메뉴 건너뛰기




Volumn 177, Issue 3, 2010, Pages 1198-1213

Cigarette smoke-related hydroquinone induces filamentous actin reorganization and heat shock protein 27 phosphorylation through p38 and extracellular signal-regulated kinase 1/2 in retinal pigment epithelium: Implications for age-related macular degeneration

Author keywords

[No Author keywords available]

Indexed keywords

BETA ACTIN; CIGARETTE SMOKE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 25; HEAT SHOCK PROTEIN 27; HYDROQUINONE; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38;

EID: 77956518441     PISSN: 00029440     EISSN: 15252191     Source Type: Journal    
DOI: 10.2353/ajpath.2010.091108     Document Type: Article
Times cited : (38)

References (65)
  • 2
    • 0035128064 scopus 로고    scopus 로고
    • Risk Factors for age-related macular degeneration
    • DOI 10.1016/S1350-9462(00)00023-9, PII S1350946200000239
    • Evans JR: Risk factors for age-related macular degeneration. Prog Retin Eye Res 2001, 20:227-253 (Pubitemid 32149928)
    • (2001) Progress in Retinal and Eye Research , vol.20 , Issue.2 , pp. 227-253
    • Evans, J.R.1
  • 3
    • 0042029472 scopus 로고    scopus 로고
    • Incidence of exudative age-related macular degeneration among elderly Americans
    • DOI 10.1016/S0161-6420(03)00495-0
    • Javitt JC, Zhou Z, Maguire MG, Fine SL, Willke RJ: Incidence of exudative age-related macular degeneration among elderly Americans. Ophthalmology 2003, 110:1534-1539 (Pubitemid 36962485)
    • (2003) Ophthalmology , vol.110 , Issue.8 , pp. 1534-1539
    • Javitt, J.C.1    Zhou, Z.2    Maguire, M.G.3    Fine, S.L.4    Willke, R.J.5
  • 4
    • 1542297335 scopus 로고    scopus 로고
    • The epidemiology of age-related macular degeneration
    • Klein R, Peto T, Bird A, Vannewkirk MR: The epidemiology of age-related macular degeneration. Am J Ophthalmol 2004, 137:486-495
    • (2004) Am J Ophthalmol , vol.137 , pp. 486-495
    • Klein, R.1    Peto, T.2    Bird, A.3    Vannewkirk, M.R.4
  • 5
    • 77951916610 scopus 로고    scopus 로고
    • The molecular genetic basis of age-related macular degeneration: An overview
    • Katta S, Kaur I, Chakrabarti S: The molecular genetic basis of age-related macular degeneration: an overview. J Genet 2009, 88:425-449
    • (2009) J Genet , vol.88 , pp. 425-449
    • Katta, S.1    Kaur, I.2    Chakrabarti, S.3
  • 6
    • 0033520641 scopus 로고    scopus 로고
    • Histopathology of age-related macular degeneration
    • Green WR: Histopathology of age-related macular degeneration. Mol Vis 1999, 5:27-36
    • (1999) Mol Vis , vol.5 , pp. 27-36
    • Green, W.R.1
  • 8
    • 0033795036 scopus 로고    scopus 로고
    • The role of oxidative stress in the pathogenesis of age-related macular degeneration
    • Beatty S, Koh H, Phil M, Henson D, Boulton M: The role of oxidative stress in the pathogenesis of age-related macular degeneration. Surv Ophthalmol 2000, 45:115-134
    • (2000) Surv Ophthalmol , vol.45 , pp. 115-134
    • Beatty, S.1    Koh, H.2    Phil, M.3    Henson, D.4    Boulton, M.5
  • 9
    • 16244368037 scopus 로고    scopus 로고
    • Risk factors for the incidence of advanced age-related macular degeneration in the Age-Related Eye Disease Study (AREDS): AREDS report no. 19
    • DOI 10.1016/j.ophtha.2004.10.047, PII S0161642004017944
    • Clemons TE, Milton RC, Klein R, Seddon JM, Ferris FL, 3rd: Risk factors for the incidence of advanced age-related macular degeneration in the Age-Related Eye Disease Study (AREDS) AREDS report no. 19. Ophthalmology 2005, 112:533-539 (Pubitemid 41108849)
