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Article: Further study on the role of HSP70 on Ca2+ homeostasis in rat ventricular myocytes subjected to simulated ischemia

TitleFurther study on the role of HSP70 on Ca2+ homeostasis in rat ventricular myocytes subjected to simulated ischemia
Authors
Keywordsκ-opioid receptor
Intracellular Ca2+
Na +/Ca2+ exchanger
Ryanodine receptor
Sarco(endo)plasmic reticulum Ca2+-ATPase
Issue Date2006
PublisherAmerican Physiological Society. The Journal's web site is located at http://intl-ajpcell.physiology.org/
Citation
American Journal Of Physiology - Cell Physiology, 2006, v. 290 n. 2, p. C583-C591 How to Cite?
AbstractWe hypothesized that activation of heat shock protein 70 (HSP70) by preconditioning, which is known to confer delayed cardioprotection, attenuates the impaired handling of Ca2+ at multiple sites. To test the hypothesis, we determined how the ryanodine receptor (RyR), sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA), and Na+/Ca2+ exchanger (NCX) handled Ca2+ in rat ventricular myocytes preconditioned with a κ-opioid receptor agonist, U50488H (UP), followed by blockade of HSP70 with a selective antisense oligonucleotide and subsequently subjected to simulated ischemia. We determined the following: 1) the Ca 2+ transients induced by electrical stimulation and caffeine, which provide the overall picture of Ca2+ homeostasis; 2) expression of RyR, SERCA, and NCX; and 3) Ca2+ fluxes via NCX by the use of 45Ca2+ in the rat ventricular myocyte. We found that UP increased the activity of RyR, SERCA, and NCX and the expression of RyR and SERCA. These effects led to increases in the release of Ca2+ from the sarcoplasmic reticulum via RyR and in the removal of Ca2+ from the cytoplasm by reuptake of Ca2+ to the SR via SERCA and by extrusion of Ca2+ out of the cell via NCX. UP also reduced mitochondrial Ca 2+ accumulation. All of the effects of UP were either abolished or significantly attenuated by blockade of HSP70 synthesis with a selective antisense oligonucleotide. The results are evidence that activation of HSP70 by preconditioning improves the ischemia-impaired Ca2+ homeostasis at multiple sites in the heart, which may be responsible, at least partly, for attenuated Ca2+ overload, improved recovery in contractile function, and cardioprotection. Copyright © 2006 the American Physiological Society.
Persistent Identifierhttp://hdl.handle.net/10722/81188
ISSN
2015 Impact Factor: 3.395
2015 SCImago Journal Rankings: 1.893
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorLiu, Jen_HK
dc.contributor.authorKam, KWLen_HK
dc.contributor.authorBorchert, GHen_HK
dc.contributor.authorKravtsov, GMen_HK
dc.contributor.authorBallard, HJen_HK
dc.contributor.authorWong, TMen_HK
dc.date.accessioned2010-09-06T08:14:50Z-
dc.date.available2010-09-06T08:14:50Z-
dc.date.issued2006en_HK
dc.identifier.citationAmerican Journal Of Physiology - Cell Physiology, 2006, v. 290 n. 2, p. C583-C591en_HK
dc.identifier.issn0363-6143en_HK
dc.identifier.urihttp://hdl.handle.net/10722/81188-
dc.description.abstractWe hypothesized that activation of heat shock protein 70 (HSP70) by preconditioning, which is known to confer delayed cardioprotection, attenuates the impaired handling of Ca2+ at multiple sites. To test the hypothesis, we determined how the ryanodine receptor (RyR), sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA), and Na+/Ca2+ exchanger (NCX) handled Ca2+ in rat ventricular myocytes preconditioned with a κ-opioid receptor agonist, U50488H (UP), followed by blockade of HSP70 with a selective antisense oligonucleotide and subsequently subjected to simulated ischemia. We determined the following: 1) the Ca 2+ transients induced by electrical stimulation and caffeine, which provide the overall picture of Ca2+ homeostasis; 2) expression of RyR, SERCA, and NCX; and 3) Ca2+ fluxes via NCX by the use of 45Ca2+ in the rat ventricular myocyte. We found that UP increased the activity of RyR, SERCA, and NCX and the expression of RyR and SERCA. These effects led to increases in the release of Ca2+ from the sarcoplasmic reticulum via RyR and in the removal of Ca2+ from the cytoplasm by reuptake of Ca2+ to the SR via SERCA and by extrusion of Ca2+ out of the cell via NCX. UP also reduced mitochondrial Ca 2+ accumulation. All of the effects of UP were either abolished or significantly attenuated by blockade of HSP70 synthesis with a selective antisense oligonucleotide. The results are evidence that activation of HSP70 by preconditioning improves the ischemia-impaired Ca2+ homeostasis at multiple sites in the heart, which may be responsible, at least partly, for attenuated Ca2+ overload, improved recovery in contractile function, and cardioprotection. Copyright © 2006 the American Physiological Society.en_HK
dc.languageengen_HK
dc.publisherAmerican Physiological Society. The Journal's web site is located at http://intl-ajpcell.physiology.org/en_HK
dc.relation.ispartofAmerican Journal of Physiology - Cell Physiologyen_HK
dc.rightsAmerican Journal of Physiology: Cell Physiology. Copyright © American Physiological Society.-
dc.subjectκ-opioid receptoren_HK
dc.subjectIntracellular Ca2+en_HK
dc.subjectNa +/Ca2+ exchangeren_HK
dc.subjectRyanodine receptoren_HK
dc.subjectSarco(endo)plasmic reticulum Ca2+-ATPaseen_HK
dc.subject.meshCalcium - metabolism-
dc.subject.meshHSP70 Heat-Shock Proteins - genetics - metabolism-
dc.subject.meshHeart Ventricles - cytology-
dc.subject.meshIschemia-
dc.subject.meshMyocytes, Cardiac - cytology - drug effects - metabolism-
dc.titleFurther study on the role of HSP70 on Ca2+ homeostasis in rat ventricular myocytes subjected to simulated ischemiaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0363-6143&volume=290&issue=2&spage=C583&epage=C591&date=2006&atitle=Further+study+on+the+role+of+HSP70+on+Ca2++homeostasis+in+rat+ventricular+myocytes+subjected+to+simulated+ischemiaen_HK
dc.identifier.emailBallard, HJ: ballard@hkucc.hku.hken_HK
dc.identifier.authorityBallard, HJ=rp00367en_HK
dc.description.naturelink_to_OA_fulltext-
dc.identifier.doi10.1152/ajpcell.00145.2005en_HK
dc.identifier.pmid16207797-
dc.identifier.scopuseid_2-s2.0-33644860565en_HK
dc.identifier.hkuros130184en_HK
dc.identifier.hkuros196065-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-33644860565&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume290en_HK
dc.identifier.issue2en_HK
dc.identifier.spageC583en_HK
dc.identifier.epageC591en_HK
dc.identifier.eissn1522-1563-
dc.identifier.isiWOS:000234531500028-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridLiu, J=26657479700en_HK
dc.identifier.scopusauthoridKam, KWL=26642919000en_HK
dc.identifier.scopusauthoridBorchert, GH=7004514387en_HK
dc.identifier.scopusauthoridKravtsov, GM=7003811092en_HK
dc.identifier.scopusauthoridBallard, HJ=7005286310en_HK
dc.identifier.scopusauthoridWong, TM=7403531434en_HK

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