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Volumn 172, Issue 3, 2008, Pages 659-670

Cellular and molecular mechanisms of heat stress-induced up-regulation of occludin protein expression: Regulatory role of heat shock factor-1

Author keywords

[No Author keywords available]

Indexed keywords

HEAT SHOCK FACTOR 1; HEAT SHOCK PROTEIN; MESSENGER RNA; OCCLUDIN; QUERCETIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG;

EID: 40449135547     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.2353/ajpath.2008.070522     Document Type: Article
Times cited : (74)

References (67)
  • 1
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • JM Anderson CM Van Itallie Tight junctions and the molecular basis for regulation of paracellular permeability Am J Physiol 269 1995 G467 G475
    • (1995) Am J Physiol , vol.269 , pp. G467-G475
    • Anderson, JM1    Van Itallie, CM2
  • 2
    • 0023809141 scopus 로고
    • Hemorrhagic shock induces bacterial translocation from the gut
    • JW Baker EA Deitch M Li RD Berg RD Specian Hemorrhagic shock induces bacterial translocation from the gut J Trauma 28 1988 896 906
    • (1988) J Trauma , vol.28 , pp. 896-906
    • Baker, JW1    Deitch, EA2    Li, M3    Berg, RD4    Specian, RD5
  • 3
    • 0024267211 scopus 로고
    • Crohn's disease—a permeability disorder of the tight junction?
    • D Hollander Crohn's disease—a permeability disorder of the tight junction? Gut 29 1988 1621 1624
    • (1988) Gut , vol.29 , pp. 1621-1624
    • Hollander, D1
  • 4
    • 0030958528 scopus 로고    scopus 로고
    • Intestinal epithelial barrier dysfunction in Crohn's disease
    • TY Ma Intestinal epithelial barrier dysfunction in Crohn's disease Proc Soc Exp Biol Med 214 1997 318 327
    • (1997) Proc Soc Exp Biol Med , vol.214 , pp. 318-327
    • Ma, TY1
  • 5
    • 0024577594 scopus 로고
    • Loosening tight junctions. Lessons from the intestine
    • JL Madara Loosening tight junctions. Lessons from the intestine J Clin Invest 83 1989 1089 1094
    • (1989) J Clin Invest , vol.83 , pp. 1089-1094
    • Madara, JL1
  • 6
    • 0000752197 scopus 로고
    • Junctional complexes in various epithelia
    • MG Farquhar GE Palade Junctional complexes in various epithelia J Cell Biol 17 1963 375 412
    • (1963) J Cell Biol , vol.17 , pp. 375-412
    • Farquhar, MG1    Palade, GE2
  • 7
    • 0033061321 scopus 로고    scopus 로고
    • Transmembrane proteins in the tight junction barrier
    • AS Fanning LL Mitic JM Anderson Transmembrane proteins in the tight junction barrier J Am Soc Nephrol 10 1999 1337 1345
    • (1999) J Am Soc Nephrol , vol.10 , pp. 1337-1345
    • Fanning, AS1    Mitic, LL2    Anderson, JM3
  • 8
    • 0035354574 scopus 로고    scopus 로고
    • Molecular structure of tight junctions and their role in epithelial transport
    • JM Anderson Molecular structure of tight junctions and their role in epithelial transport News Physiol Sci 16 2001 126 130
    • (2001) News Physiol Sci , vol.16 , pp. 126-130
    • Anderson, JM1
  • 9
    • 0023030826 scopus 로고
    • Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia
    • BR Stevenson JD Siliciano MS Mooseker DA Goodenough Identification of ZO-1: a high molecular weight polypeptide associated with the tight junction (zonula occludens) in a variety of epithelia J Cell Biol 103 1986 755 766
    • (1986) J Cell Biol , vol.103 , pp. 755-766
    • Stevenson, BR1    Siliciano, JD2    Mooseker, MS3    Goodenough, DA4
  • 10
    • 0034513771 scopus 로고    scopus 로고
    • Transmembrane proteins of tight junctions