    • (2005) Ophthalmology , vol.112 , Issue.4 , pp. 533-539
    • Milton, R.C.1    Clemons, T.E.2    Klien, R.3    Seddon, J.M.4    Ferris III, F.L.5
  • 13
    • 0032518733 scopus 로고    scopus 로고
    • Relation of smoking to the incidence of age-related maculopathy. The beaver dam eye study
    • Klein R, Klein BE, Moss SE: Relation of smoking to the incidence of age-related maculopathy: the Beaver Dam Eye Study. Am J Epidemiol 1998, 147:103-110 (Pubitemid 28060479)
    • (1998) American Journal of Epidemiology , vol.147 , Issue.2 , pp. 103-110
    • Klein, R.1    Klein, B.E.K.2    Moss, S.E.3
  • 14
    • 0031595250 scopus 로고    scopus 로고
    • The association betwen cigarette smoking and ocular diseases
    • DOI 10.1016/S0039-6257(98)00002-2, PII S0039625798000022
    • Solberg Y, Rosner M, Belkin M: The association between cigarette smoking and ocular diseases. Surv Ophthalmol 1998, 42:535-547 (Pubitemid 28272741)
    • (1998) Survey of Ophthalmology , vol.42 , Issue.6 , pp. 535-547
    • Solberg, Y.1    Rosner, M.2    Belkin, M.3
  • 15
    • 70449644673 scopus 로고    scopus 로고
    • Molecular regulation of cigarette smoke induced-oxidative stress in human retinal pigment epithelial cells: Implications for age-related macular degeneration
    • Bertram KM, Baglole CJ, Phipps RP, Libby RT: Molecular regulation of cigarette smoke induced-oxidative stress in human retinal pigment epithelial cells: implications for age-related macular degeneration. Am J Physiol Cell Physiol 2009, 297:C1200-C1210
    • (2009) Am J Physiol Cell Physiol , vol.297
    • Bertram, K.M.1    Baglole, C.J.2    Phipps, R.P.3    Libby, R.T.4
  • 17
    • 0033022871 scopus 로고    scopus 로고
    • The toxicology of hydroquinone - Relevance to occupational and environmental exposure
    • DOI 10.1080/10408449991349221
    • DeCaprio AP: The toxicology of hydroquinone: relevance to occupational and environmental exposure. Crit Rev Toxicol 1999, 29:283-330 (Pubitemid 29262956)
    • (1999) Critical Reviews in Toxicology , vol.29 , Issue.3 , pp. 283-330
    • DeCaprio, A.P.1
  • 18
    • 0019231760 scopus 로고
    • Clinico-morphologic correlations of drusen of Bruch's membrane
    • Burns RP, Feeney-Burns L: Clinico-morphologic correlations of drusen of Bruch's membrane. Trans Am Ophthalmol Soc 1980, 78:206-225
    • (1980) Trans Am Ophthalmol Soc , vol.78 , pp. 206-225
    • Burns, R.P.1    Feeney-Burns, L.2
  • 20
    • 34047244381 scopus 로고    scopus 로고
    • Relationship of basal laminar deposit and membranous debris to the clinical presentation of early age-related macular degeneration
    • DOI 10.1167/iovs.06-0443
    • Sarks S, Cherepanoff S, Killingsworth M, Sarks J: Relationship of Basal laminar deposit and membranous debris to the clinical presentation of early age-related macular degeneration. Invest Ophthalmol Vis Sci 2007, 48:968-977 (Pubitemid 351261384)
    • (2007) Investigative Ophthalmology and Visual Science , vol.48 , Issue.3 , pp. 968-977
    • Sarks, S.1    Cherepanoff, S.2    Killingsworth, M.3    Sarks, J.4
  • 23
    • 38549098235 scopus 로고    scopus 로고
    • MMP-14 and TIMP-2 overexpression protects against hydroquinone-induced oxidant injury in RPE: Implications for extracellular matrix turnover
    • DOI 10.1167/iovs.07-0392
    • Alcazar O, Cousins SW, Marin-Castano ME: MMP-14 and TIMP-2 overexpression protects against hydroquinone-induced oxidant injury in RPE: implications for extracellular matrix turnover. Invest Ophthalmol Vis Sci 2007, 48:5662-5670 (Pubitemid 351260869)
