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Volumn 41, Issue 5, 2006, Pages 816-822

PKA-mediated ERK1/2 inactivation and hsp70 gene expression following exercise

Author keywords

c Jun NH2 terminal kinases stress activated protein kinase; Heat shock transcription factor 1; Intracellular signaling; Phosphorylation; Repression

Indexed keywords

CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE INHIBITOR; HEAT SHOCK PROTEIN 70; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; STRESS ACTIVATED PROTEIN KINASE; UB 1026; UNCLASSIFIED DRUG;

EID: 33750340059     PISSN: 00222828     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yjmcc.2006.05.010     Document Type: Article
Times cited : (19)

References (38)
  • 1
    • 0032572603 scopus 로고    scopus 로고
    • Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease
    • Benjamin I.J., and McMillan D.R. Stress (heat shock) proteins: molecular chaperones in cardiovascular biology and disease. Circ. Res. 83 2 (1998) 117-132
    • (1998) Circ. Res. , vol.83 , Issue.2 , pp. 117-132
    • Benjamin, I.J.1    McMillan, D.R.2
  • 2
    • 3242879188 scopus 로고    scopus 로고
    • "The stress of dying": the role of heat shock proteins in the regulation of apoptosis
    • Beere H.M. "The stress of dying": the role of heat shock proteins in the regulation of apoptosis. J. Cell. Sci. 117 Pt 13 (2004) 2641-2651
    • (2004) J. Cell. Sci. , vol.117 , Issue.PART 13 , pp. 2641-2651
    • Beere, H.M.1
  • 4
    • 0037013182 scopus 로고    scopus 로고
    • Exercise improves postischemic cardiac function in males but not females: consequences of a novel sex-specific heat shock protein 70 response
    • Paroo Z., Haist J.V., Karmazyn M., and Noble E.G. Exercise improves postischemic cardiac function in males but not females: consequences of a novel sex-specific heat shock protein 70 response. Circ. Res. 90 8 (2002) 911-917
    • (2002) Circ. Res. , vol.90 , Issue.8 , pp. 911-917
    • Paroo, Z.1    Haist, J.V.2    Karmazyn, M.3    Noble, E.G.4
  • 5
    • 0028873201 scopus 로고
    • Activation of heat-shock transcription factor in rat heart after heat shock and exercise
    • Locke M., Noble E.G., Tanguay R.M., Feild M.R., Ianuzzo S.E., and Ianuzzo C.D. Activation of heat-shock transcription factor in rat heart after heat shock and exercise. Am. J. Physiol. 268 6 Pt 1 (1995) C1387-C1394
    • (1995) Am. J. Physiol. , vol.268 , Issue.6 PART 1
    • Locke, M.1    Noble, E.G.2    Tanguay, R.M.3    Feild, M.R.4    Ianuzzo, S.E.5    Ianuzzo, C.D.6
  • 6
    • 0032555685 scopus 로고    scopus 로고
    • Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1
    • Zou J., Guo Y., Guettouche T., Smith D.F., and Voellmy R. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell 94 4 (1998) 471-480
    • (1998) Cell , vol.94 , Issue.4 , pp. 471-480
    • Zou, J.1    Guo, Y.2    Guettouche, T.3    Smith, D.F.4    Voellmy, R.5
  • 7
    • 0032031725 scopus 로고    scopus 로고
    • Molecular chaperones as HSF1-specific transcriptional repressors
    • Shi Y., Mosser D.D., and Morimoto R.I. Molecular chaperones as HSF1-specific transcriptional repressors. Genes Dev. 12 5 (1998) 654-666
    • (1998) Genes Dev. , vol.12 , Issue.5 , pp. 654-666
    • Shi, Y.1    Mosser, D.D.2    Morimoto, R.I.3
  • 8
    • 0019258079 scopus 로고
    • Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides
    • Hightower L.E. Cultured animal cells exposed to amino acid analogues or puromycin rapidly synthesize several polypeptides. J. Cell. Physiol. 102 3 (1980) 407-427
    • (1980) J. Cell. Physiol. , vol.102 , Issue.3 , pp. 407-427
    • Hightower, L.E.1
  • 9
    • 0022455603 scopus 로고
    • Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes
    • Ananthan J., Goldberg A.L., and Voellmy R. Abnormal proteins serve as eukaryotic stress signals and trigger the activation of heat shock genes. Science (Wash DC) 232 (1986) 522-525
    • (1986) Science (Wash DC) , vol.232 , pp. 522-525
    • Ananthan, J.1    Goldberg, A.L.2    Voellmy, R.3
  • 10
    • 0027461364 scopus 로고
    • Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress
    • Sarge K.D., Murphy S.P., and Morimoto R.I. Activation of heat shock gene transcription by heat shock factor 1 involves oligomerization, acquisition of DNA-binding activity, and nuclear localization and can occur in the absence of stress. Mol. Cell. Biol. 13 3 (1993) 1392-1407
    • (1993) Mol. Cell. Biol. , vol.13 , Issue.3 , pp. 1392-1407
    • Sarge, K.D.1    Murphy, S.P.2    Morimoto, R.I.3
  • 11
    • 0027113344 scopus 로고
    • Effect of sodium salicylate on the human heat shock response
    • Jurivich D.A., Sistonen L., Kroes R.A., and Morimoto R.I. Effect of sodium salicylate on the human heat shock response. Science 255 5049 (1992) 1243-1245
    • (1992) Science , vol.255 , Issue.5049 , pp. 1243-1245
    • Jurivich, D.A.1    Sistonen, L.2    Kroes, R.A.3    Morimoto, R.I.4
  • 12
    • 0029909656 scopus 로고    scopus 로고
    • Sodium salicylate decreases intracellular ATP, induces both heat shock factor binding and chromosomal puffing, but does not induce hsp 70 gene transcription in Drosophila
    • Winegarden N.A., Wong K.S., Sopta M., and Westwood J.T. Sodium salicylate decreases intracellular ATP, induces both heat shock factor binding and chromosomal puffing, but does not induce hsp 70 gene transcription in Drosophila. J. Biol. Chem. 271 43 (1996) 26971-26980
    • (1996) J. Biol. Chem. , vol.271 , Issue.43 , pp. 26971-26980
    • Winegarden, N.A.1    Wong, K.S.2    Sopta, M.3    Westwood, J.T.4
  • 13
    • 0029055176 scopus 로고
    • Multiple layers of regulation of human heat shock transcription factor 1
    • Zuo J., Rungger D., and Voellmy R. Multiple layers of regulation of human heat shock transcription factor 1. Mol. Cell. Biol. 15 8 (1995) 4319-4330
    • (1995) Mol. Cell. Biol. , vol.15 , Issue.8 , pp. 4319-4330
    • Zuo, J.1    Rungger, D.2    Voellmy, R.3
  • 14
    • 0031055277 scopus 로고    scopus 로고
    • Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers
    • Xia W., and Voellmy R. Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers. J. Biol. Chem. 272 7 (1997) 4094-4102
    • (1997) J. Biol. Chem. , vol.272 , Issue.7 , pp. 4094-4102
    • Xia, W.1    Voellmy, R.2
  • 15
    • 4544294195 scopus 로고    scopus 로고
    • Regulation of myocardial heat shock protein 70 gene expression following exercise
    • Melling J.C.W., Thorp D.B., and Noble E.G. Regulation of myocardial heat shock protein 70 gene expression following exercise. J. Mol. Cell. Cardiol. 37 4 (2004) 847-855
    • (2004) J. Mol. Cell. Cardiol. , vol.37 , Issue.4 , pp. 847-855
    • Melling, J.C.W.1    Thorp, D.B.2    Noble, E.G.3
  • 17
    • 2942578973 scopus 로고    scopus 로고
    • Cyclic adenosine monophosphate inhibits nitric oxide-induced apoptosis of cardiac muscle cells in a c-Jun N-terminal kinase-dependent manner
    • Chae H.J., Chae S.W., and Kim H.R. Cyclic adenosine monophosphate inhibits nitric oxide-induced apoptosis of cardiac muscle cells in a c-Jun N-terminal kinase-dependent manner. Immunopharmacol Immunotoxicol 26 2 (2004) 249-263
    • (2004) Immunopharmacol Immunotoxicol , vol.26 , Issue.2 , pp. 249-263
    • Chae, H.J.1    Chae, S.W.2    Kim, H.R.3
  • 18
    • 0029846433 scopus 로고    scopus 로고
    • Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1
    • Chu B., Soncin F., Price B.D., Stevenson M.A., and Calderwood S.K. Sequential phosphorylation by mitogen-activated protein kinase and glycogen synthase kinase 3 represses transcriptional activation by heat shock factor-1. J. Biol. Chem. 271 48 (1996) 30847-30857