    • MS Balda K Matter Transmembrane proteins of tight junctions Semin Cell Dev Biol 11 2000 281 289
    • (2000) Semin Cell Dev Biol , vol.11 , pp. 281-289
    • Balda, MS1    Matter, K2
  • 11
    • 34447281675 scopus 로고    scopus 로고
    • Molecular basis of epithelial barrier regulation: from basic mechanisms to clinical application
    • JR Turner Molecular basis of epithelial barrier regulation: from basic mechanisms to clinical application Am J Pathol 169 2006 1901 1909
    • (2006) Am J Pathol , vol.169 , pp. 1901-1909
    • Turner, JR1
  • 14
    • 0030748172 scopus 로고    scopus 로고
    • COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos
    • Y Chen C Merzdorf DL Paul DA Goodenough COOH terminus of occludin is required for tight junction barrier function in early Xenopus embryos J Cell Biol 138 1997 891 899
    • (1997) J Cell Biol , vol.138 , pp. 891-899
    • Chen, Y1    Merzdorf, C2    Paul, DL3    Goodenough, DA4
  • 15
    • 0033783241 scopus 로고    scopus 로고
    • Protein kinase C activation leads to dephosphorylation of occludin and tight junction permeability increase in LLC-PK1 epithelial cell sheets
    • H Clarke AP Soler JM Mullin Protein kinase C activation leads to dephosphorylation of occludin and tight junction permeability increase in LLC-PK1 epithelial cell sheets J Cell Sci 113 2000 3187 3196
    • (2000) J Cell Sci , vol.113 , pp. 3187-3196
    • Clarke, H1    Soler, AP2    Mullin, JM3
  • 16
    • 0032792058 scopus 로고    scopus 로고
    • Redistribution and phosphorylation of occludin during opening and resealing of tight junctions in cultured epithelial cells
    • P Farshori B Kachar Redistribution and phosphorylation of occludin during opening and resealing of tight junctions in cultured epithelial cells J Membr Biol 170 1999 147 156
    • (1999) J Membr Biol , vol.170 , pp. 147-156
    • Farshori, P1    Kachar, B2
  • 17
    • 0036901407 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress
    • RK Rao S Basuroy VU Rao KJ Karnaky Jr A Gupta Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress Biochem J 368 2002 471 481
    • (2002) Biochem J , vol.368 , pp. 471-481
    • Rao, RK1    Basuroy, S2    Rao, VU3    Karnaky, KJ4    Gupta, A5
  • 18
    • 0034695923 scopus 로고    scopus 로고
    • Oncogenic Raf-1 disrupts epithelial tight junctions via downregulation of occludin
    • D Li RJ Mrsny Oncogenic Raf-1 disrupts epithelial tight junctions via downregulation of occludin J Cell Biol 148 2000 791 800
    • (2000) J Cell Biol , vol.148 , pp. 791-800
    • Li, D1    Mrsny, RJ2
  • 19
    • 0023604564 scopus 로고
    • Time course of endotoxemia and cardiovascular changes in heat-stressed primates
    • P Gathiram SL Gaffin JG Brock-Utne MT Wells Time course of endotoxemia and cardiovascular changes in heat-stressed primates Aviat Space Environ Med 58 1987 1071 1074
    • (1987) Aviat Space Environ Med , vol.58 , pp. 1071-1074
    • Gathiram, P1    Gaffin, SL2    Brock-Utne, JG3    Wells, MT4
  • 20
    • 0023772589 scopus 로고
    • Portal and systemic plasma lipopolysaccharide concentrations in heat-stressed primates
    • P Gathiram MT Wells D Raidoo JG Brock-Utne SL Gaffin Portal and systemic plasma lipopolysaccharide concentrations in heat-stressed primates Circ Shock 25 1988 223 230
    • (1988) Circ Shock , vol.25 , pp. 223-230
    • Gathiram, P1    Wells, MT2    Raidoo, D3    Brock-Utne, JG4    Gaffin, SL5
  • 21
    • 0035023131 scopus 로고    scopus 로고
    • Mechanisms of circulatory and intestinal barrier dysfunction during whole body hyperthermia