    • (2007) Investigative Ophthalmology and Visual Science , vol.48 , Issue.12 , pp. 5662-5670
    • Alcazar, O.1    Cousins, S.W.2    Marin-Castano, M.E.3
  • 24
    • 27244452645 scopus 로고    scopus 로고
    • Nonlethal oxidant injury to human retinal pigment epithelium cells causes cell membrane blebbing but decreased MMP-2 activity
    • Marin-Castano ME, Csaky KG, Cousins SW: Nonlethal oxidant injury to human retinal pigment epithelium cells causes cell membrane blebbing but decreased MMP-2 activity. Invest Ophthalmol Vis Sci 2005, 46:3331-3340
    • (2005) Invest Ophthalmol Vis Sci , vol.46 , pp. 3331-3340
    • Marin-Castano, M.E.1    Csaky, K.G.2    Cousins, S.W.3
  • 26
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/heat shock protein 27 pathway in vascular endothelial cells
    • Huot J, Houle F, Marceau F, Landry J: Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated protein kinase/ heat shock protein 27 pathway in vascular endothelial cells. Circ Res 1997, 80:383-392 (Pubitemid 27093353)
    • (1997) Circulation Research , vol.80 , Issue.3 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 27
    • 0035893961 scopus 로고    scopus 로고
    • The actin cytoskeleton response to oxidants: From small heat shock protein phosphorylation to changes in the redox state of actin itself
    • DOI 10.1016/S0891-5849(01)00749-3, PII S0891584901007493
    • Dalle-Donne I, Rossi R, Milzani A, Di Simplicio P, Colombo R: The actin cytoskeleton response to oxidants: from small heat shock protein phosphorylation to changes in the redox state of actin itself. Free Radic Biol Med 2001, 31:1624-1632 (Pubitemid 34024985)
    • (2001) Free Radical Biology and Medicine , vol.31 , Issue.12 , pp. 1624-1632
    • Dalle-Donne, I.1    Rossi, R.2    Milzani, A.3    Di Simplicio, P.4    Colombo, R.5
  • 29
    • 0032583203 scopus 로고    scopus 로고
    • SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis
    • DOI 10.1083/jcb.143.5.1361
    • Huot J, Houle F, Rousseau S, Deschesnes RG, Shah GM, Landry J: SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis. J Cell Biol 1998, 143:1361-1373 (Pubitemid 28559836)
    • (1998) Journal of Cell Biology , vol.143 , Issue.5 , pp. 1361-1373
    • Huot, J.1    Houle, F.2    Rousseau, S.3    Deschesnes, R.G.4    Shah, G.M.5    Landry, J.6
  • 30
    • 0028071812 scopus 로고
    • Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity
    • Benndorf R, Hayess K, Ryazantsev S, Wieske M, Behlke J, Lutsch G: Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J Biol Chem 1994, 269:20780-20784 (Pubitemid 24260495)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.32 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3    Wieske, M.4    Behlke, J.5    Lutsch, G.6
  • 32
    • 67349098413 scopus 로고    scopus 로고
    • Angiotensin II-induced hypertension regulates AT1 receptor subtypes and extracellular matrix turnover in mouse retinal pigment epithelium
    • Praddaude F, Cousins SW, Pecher C, Marin-Castano ME: Angiotensin II-induced hypertension regulates AT1 receptor subtypes and extracellular matrix turnover in mouse retinal pigment epithelium. Exp Eye Res 2009, 89:109-118
    • (2009) Exp Eye Res , vol.89 , pp. 109-118
    • Praddaude, F.1    Cousins, S.W.2    Pecher, C.3    Marin-Castano, M.E.4
  • 33
    • 0029872876 scopus 로고    scopus 로고
    • ARPE-19, a human retinal pigment epithelial cell line with differentiated properties
