuseid_2-s2.0-78650664487en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78650664487&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume7en_US
dc.identifier.issue4en_US
dc.identifier.spage281en_US
dc.identifier.epage287en_US
dc.publisher.placeNetherlandsen_US
dc.identifier.scopusauthoridZeng, L=16647753300en_US
dc.identifier.scopusauthoridTan, J=25648410200en_US
dc.identifier.scopusauthoridHu, Z=7404210124en_US
dc.identifier.scopusauthoridLu, W=27868087600en_US
dc.identifier.scopusauthoridYang, B=18635779100en_US

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