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Preheating accelerates mitogen-activated protein (MAP) kinase inactivation post-heat shock via a heat shock protein 70-mediated increase in phosphorylated MAP kinase phosphatase-1

Cited 36 time in Web of Science Cited 39 time in Scopus
Authors
Lee, Kyoung-Hee; Lee, Choon-Taek; Kim, Young Whan; Han, Sung Koo; Shim, Young-Soo; Yoo, Chul-Gyu
Issue Date
2005-01-29
Publisher
American Society for Biochemistry and Molecular Biology
Citation
J Biol Chem. 2005 Apr 1;280(13):13179-86. Epub 2005 Jan 26.
Keywords
Adenoviridae/geneticsAnimalsBlotting, WesternBronchi/cytologyCell Cycle Proteins/*antagonists & inhibitors/*metabolismCells, CulturedDual Specificity Phosphatase 1Enzyme Inhibitors/pharmacologyEpithelial Cells/cytologyHSP70 Heat-Shock Proteins/*metabolismHot TemperatureHumansImmediate-Early Proteins/*antagonists & inhibitors/*metabolismJNK Mitogen-Activated Protein Kinases/metabolismMAP Kinase Kinase 4*MAP Kinase Signaling SystemMiceMitogen-Activated Protein Kinase Kinases/metabolismNIH 3T3 CellsOligonucleotides/chemistryOligonucleotides, Antisense/chemistryPhosphoprotein Phosphatases/*antagonists & inhibitors/*metabolismPhosphorylationProtein BindingProtein Phosphatase 1Protein Tyrosine Phosphatases/*antagonists & inhibitors/*metabolismTime FactorsUp-Regulation
Abstract
Heat shock (HS) activates mitogen-activated protein (MAP) kinases. Although prior exposure to nonlethal HS makes cells refractory to the lethal effect of a subsequent HS, it is unclear whether this also occurs in MAP kinase activation. This study was undertaken to evaluate the effect of a heat pretreatment on MAP kinase activation by a subsequent HS and to elucidate its possible mechanism. Preheating did not make BEAS-2B cells refractory to extracellular signal-regulated protein kinase (ERK) and c-Jun N-terminal kinase (JNK) activation by a second HS but accelerated their inactivation after HS. The rapid inactivation of ERK and JNK was dependent on de novo protein synthesis and associated with the up-regulation of heat shock protein 70 (HSP70). Moreover, the inhibition of phosphatase activity reversed this rapid inactivation. MAP kinase phosphatase-1 (MKP-1) expression was increased by HS, and the presence of its phosphorylated form (p-MKP-1) correlated with the observed rapid ERK and JNK inactivation. Blocking induction of p-MKP-1 with antisense MKP-1 oligonucleotides suppressed the rapid inactivation of ERK and JNK in preheated cells. HSP70 overexpression caused the early phosphorylation of MKP-1. Moreover, MKP-1 phosphorylation and the rapid inactivation of ERK were inhibited by blocking HSP70 induction in preheated cells. In addition, MKP-1 was insolubilized by HS, and HSP70 associated physically with MKP-1, suggesting that a chaperone effect of HSP70 might have caused the early phosphorylation of MKP-1. These results indicate that preheating accelerated MAP kinase inactivation after a second HS and that this is related to a HSP70-mediated increase in p-MKP-1.
ISSN
0021-9258 (Print)
Language
English
URI
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&dopt=Citation&list_uids=15677475

http://hdl.handle.net/10371/29655
DOI
https://doi.org/10.1074/jbc.M410059200
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College of Medicine/School of Medicine (의과대학/대학원)Internal Medicine (내과학전공)Journal Papers (저널논문_내과학전공)
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