    • DOI 10.1006/exer.1996.0020
    • Dunn KC, Aotaki-Keen AE, Putkey FR, Hjelmeland LM: ARPE-19, a human retinal pigment epithelial cell line with differentiated properties. Exp Eye Res 1996, 62:155-169 (Pubitemid 26140102)
    • (1996) Experimental Eye Research , vol.62 , Issue.2 , pp. 155-169
    • Dunn, K.C.1    Aotaki-Keen, A.E.2    Putkey, F.R.3    Hjelmeland, L.M.4
  • 34
    • 0037057530 scopus 로고    scopus 로고
    • A potential role of heat shock proteins and nicotinamide N-methyl transferase in predicting response to radiation in bladder cancer
    • Kassem H, Sangar V, Cowan R, Clarke N, Margison GP: A potential role of heat shock proteins and nicotinamide N-methyl transferase in predicting response to radiation in bladder cancer. Int J Cancer 2002, 101:454-460
    • (2002) Int J Cancer , vol.101 , pp. 454-460
    • Kassem, H.1    Sangar, V.2    Cowan, R.3    Clarke, N.4    Margison, G.P.5
  • 35
    • 33747040122 scopus 로고    scopus 로고
    • Heat shock inhibits both aminoglycoside- and cisplatin-induced sensory hair cell death
    • Cunningham LL, Brandon CS: Heat shock inhibits both aminoglycoside- and cisplatin-induced sensory hair cell death. J Assoc Res Otolaryngol 2006, 7:299-307
    • (2006) J Assoc Res Otolaryngol , vol.7 , pp. 299-307
    • Cunningham, L.L.1    Brandon, C.S.2
  • 36
    • 0037129827 scopus 로고    scopus 로고
    • Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes
    • RESEARCH0034
    • Vandesompele J, De Preter K, Pattyn F, Poppe B, Van Roy N, De Paepe A, Speleman F: Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol 2002, 3:RESEARCH0034
    • (2002) Genome Biol , vol.3
    • Vandesompele, J.1    De Preter, K.2    Pattyn, F.3    Poppe, B.4    Van Roy, N.5    De Paepe, A.6    Speleman, F.7
  • 37
    • 0035710746 scopus 로고    scopus 로고
    • -DeltaDeltaCT method
    • DOI 10.1006/meth.2001.1262
    • Livak KJ, Schmittgen TD: Analysis of relative gene expression data using real-time quantitative PCR and the 2(-Delta Delta C(T)) method. Methods 2001, 25:402-408 (Pubitemid 34164012)
    • (2001) Methods , vol.25 , Issue.4 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 38
    • 0028286541 scopus 로고
    • Dephosphorylation of the small heat shock protein Hsp27 in vivo by protein phosphatase 2A
    • Cairns J, Qin S, Philp R, Tan YH, Guy GR: Dephosphorylation of the small heat shock protein Hsp27 in vivo by protein phosphatase 2A. J Biol Chem 1994, 269:9176-9183 (Pubitemid 24209242)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.12 , pp. 9176-9183
    • Cairns, J.1    Qin, S.2    Philp, R.3    Tan, Y.H.4    Guy, G.R.5
  • 39
    • 3042739490 scopus 로고    scopus 로고
    • Oxidative stress causes ERK phosphorylation and cell death in cultured retinal pigment epithelium: Prevention of cell death by AG126 and 15-deoxy-delta 12, 14-PGJ2
    • Garg TK, Chang JY: Oxidative stress causes ERK phosphorylation and cell death in cultured retinal pigment epithelium: prevention of cell death by AG126 and 15-deoxy-delta 12, 14-PGJ2. BMC Ophthalmol 2003, 3:5-20
    • (2003) BMC Ophthalmol , vol.3 , pp. 5-20
    • Garg, T.K.1    Chang, J.Y.2
  • 41
    • 0034671847 scopus 로고    scopus 로고
    • The p38 pathway provides negative feedback for ras proliferative signaling
    • DOI 10.1074/jbc.M002856200
    • Chen G, Hitomi M, Han J, Stacey DW: The p38 pathway provides negative feedback for Ras proliferative signaling. J Biol Chem 2000, 275:38973-38980 (Pubitemid 32058908)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.50 , pp. 38973-38980
