S-Space College of Medicine/School of Medicine (의과대학/대학원) Internal Medicine (내과학전공) Journal Papers (저널논문_내과학전공)
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
- Issue Date
- J Biol Chem. 2005 Apr 1;280(13):13179-86. Epub 2005 Jan 26.
- Adenoviridae/genetics ; Animals ; Blotting, Western ; Bronchi/cytology ; Cell Cycle Proteins/*antagonists & inhibitors/*metabolism ; Cells, Cultured ; Dual Specificity Phosphatase 1 ; Enzyme Inhibitors/pharmacology ; Epithelial Cells/cytology ; HSP70 Heat-Shock Proteins/*metabolism ; Hot Temperature ; Humans ; Immediate-Early Proteins/*antagonists & inhibitors/*metabolism ; JNK Mitogen-Activated Protein Kinases/metabolism ; MAP Kinase Kinase 4 ; Mice ; Mitogen-Activated Protein Kinase Kinases/metabolism ; NIH 3T3 Cells ; Oligonucleotides/chemistry ; Oligonucleotides, Antisense/chemistry ; Phosphoprotein Phosphatases/*antagonists & inhibitors/*metabolism ; Phosphorylation ; Protein Binding ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/*antagonists & inhibitors/*metabolism ; Time Factors ; Up-Regulation ; MAP Kinase Signaling System
- 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.
- 0021-9258 (Print)
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