    • DM Hall GR Buettner LW Oberley L Xu RD Matthes CV Gisolfi Mechanisms of circulatory and intestinal barrier dysfunction during whole body hyperthermia Am J Physiol 280 2001 H509 H521
    • (2001) Am J Physiol , vol.280 , pp. H509-H521
    • Hall, DM1    Buettner, GR2    Oberley, LW3    Xu, L4    Matthes, RD5    Gisolfi, CV6
  • 24
    • 0023618826 scopus 로고
    • Antilipopolysaccharide improves survival in primates subjected to heat stroke
    • P Gathiram MT Wells JG Brock-Utne SL Gaffin Antilipopolysaccharide improves survival in primates subjected to heat stroke Circ Shock 23 1987 157 164
    • (1987) Circ Shock , vol.23 , pp. 157-164
    • Gathiram, P1    Wells, MT2    Brock-Utne, JG3    Gaffin, SL4
  • 25
    • 0023952302 scopus 로고
    • Prophylactic corticosteroid increases survival in experimental heat stroke in primates
    • P Gathiram MT Wells JG Brock-Utne SL Gaffin Prophylactic corticosteroid increases survival in experimental heat stroke in primates Aviat Space Environ Med 59 1988 352 355
    • (1988) Aviat Space Environ Med , vol.59 , pp. 352-355
    • Gathiram, P1    Wells, MT2    Brock-Utne, JG3    Gaffin, SL4
  • 26
    • 0025845787 scopus 로고
    • Endotoxemia and release of tumor necrosis factor and interleukin 1 alpha in acute heatstroke
    • A Bouchama RS Parhar A el-Yazigi K Sheth S al-Sedairy Endotoxemia and release of tumor necrosis factor and interleukin 1 alpha in acute heatstroke J Appl Physiol 70 1991 2640 2644
    • (1991) J Appl Physiol , vol.70 , pp. 2640-2644
    • Bouchama, A1    Parhar, RS2    el-Yazigi, A3    Sheth, K4    al-Sedairy, S5
  • 27
    • 0023607538 scopus 로고
    • Prevention of endotoxaemia by non-absorbable antibiotics in heat stress
    • P Gathiram MT Wells JG Brock-Utne BC Wessels SL Gaffin Prevention of endotoxaemia by non-absorbable antibiotics in heat stress J Clin Pathol 40 1987 1364 1368
    • (1987) J Clin Pathol , vol.40 , pp. 1364-1368
    • Gathiram, P1    Wells, MT2    Brock-Utne, JG3    Wessels, BC4    Gaffin, SL5
  • 28
    • 33646084611 scopus 로고    scopus 로고
    • Oral glutamine enhances heat shock protein expression and improves survival following hyperthermia
    • KD Singleton PE Wischmeyer Oral glutamine enhances heat shock protein expression and improves survival following hyperthermia Shock 25 2006 295 299
    • (2006) Shock , vol.25 , pp. 295-299
    • Singleton, KD1    Wischmeyer, PE2
  • 29
    • 33644856858 scopus 로고    scopus 로고
    • Physiologically relevant increase in temperature causes an increase in intestinal epithelial tight junction permeability
    • K Dokladny PL Moseley TY Ma Physiologically relevant increase in temperature causes an increase in intestinal epithelial tight junction permeability Am J Physiol 290 2006 G204 G212
    • (2006) Am J Physiol , vol.290 , pp. G204-G212
    • Dokladny, K1    Moseley, PL2    Ma, TY3
  • 30
    • 33748416881 scopus 로고    scopus 로고
    • Induction of physiological thermotolerance in MDCK monolayers: contribution of heat shock protein 70
    • K Dokladny W Wharton R Lobb TY Ma PL Moseley Induction of physiological thermotolerance in MDCK monolayers: contribution of heat shock protein 70 Cell Stress Chaperones 11 2006 268 275
    • (2006) Cell Stress Chaperones , vol.11 , pp. 268-275
    • Dokladny, K1    Wharton, W2    Lobb, R3    Ma, TY4    Moseley, PL5
  • 31
    • 0024593744 scopus 로고
    • Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability
    • IJ Hidalgo TJ Raub RT Borchardt Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability Gastroenterology 96 1989 736 749
    • (1989) Gastroenterology , vol.96 , pp. 736-749
    • Hidalgo, IJ1    Raub, TJ2    Borchardt, RT3
  • 32