    • Chen, G.1    Hitomi, M.2    Han, J.3    Stacey, D.W.4
  • 43
    • 0034746841 scopus 로고    scopus 로고
    • SB203580 promote EGF-stimulated early morphological differentiation in PC12 cell through activating ERK pathway
    • DOI 10.1002/jcb.1253
    • New L, Li Y, Ge B, Zhong H, Mansbridge J, Liu K, Han J: SB203580 promotes EGF-stimulated early morphological differentiation in PC12 cell through activating ERK pathway. J Cell Biochem 2001, 83:585-596 (Pubitemid 33055436)
    • (2001) Journal of Cellular Biochemistry , vol.83 , Issue.4 , pp. 585-596
    • New, L.1    Li, Y.2    Ge, B.3    Zhong, H.4    Mansbridge, J.5    Liu, K.6    Han, J.7
  • 45
    • 0037632950 scopus 로고    scopus 로고
    • Regulation of ERK-mediated signal transduction by p38 MAP kinase in human monocytic THP-1 cells
    • DOI 10.1093/jb/mvg077
    • Numazawa S, Watabe M, Nishimura S, Kurosawa M, Izuno M, Yoshida T: Regulation of ERK-mediated signal transduction by p38 MAP kinase in human monocytic THP-1 cells. J Biochem 2003, 133:599-605 (Pubitemid 36759467)
    • (2003) Journal of Biochemistry , vol.133 , Issue.5 , pp. 599-605
    • Numazawa, S.1    Watabe, M.2    Nishimura, S.3    Kurosawa, M.4    Izuno, M.5    Yoshida, T.6
  • 46
    • 67049158005 scopus 로고    scopus 로고
    • Phosphoproteome study reveals Hsp27 as a novel signaling molecule involved in GDNF-induced neurite outgrowth
    • Hong Z, Zhang QY, Liu J, Wang ZQ, Zhang Y, Xiao Q, Lu J, Zhou HY, Chen S: Phosphoproteome study reveals Hsp27 as a novel signaling molecule involved in GDNF-induced neurite outgrowth. J Proteome Res 2009, 8:2768-2787
    • (2009) J Proteome Res , vol.8 , pp. 2768-2787
    • Hong, Z.1    Zhang, Q.Y.2    Liu, J.3    Wang, Z.Q.4    Zhang, Y.5    Xiao, Q.6    Lu, J.7    Zhou, H.Y.8    Chen, S.9
  • 47
    • 33751078036 scopus 로고    scopus 로고
    • UVB irradiation-induced changes in the 27-kd heat shock protein (HSP27) in human corneal epithelial cells
    • DOI 10.1097/01.ico.0000224643.43601.5d, PII 0000322620060900000017
    • Shi B, Han B, Schwab IR, Isseroff RR: UVB irradiation-induced changes in the 27-kd heat shock protein (HSP27) in human corneal epithelial cells. Cornea 2006, 25:948-955 (Pubitemid 44763857)
    • (2006) Cornea , vol.25 , Issue.8 , pp. 948-955
    • Shi, B.1    Han, B.2    Schwab, I.R.3    Isseroff, R.R.4
  • 48
    • 0034895095 scopus 로고    scopus 로고
    • In situ immunohistochemical study of Bcl-2 and heat shock proteins in human corneal endothelial cells during corneal storage
    • Gain P, Thuret G, Chiquet C, Dumollard JM, Mosnier JF, Campos L: In situ immunohistochemical study of Bcl-2 and heat shock proteins in human corneal endothelial cells during corneal storage. Br J Ophthalmol 2001, 85:996-1000
    • (2001) Br J Ophthalmol , vol.85 , pp. 996-1000
    • Gain, P.1    Thuret, G.2    Chiquet, C.3    Dumollard, J.M.4    Mosnier, J.F.5    Campos, L.6
  • 49
    • 70350474677 scopus 로고    scopus 로고
    • Heat shock protein 27 phosphorylation: Kinases, phosphatases, functions and pathology
    • Kostenko S, Moens U: Heat shock protein 27 phosphorylation: kinases, phosphatases, functions and pathology. Cell Mol Life Sci 2009, 66:3289-3307
    • (2009) Cell Mol Life Sci , vol.66 , pp. 3289-3307
    • Kostenko, S.1    Moens, U.2
  • 50
    • 33947383078 scopus 로고    scopus 로고
    • Changes in select redox proteins of the retinal pigment epithelium in age-related macular degeneration