    • (1996) J. Biol. Chem. , vol.271 , Issue.48 , pp. 30847-30857
    • Chu, B.1    Soncin, F.2    Price, B.D.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 19
    • 0034674061 scopus 로고    scopus 로고
    • c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity
    • Dai R., Frejtag W., He B., Zhang Y., and Mivechi N.F. c-Jun NH2-terminal kinase targeting and phosphorylation of heat shock factor-1 suppress its transcriptional activity. J. Biol. Chem. 275 24 (2000) 18210-18218
    • (2000) J. Biol. Chem. , vol.275 , Issue.24 , pp. 18210-18218
    • Dai, R.1    Frejtag, W.2    He, B.3    Zhang, Y.4    Mivechi, N.F.5
  • 20
    • 0942298235 scopus 로고    scopus 로고
    • c-Jun is regulated by combination of enhanced expression and phosphorylation in acute-overloaded rat heart
    • Nadruz Jr. W., Kobarg C.B., Kobarg J., and Franchini K.G. c-Jun is regulated by combination of enhanced expression and phosphorylation in acute-overloaded rat heart. Am. J. Physiol., Heart Circ. Physiol. 286 2 (2004) H760-H767
    • (2004) Am. J. Physiol., Heart Circ. Physiol. , vol.286 , Issue.2
    • Nadruz Jr., W.1    Kobarg, C.B.2    Kobarg, J.3    Franchini, K.G.4
  • 22
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 23
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 1 (1987) 156-159
    • (1987) Anal. Biochem. , vol.162 , Issue.1 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 24
    • 0030872474 scopus 로고    scopus 로고
    • Ischemic preconditioning induces selective translocation of protein kinase C isoforms epsilon and eta in the heart of conscious rabbits without subcellular redistribution of total protein kinase C activity
    • Ping P., Zhang J., Qiu Y., Tang X.L., Manchikalapudi S., Cao X., et al. Ischemic preconditioning induces selective translocation of protein kinase C isoforms epsilon and eta in the heart of conscious rabbits without subcellular redistribution of total protein kinase C activity. Circ. Res. 81 3 (1997) 404-414
    • (1997) Circ. Res. , vol.81 , Issue.3 , pp. 404-414
    • Ping, P.1    Zhang, J.2    Qiu, Y.3    Tang, X.L.4    Manchikalapudi, S.5    Cao, X.6
  • 25
    • 0037032817 scopus 로고    scopus 로고
    • Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases
    • Johnson G.L., and Lapadat R. Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases. Science 298 5600 (2002) 1911-1912
    • (2002) Science , vol.298 , Issue.5600 , pp. 1911-1912
    • Johnson, G.L.1    Lapadat, R.2
  • 26
    • 0029804194 scopus 로고    scopus 로고
    • Repression of human heat shock factor 1 activity at control temperature by phosphorylation
    • Knauf U., Newton E.M., Kyriakis J., and Kingston R.E. Repression of human heat shock factor 1 activity at control temperature by phosphorylation. Genes Dev. 10 21 (1996) 2782-2793
    • (1996) Genes Dev. , vol.10 , Issue.21 , pp. 2782-2793
    • Knauf, U.1    Newton, E.M.2    Kyriakis, J.3    Kingston, R.E.4
  • 27
    • 10344252829 scopus 로고    scopus 로고
    • Interactions between extracellular signal-regulated protein kinase 1, 14-3-3epsilon, and heat shock factor 1 during stress
    • Wang X., Grammatikakis N., Siganou A., Stevenson M.A., and Calderwood S.K. Interactions between extracellular signal-regulated protein kinase 1, 14-3-3epsilon, and heat shock factor 1 during stress. J. Biol. Chem. 279 47 (2004) 49460-49469
    • (2004) J. Biol. Chem. , vol.279 , Issue.47 , pp. 49460-49469
    • Wang, X.1    Grammatikakis, N.2    Siganou, A.3    Stevenson, M.A.4    Calderwood, S.K.5
  • 28
    • 0041468990 scopus 로고    scopus 로고
    • Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1