    • 0032861253 scopus 로고    scopus 로고
    • Biosynthesis and secretion of the mannose 6-phosphate receptor and its ligands in polarized Caco-2 cells
    • DA Wick B Seetharam NM Dahms Biosynthesis and secretion of the mannose 6-phosphate receptor and its ligands in polarized Caco-2 cells Am J Physiol 277 1999 G506 G514
    • (1999) Am J Physiol , vol.277 , pp. G506-G514
    • Wick, DA1    Seetharam, B2    Dahms, NM3
  • 33
    • 0027014940 scopus 로고
    • Secreted placental alkaline phosphatase as a eukaryotic reporter gene
    • BR Cullen MH Malim Secreted placental alkaline phosphatase as a eukaryotic reporter gene Methods Enzymol 216 1992 362 368
    • (1992) Methods Enzymol , vol.216 , pp. 362-368
    • Cullen, BR1    Malim, MH2
  • 34
    • 33644981348 scopus 로고    scopus 로고
    • Molecular mechanism of tumor necrosis factor-alpha modulation of intestinal epithelial tight junction barrier
    • D Ye I Ma TY Ma Molecular mechanism of tumor necrosis factor-alpha modulation of intestinal epithelial tight junction barrier Am J Physiol 290 2006 G496 G504
    • (2006) Am J Physiol , vol.290 , pp. G496-G504
    • Ye, D1    Ma, I2    Ma, TY3
  • 35
    • 0041976029 scopus 로고    scopus 로고
    • The use of real-time reverse transcriptase PCR for the quantification of cytokine gene expression
    • L Overbergh A Giulietti D Valckx R Decallonne R Bouillon C Mathieu The use of real-time reverse transcriptase PCR for the quantification of cytokine gene expression J Biomol Tech 14 2003 33 43
    • (2003) J Biomol Tech , vol.14 , pp. 33-43
    • Overbergh, L1    Giulietti, A2    Valckx, D3    Decallonne, R4    Bouillon, R5    Mathieu, C6
  • 36
    • 17644378093 scopus 로고    scopus 로고
    • Lipopolysaccharide induces 5-lipoxygenase-activating protein gene expression in THP-1 cells via a NF-kappaB and C/EBP-mediated mechanism
    • KJ Serio KV Reddy TD Bigby Lipopolysaccharide induces 5-lipoxygenase-activating protein gene expression in THP-1 cells via a NF-kappaB and C/EBP-mediated mechanism Am J Physiol 288 2005 C1125 C1133
    • (2005) Am J Physiol , vol.288 , pp. C1125-C1133
    • Serio, KJ1    Reddy, KV2    Bigby, TD3
  • 37
    • 0034099223 scopus 로고    scopus 로고
    • Restoration of tight junction structure and barrier function by down-regulation of the mitogen-activated protein kinase pathway in ras-transformed Madin-Darby canine kidney cells
    • Y Chen Q Lu EE Schneeberger DA Goodenough Restoration of tight junction structure and barrier function by down-regulation of the mitogen-activated protein kinase pathway in ras-transformed Madin-Darby canine kidney cells Mol Biol Cell 11 2000 849 862
    • (2000) Mol Biol Cell , vol.11 , pp. 849-862
    • Chen, Y1    Lu, Q2    Schneeberger, EE3    Goodenough, DA4
  • 38
    • 0030844237 scopus 로고    scopus 로고
    • Role of the 5.8S rRNA in ribosome translocation
    • S Abou Elela RN Nazar Role of the 5.8S rRNA in ribosome translocation Nucleic Acids Res 25 1997 1788 1794
    • (1997) Nucleic Acids Res , vol.25 , pp. 1788-1794
    • Abou Elela, S1    Nazar, RN2
  • 39
    • 0026055736 scopus 로고
    • Actinomycin D and 7-aminoactinomycin D binding to single-stranded DNA
    • RM Wadkins TM Jovin Actinomycin D and 7-aminoactinomycin D binding to single-stranded DNA Biochemistry 30 1991 9469 9478
    • (1991) Biochemistry , vol.30 , pp. 9469-9478
    • Wadkins, RM1    Jovin, TM2
  • 40
    • 0027522356 scopus 로고
    • Cells in stress: transcriptional activation of heat shock genes
    • RI Morimoto Cells in stress: transcriptional activation of heat shock genes Science 259 1993 1409 1410