    • Decanini A, Nordgaard CL, Feng X, Ferrington DA, Olsen TW: Changes in select redox proteins of the retinal pigment epithelium in age-related macular degeneration. Am J Ophthalmol 2007, 143:607-615
    • (2007) Am J Ophthalmol , vol.143 , pp. 607-615
    • Decanini, A.1    Nordgaard, C.L.2    Feng, X.3    Ferrington, D.A.4    Olsen, T.W.5
  • 51
    • 0028924759 scopus 로고
    • Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27
    • Lavoie JN, Lambert H, Hickey E, Weber LA, Landry J: Modulation of cellular thermoresistance and actin filament stability accompanies phosphorylation-induced changes in the oligomeric structure of heat shock protein 27. Mol Cell Biol 1995, 15:505-516 (Pubitemid 24379949)
    • (1995) Molecular and Cellular Biology , vol.15 , Issue.1 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3    Weber, L.A.4    Landry, J.5
  • 52
    • 0031056783 scopus 로고    scopus 로고
    • Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27
    • Guay J, Lambert H, Gingras-Breton G, Lavoie JN, Huot J, Landry J: Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci 1997, 110 (Pt 3):357-368 (Pubitemid 27095655)
    • (1997) Journal of Cell Science , vol.110 , Issue.3 , pp. 357-368
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3    Lavoie, J.N.4    Huot, J.5    Landry, J.6
  • 53
    • 0032143920 scopus 로고    scopus 로고
    • Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes
    • Clerk A, Michael A, Sugden PH: Stimulation of multiple mitogen-activated protein kinase sub-families by oxidative stress and phosphorylation of the small heat shock protein, HSP25/27, in neonatal ventricular myocytes. Biochem J 1998, 333 (Pt 3):581-589 (Pubitemid 28398524)
    • (1998) Biochemical Journal , vol.333 , Issue.3 , pp. 581-589
    • Clerk, A.1    Michael, A.2    Sugden, P.H.3
  • 54
    • 0036558366 scopus 로고    scopus 로고
    • Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins
    • DOI 10.1023/A:1015549725819
    • Gusev NB, Bogatcheva NV, Marston SB: Structure and properties of small heat shock proteins (sHsp) and their interaction with cytoskeleton proteins. Biochemistry (Mosc) 2002, 67:511-519 (Pubitemid 34719953)
    • (2002) Biochemistry (Moscow) , vol.67 , Issue.5 , pp. 511-519
    • Gusev, N.B.1    Bogatcheva, N.V.2    Marston, S.B.3
  • 55
    • 0031772351 scopus 로고    scopus 로고
    • In vivo evaluation of hsp27 as an inhibitor of actin polymerization: hsp27 limits actin stress fiber and focal adhesion formation after heat shock
    • Schneider GB, Hamano H, Cooper LF: In vivo evaluation of hsp27 as an inhibitor of actin polymerization: hsp27 limits actin stress fiber and focal adhesion formation after heat shock. J Cell Physiol 1998, 177:575-584
    • (1998) J Cell Physiol , vol.177 , pp. 575-584
    • Schneider, G.B.1    Hamano, H.2    Cooper, L.F.3
  • 56
    • 0028832107 scopus 로고
    • Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein HSP27
    • Huot J, Lambert H, Lavoie JN, Guimond A, Houle F, Landry J: Characterization of 45-kDa/54-kDa HSP27 kinase, a stress-sensitive kinase which may activate the phosphorylation-dependent protective function of mammalian 27-kDa heat-shock protein HSP27. Eur J Biochem 1995, 227:416-427
    • (1995) Eur J Biochem , vol.227 , pp. 416-427
    • Huot, J.1    Lambert, H.2    Lavoie, J.N.3    Guimond, A.4    Houle, F.5    Landry, J.6
  • 57
    • 0344791691 scopus 로고    scopus 로고
    • Basal linear deposit and large drusen are specific for early age-related maculopathy