    • Wang X., Grammatikakis N., Siganou A., and Calderwood S.K. Regulation of molecular chaperone gene transcription involves the serine phosphorylation, 14-3-3 epsilon binding, and cytoplasmic sequestration of heat shock factor 1. Mol. Cell. Biol. 23 17 (2003) 6013-6026
    • (2003) Mol. Cell. Biol. , vol.23 , Issue.17 , pp. 6013-6026
    • Wang, X.1    Grammatikakis, N.2    Siganou, A.3    Calderwood, S.K.4
  • 29
    • 0041529686 scopus 로고    scopus 로고
    • Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras
    • Dumaz N., and Marais R. Protein kinase A blocks Raf-1 activity by stimulating 14-3-3 binding and blocking Raf-1 interaction with Ras. J. Biol. Chem. 278 32 (2003) 29819-29823
    • (2003) J. Biol. Chem. , vol.278 , Issue.32 , pp. 29819-29823
    • Dumaz, N.1    Marais, R.2
  • 30
    • 0034745354 scopus 로고    scopus 로고
    • Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth
    • Song J., Takeda M., and Morimoto R.I. Bag1-Hsp70 mediates a physiological stress signalling pathway that regulates Raf-1/ERK and cell growth. Nat. Cell. Biol. 3 3 (2001) 276-282
    • (2001) Nat. Cell. Biol. , vol.3 , Issue.3 , pp. 276-282
    • Song, J.1    Takeda, M.2    Morimoto, R.I.3
  • 31
    • 3543054528 scopus 로고    scopus 로고
    • Divergent effects of exercise on metabolic and mitogenic signaling pathways in human skeletal muscle
    • Widegren U., Jiang X.J., Krook A., Chibalin A.V., Bjornholm M., Tally M., et al. Divergent effects of exercise on metabolic and mitogenic signaling pathways in human skeletal muscle. FASEB J. 12 13 (1998) 1379-1389
    • (1998) FASEB J. , vol.12 , Issue.13 , pp. 1379-1389
    • Widegren, U.1    Jiang, X.J.2    Krook, A.3    Chibalin, A.V.4    Bjornholm, M.5    Tally, M.6
  • 34
    • 0033571738 scopus 로고    scopus 로고
    • Salicylic acid and aspirin inhibit the activity of RSK2 kinase and repress RSK2-dependent transcription of cyclic AMP response element binding protein- and NF-kappa B-responsive genes
    • Stevenson M.A., Zhao M.J., Asea A., Coleman C.N., and Calderwood S.K. Salicylic acid and aspirin inhibit the activity of RSK2 kinase and repress RSK2-dependent transcription of cyclic AMP response element binding protein- and NF-kappa B-responsive genes. J. Immunol. 163 10 (1999) 5608-5616
    • (1999) J. Immunol. , vol.163 , Issue.10 , pp. 5608-5616
    • Stevenson, M.A.1    Zhao, M.J.2    Asea, A.3    Coleman, C.N.4    Calderwood, S.K.5
  • 35
    • 0037799236 scopus 로고    scopus 로고
    • Heat shock factor 1 contains two functional domains that mediate transcriptional repression of the c-fos and c-fms genes
    • Xie Y., Zhong R., Chen C., and Calderwood S.K. Heat shock factor 1 contains two functional domains that mediate transcriptional repression of the c-fos and c-fms genes. J. Biol. Chem. 278 7 (2003) 4687-4698
    • (2003) J. Biol. Chem. , vol.278 , Issue.7 , pp. 4687-4698
    • Xie, Y.1    Zhong, R.2    Chen, C.3    Calderwood, S.K.4
  • 37
    • 0036021808 scopus 로고    scopus 로고
    • Exercise-induced elevation of HSP70 is intensity dependent
    • Milne K.J., and Noble E.G. Exercise-induced elevation of HSP70 is intensity dependent. J. Appl. Physiol. 93 2 (2002) 561-568
    • (2002) J. Appl. Physiol. , vol.93 , Issue.2 , pp. 561-568
    • Milne, K.J.1    Noble, E.G.2
  • 38
    • 0034957926 scopus 로고    scopus 로고
    • JNK phosphorylates the HSF1 transcriptional activation domain: role of JNK in the regulation of the heat shock response
    • Park J., and Liu A.Y. JNK phosphorylates the HSF1 transcriptional activation domain: role of JNK in the regulation of the heat shock response. J. Cell. Biochem. 82 2 (2001) 326-338
    • (2001) J. Cell. Biochem. , vol.82 , Issue.2 , pp. 326-338
    • Park, J.1    Liu, A.Y.2


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