    • (1993) Science , vol.259 , pp. 1409-1410
    • Morimoto, RI1
  • 41
    • 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
    • KD Sarge SP Murphy RI Morimoto 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 1993 1392 1407
    • (1993) Mol Cell Biol , vol.13 , pp. 1392-1407
    • Sarge, KD1    Murphy, SP2    Morimoto, RI3
  • 42
    • 0028951778 scopus 로고
    • Quercetin suppresses heat shock response by down regulation of HSF1
    • N Nagai A Nakai K Nagata Quercetin suppresses heat shock response by down regulation of HSF1 Biochem Biophys Res Commun 208 1995 1099 1105
    • (1995) Biochem Biophys Res Commun , vol.208 , pp. 1099-1105
    • Nagai, N1    Nakai, A2    Nagata, K3
  • 43
    • 0033534750 scopus 로고    scopus 로고
    • Proteasome inhibitors MG132 and lactacystin hyperphosphorylate HSF1 and induce hsp70 and hsp27 expression
    • D Kim SH Kim GC Li Proteasome inhibitors MG132 and lactacystin hyperphosphorylate HSF1 and induce hsp70 and hsp27 expression Biochem Biophys Res Commun 254 1999 264 268
    • (1999) Biochem Biophys Res Commun , vol.254 , pp. 264-268
    • Kim, D1    Kim, SH2    Li, GC3
  • 44
    • 0026755773 scopus 로고
    • Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoids
    • N Hosokawa K Hirayoshi H Kudo H Takechi A Aoike K Kawai K Nagata Inhibition of the activation of heat shock factor in vivo and in vitro by flavonoids Mol Cell Biol 12 1992 3490 3498
    • (1992) Mol Cell Biol , vol.12 , pp. 3490-3498
    • Hosokawa, N1    Hirayoshi, K2    Kudo, H3    Takechi, H4    Aoike, A5    Kawai, K6    Nagata, K7
  • 46
    • 0027220589 scopus 로고
    • Protein traffic on the heat shock promoter: parking, stalling, and trucking along
    • J Lis C Wu Protein traffic on the heat shock promoter: parking, stalling, and trucking along Cell 74 1993 1 4
    • (1993) Cell , vol.74 , pp. 1-4
    • Lis, J1    Wu, C2
  • 47
    • 0028966256 scopus 로고
    • Transduction of the stress signal and mechanisms of transcriptional regulation of heat shock/stress protein gene expression in higher eukaryotes
    • R Voellmy Transduction of the stress signal and mechanisms of transcriptional regulation of heat shock/stress protein gene expression in higher eukaryotes Crit Rev Eukaryot Gene Expr 4 1994 357 401
    • (1994) Crit Rev Eukaryot Gene Expr , vol.4 , pp. 357-401
    • Voellmy, R1
  • 48
    • 33744822167 scopus 로고    scopus 로고
    • Glutamine's protection against cellular injury is dependent on heat shock factor-1
    • AL Morrison M Dinges KD Singleton K Odoms HR Wong PE Wischmeyer Glutamine's protection against cellular injury is dependent on heat shock factor-1 Am J Physiol 290 2006 C1625 C1632
    • (2006) Am J Physiol , vol.290 , pp. C1625-C1632
    • Morrison, AL1    Dinges, M2    Singleton, KD3    Odoms, K4    Wong, HR5    Wischmeyer, PE6
  • 49
    • 0027474909 scopus 로고
    • Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1
    • R Baler G Dahl R Voellmy Activation of human heat shock genes is accompanied by oligomerization, modification, and rapid translocation of heat shock transcription factor HSF1 Mol Cell Biol 13 1993 2486 2496
    • (1993) Mol Cell Biol , vol.13 , pp. 2486-2496
    • Baler, R1    Dahl, G2    Voellmy, R3
  • 50
    • 0029683566 scopus 로고    scopus 로고
    • The transcriptional regulation of heat shock genes: a plethora of heat shock factors and regulatory conditions
    • RI Morimoto PE Kroeger JJ Cotto The transcriptional regulation of heat shock genes: a plethora of heat shock factors and regulatory conditions EXS 77 1996 139 163
    • (1996) EXS , vol.77 , pp. 139-163