    • Curcio CA, Millican CL: Basal linear deposit and large drusen are specific for early age-related maculopathy. Arch Ophthalmol 1999, 117:329-339
    • (1999) Arch Ophthalmol , vol.117 , pp. 329-339
    • Curcio, C.A.1    Millican, C.L.2
  • 58
    • 0028988138 scopus 로고
    • SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1
    • Cuenda A, Rouse J, Doza YN, Meier R, Cohen P, Gallagher TF, Young PR, Lee JC: SB 203580 is a specific inhibitor of a MAP kinase homologue which is stimulated by cellular stresses and interleukin-1. FEBS Lett 1995, 364:229-233
    • (1995) FEBS Lett , vol.364 , pp. 229-233
    • Cuenda, A.1    Rouse, J.2    Doza, Y.N.3    Meier, R.4    Cohen, P.5    Gallagher, T.F.6    Young, P.R.7    Lee, J.C.8
  • 60
    • 2542433090 scopus 로고    scopus 로고
    • Protein phosphatase 2A-mediated cross-talk between p38 MAPK and ERK in apoptosis of cardiac myocytes
    • DOI 10.1152/ajpheart.01050.2003
    • Liu Q, Hofmann PA: Protein phosphatase 2A-mediated cross-talk between p38 MAPK and ERK in apoptosis of cardiac myocytes. Am J Physiol Heart Circ Physiol 2004, 286:H2204-H2212 (Pubitemid 38685234)
    • (2004) American Journal of Physiology - Heart and Circulatory Physiology , vol.286 , Issue.6
    • Liu, Q.1    Hofmann, P.A.2
  • 61
    • 0000714961 scopus 로고    scopus 로고
    • Regulation of protein kinase cascades by protein phosphatase 2A
    • DOI 10.1016/S0968-0004(99)01375-4, PII S0968000499013754
    • Millward TA, Zolnierowicz S, Hemmings BA: Regulation of protein kinase cascades by protein phosphatase 2A. Trends Biochem Sci 1999, 24:186-191 (Pubitemid 29348452)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.5 , pp. 186-191
    • Millward, T.A.1    Zolnierowicz, S.2    Hemmings, B.A.3
  • 62
    • 0035105516 scopus 로고    scopus 로고
    • P38 mitogen-activated protein kinase-dependent activation of protein phosphatases 1 and 2A inhibits MEK1 and MEK2 activity and collagenase 1 (MMP-1) gene expression
    • DOI 10.1128/MCB.21.7.2373-2383.2001
    • Westermarck J, Li SP, Kallunki T, Han J, Kahari VM: p38 mitogen-activated protein kinase-dependent activation of protein phosphatases 1 and 2A inhibits MEK1 and MEK2 activity and collagenase 1 (MMP-1) gene expression. Mol Cell Biol 2001, 21:2373-2383 (Pubitemid 32222090)
    • (2001) Molecular and Cellular Biology , vol.21 , Issue.7 , pp. 2373-2383
    • Westermarck, J.1    Li, S.-P.2    Kallunki, T.3    Han, J.4    Kahari, V.-M.5
  • 63
    • 0035831516 scopus 로고    scopus 로고
    • Stress-induced Inhibition of ERK1 and ERK2 by Direct Interaction with p38 MAP Kinase
    • DOI 10.1074/jbc.C000917200
    • Zhang H, Shi X, Hampong M, Blanis L, Pelech S: Stress-induced inhibition of ERK1 and ERK2 by direct interaction with p38 MAP kinase. J Biol Chem 2001, 276:6905-6908 (Pubitemid 37391982)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.10 , pp. 6905-6908
    • Zhang, H.1    Shi, X.2    Hampong, M.3    Blanis, L.4    Pelech, S.5
  • 65
    • 0033538498 scopus 로고    scopus 로고
    • MAPK cascade
    • Singh RP, Dhawan P, Golden C, Kapoor GS, Mehta KD: One-way cross-talk between p38(MAPK) and p42/44(MAPK). Inhibition of p38(MAPK) induces low density lipoprotein receptor expression through activation of the p42/44(MAPK) cascade. J Biol Chem 1999, 274:19593-19600 (Pubitemid 129519400)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.28 , pp. 19593-19600
    • Singh, R.P.1    Dhawan, P.2    Golden, C.3    Kapoor, G.S.4    Mehta, K.D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.