    • Morimoto, RI1    Kroeger, PE2    Cotto, JJ3
  • 51
    • 0029680415 scopus 로고    scopus 로고
    • Sensing stress and responding to stress
    • R Voellmy Sensing stress and responding to stress EXS 77 1996 121 137
    • (1996) EXS , vol.77 , pp. 121-137
    • Voellmy, R1
  • 53
    • 0030043401 scopus 로고    scopus 로고
    • Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation
    • JJ Cotto M Kline RI Morimoto Activation of heat shock factor 1 DNA binding precedes stress-induced serine phosphorylation. Evidence for a multistep pathway of regulation J Biol Chem 271 1996 3355 3358
    • (1996) J Biol Chem , vol.271 , pp. 3355-3358
    • Cotto, JJ1    Kline, M2    Morimoto, RI3
  • 54
    • 0032535245 scopus 로고    scopus 로고
    • Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators
    • RI Morimoto Regulation of the heat shock transcriptional response: cross talk between a family of heat shock factors, molecular chaperones, and negative regulators Genes Dev 12 1998 3788 3796
    • (1998) Genes Dev , vol.12 , pp. 3788-3796
    • Morimoto, RI1
  • 55
    • 0031055277 scopus 로고    scopus 로고
    • Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers
    • W Xia R Voellmy Hyperphosphorylation of heat shock transcription factor 1 is correlated with transcriptional competence and slow dissociation of active factor trimers J Biol Chem 272 1997 4094 4102
    • (1997) J Biol Chem , vol.272 , pp. 4094-4102
    • Xia, W1    Voellmy, R2
  • 56
    • 18244384703 scopus 로고    scopus 로고
    • Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress
    • T Guettouche F Boellmann WS Lane R Voellmy Analysis of phosphorylation of human heat shock factor 1 in cells experiencing a stress BMC Biochem 6 2005 4
    • (2005) BMC Biochem , vol.6 , pp. 4
    • Guettouche, T1    Boellmann, F2    Lane, WS3    Voellmy, R4
  • 57
    • 0032571397 scopus 로고    scopus 로고
    • Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis
    • DR McMillan X Xiao L Shao K Graves IJ Benjamin Targeted disruption of heat shock transcription factor 1 abolishes thermotolerance and protection against heat-inducible apoptosis J Biol Chem 273 1998 7523 7528
    • (1998) J Biol Chem , vol.273 , pp. 7523-7528
    • McMillan, DR1    Xiao, X2    Shao, L3    Graves, K4    Benjamin, IJ5
  • 58
    • 0036892818 scopus 로고    scopus 로고
    • Ablation of the heat shock factor-1 increases susceptibility to hyperoxia-mediated cellular injury
    • V Malhotra NW Kooy AG Denenberg KE Dunsmore HR Wong Ablation of the heat shock factor-1 increases susceptibility to hyperoxia-mediated cellular injury Exp Lung Res 28 2002 609 622
    • (2002) Exp Lung Res , vol.28 , pp. 609-622
    • Malhotra, V1    Kooy, NW2    Denenberg, AG3    Dunsmore, KE4    Wong, HR5
  • 59
    • 0141671923 scopus 로고    scopus 로고
    • Use of Hsf1(−/−) mice reveals an essential role for HSF1 to protect lung against cadmium-induced injury
    • D Wirth E Christians X Li IJ Benjamin P Gustin Use of Hsf1(−/−) mice reveals an essential role for HSF1 to protect lung against cadmium-induced injury Toxicol Appl Pharmacol 192 2003 12 20
    • (2003) Toxicol Appl Pharmacol , vol.192 , pp. 12-20
    • Wirth, D1    Christians, E2    Li, X3    Benjamin, IJ4    Gustin, P5
  • 60
    • 0033229880 scopus 로고    scopus 로고
    • HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice
    • X Xiao X Zuo AA Davis DR McMillan BB Curry JA Richardson IJ Benjamin HSF1 is required for extra-embryonic development, postnatal growth and protection during inflammatory responses in mice EMBO J 18 1999 5943 5952
    • (1999) EMBO J , vol.18 , pp. 5943-5952
    • Xiao, X1    Zuo, X2    Davis, AA3    McMillan, DR4    Curry, BB5    Richardson, JA6    Benjamin, IJ7
  • 61
    • 0037281331 scopus 로고    scopus 로고
    • Quercetin suppresses proinflammatory cytokines production through MAP kinases and NF-kappaB pathway in lipopolysaccharide-stimulated macrophage
    • SY Cho SJ Park MJ Kwon TS Jeong SH Bok WY Choi WI Jeong SY Ryu SH Do CS Lee JC Song KS Jeong Quercetin suppresses proinflammatory cytokines production through MAP kinases and NF-kappaB pathway in lipopolysaccharide-stimulated macrophage Mol Cell Biochem 243 2003 153 160
    • (2003) Mol Cell Biochem , vol.243 , pp. 153-160
    • Cho, SY1    Park, SJ2    Kwon, MJ3    Jeong, TS4    Bok, SH5    Choi, WY6    Jeong, WI7    Ryu, SY8    Do, SH9    Lee, CS10    Song, JC11    Jeong, KS12
  • 62
    • 33645299344 scopus 로고    scopus 로고
    • The inhibitory effect of quercetin on IL-6 production by LPS-stimulated neutrophils
    • J Liu X Li Y Yue J Li T He Y He The inhibitory effect of quercetin on IL-6 production by LPS-stimulated neutrophils Cell Mol Immunol 2 2005 455 460
    • (2005) Cell Mol Immunol , vol.2 , pp. 455-460
    • Liu, J1    Li, X2    Yue, Y3    Li, J4    He, T5    He, Y6
  • 63
    • 14744294057 scopus 로고    scopus 로고
    • In vivo quercitrin anti-inflammatory effect involves release of quercetin, which inhibits inflammation through down-regulation of the NF-kappaB pathway
    • M Comalada D Camuesco S Sierra I Ballester J Xaus J Galvez A Zarzuelo In vivo quercitrin anti-inflammatory effect involves release of quercetin, which inhibits inflammation through down-regulation of the NF-kappaB pathway Eur J Immunol 35 2005 584 592
    • (2005) Eur J Immunol , vol.35 , pp. 584-592
    • Comalada, M1    Camuesco, D2    Sierra, S3    Ballester, I4    Xaus, J5    Galvez, J6    Zarzuelo, A7
  • 64
    • 0032729498 scopus 로고    scopus 로고
    • Bioflavonoid quercetin inhibits interleukin-1-induced transcriptional expression of monocyte chemoattractant protein-1 in glomerular cells via suppression of nuclear factor-kappaB
    • Y Ishikawa H Sugiyama E Stylianou M Kitamura Bioflavonoid quercetin inhibits interleukin-1-induced transcriptional expression of monocyte chemoattractant protein-1 in glomerular cells via suppression of nuclear factor-kappaB J Am Soc Nephrol 10 1999 2290 2296
    • (1999) J Am Soc Nephrol , vol.10 , pp. 2290-2296
    • Ishikawa, Y1    Sugiyama, H2    Stylianou, E3    Kitamura, M4
  • 65
    • 33645836334 scopus 로고    scopus 로고
    • The antiproliferative effect of quercetin in cancer cells is mediated via inhibition of the PI3K-Akt/PKB pathway
    • N Gulati B Laudet VM Zohrabian R Murali M Jhanwar-Uniyal The antiproliferative effect of quercetin in cancer cells is mediated via inhibition of the PI3K-Akt/PKB pathway Anticancer Res 26 2006 1177 1181
    • (2006) Anticancer Res , vol.26 , pp. 1177-1181
    • Gulati, N1    Laudet, B2    Zohrabian, VM3    Murali, R4    Jhanwar-Uniyal, M5
  • 67
    • 20344382953 scopus 로고    scopus 로고
    • Quercetin, but not rutin and quercitrin, prevention of H2O2-induced apoptosis via anti-oxidant activity and heme oxygenase 1 gene expression in macrophages
    • JM Chow SC Shen SK Huan HY Lin YC Chen Quercetin, but not rutin and quercitrin, prevention of H2O2-induced apoptosis via anti-oxidant activity and heme oxygenase 1 gene expression in macrophages Biochem Pharmacol 69 2005 1839 1851
    • (2005) Biochem Pharmacol , vol.69 , pp. 1839-1851
    • Chow, JM1    Shen, SC2    Huan, SK3    Lin, HY4    Chen, YC5


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