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Volumn 69, Issue 5, 2006, Pages 806-814

Glucose and diabetes: Effects on podocyte and glomerular p38MAPK, heat shock protein 25, and actin cytoskeleton

Author keywords

Actin; Cytoskeleton; Diabetic nephropathy; Heat shock protein 25; p38 mitogen activated protein kinase; Podocyte

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; 4 ETHYL 2 (4 METHOXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; F ACTIN; G ACTIN; GLUCOSE; HEAT SHOCK PROTEIN 25; MITOGEN ACTIVATED PROTEIN KINASE P38; MITOGEN ACTIVATED PROTEIN KINASE P38 INHIBITOR; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

EID: 33644533898     PISSN: 00852538     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.ki.5000033     Document Type: Article
Times cited : (47)

References (52)
  • 1
    • 0142124436 scopus 로고    scopus 로고
    • Glycoxidation: The menace of diabetes and aging
    • Vlassara H, Palace MR. Glycoxidation: the menace of diabetes and aging. Mt Sinai J Med 2003; 70: 232-241.
    • (2003) Mt Sinai J Med , vol.70 , pp. 232-241
    • Vlassara, H.1    Palace, M.R.2
  • 2
    • 0031453830 scopus 로고    scopus 로고
    • Immunohistochemical colocalization of glycoxidation products and lipid peroxidation products in diabetic renal glomerular lesions. Implication for glycoxidative stress in the pathogenesis of diabetic nephropathy
    • Horie K, Miyata T, Maeda K et al. Immunohistochemical colocalization of glycoxidation products and lipid peroxidation products in diabetic renal glomerular lesions. Implication for glycoxidative stress in the pathogenesis of diabetic nephropathy. J Clin Invest 1997; 100: 2995-3004.
    • (1997) J Clin Invest , vol.100 , pp. 2995-3004
    • Horie, K.1    Miyata, T.2    Maeda, K.3
  • 3
    • 0036145348 scopus 로고    scopus 로고
    • Oxidative stress and nitric oxide synthase in rat diabetic nephropathy: Effects of ACEI and ARB
    • Onozato ML, Tojo A, Goto A et al. Oxidative stress and nitric oxide synthase in rat diabetic nephropathy: effects of ACEI and ARB. Kidney Int 2002; 61: 186-194.
    • (2002) Kidney Int , vol.61 , pp. 186-194
    • Onozato, M.L.1    Tojo, A.2    Goto, A.3
  • 4
    • 4344609666 scopus 로고    scopus 로고
    • High expression of PKC-MAPK pathway mRNAs correlates with glomerular lesions in human diabetic nephropathy
    • Toyoda M, Suzuki D, Honma M et al. High expression of PKC-MAPK pathway mRNAs correlates with glomerular lesions in human diabetic nephropathy. Kidney Int 2004; 66: 1107-1114.
    • (2004) Kidney Int , vol.66 , pp. 1107-1114
    • Toyoda, M.1    Suzuki, D.2    Honma, M.3
  • 5
    • 0030760729 scopus 로고    scopus 로고
    • Characterization of protein kinase C beta isoform activation on the gene expression of transforming growth factor-beta, extracellular matrix components, and prostanoids in the glomeruli of diabetic rats
    • Koya D, Jirousek MR, Lin YW et al. Characterization of protein kinase C beta isoform activation on the gene expression of transforming growth factor-beta, extracellular matrix components, and prostanoids in the glomeruli of diabetic rats. J Clin Invest 1997; 100: 115-126.
    • (1997) J Clin Invest , vol.100 , pp. 115-126
    • Koya, D.1    Jirousek, M.R.2    Lin, Y.W.3
  • 6
    • 0033930127 scopus 로고    scopus 로고
    • Small heat shock protein alteration provides a mechanism to reduce mesangial cell contractility in diabetes and oxidative stress
    • Dunlop ME, Muggli EE. Small heat shock protein alteration provides a mechanism to reduce mesangial cell contractility in diabetes and oxidative stress. Kidney Int 2000; 57: 464-475.
    • (2000) Kidney Int , vol.57 , pp. 464-475
    • Dunlop, M.E.1    Muggli, E.E.2
  • 7
    • 0042867408 scopus 로고    scopus 로고
    • Reactive oxygen species-regulated signaling pathways in diabetic nephropathy
    • Lee HB, Yu MR, Yang Y et al. Reactive oxygen species-regulated signaling pathways in diabetic nephropathy. J Am Soc Nephrol 2003; 4: S241-S245.
    • (2003) J Am Soc Nephrol , vol.4
    • Lee, H.B.1    Yu, M.R.2    Yang, Y.3
  • 8
    • 0035071318 scopus 로고    scopus 로고
    • 12-Lipoxygenase is increased in glucose-stimulated mesangial cells and in experimental diabetic nephropathy
    • Kang S-W, Adler SG, Nast CC et al. 12-lipoxygenase is increased in glucose-stimulated mesangial cells and in experimental diabetic nephropathy. Kidney Int 2001; 59: 1354-1362.
    • (2001) Kidney Int , vol.59 , pp. 1354-1362
    • Kang, S.-W.1    Adler, S.G.2    Nast, C.C.3
  • 9
    • 0034924523 scopus 로고    scopus 로고
    • Glomerular p38 mitogen-activated protein kinase (MAPK) and MAPK kinase 3/6 mRNA expression and activity are increased in early diabetic nephropathy
    • Kang S-W, Adler SG, LaPage J, Natarajan R. Glomerular p38 mitogen-activated protein kinase (MAPK) and MAPK kinase 3/6 mRNA expression and activity are increased in early diabetic nephropathy. Kidney Int 2001; 60: 543-552.
    • (2001) Kidney Int , vol.60 , pp. 543-552
    • Kang, S.-W.1    Adler, S.G.2    LaPage, J.3    Natarajan, R.4
  • 10
    • 0344667756 scopus 로고    scopus 로고
    • Role of 12-lipoxygenase in the stimulation of p38 mitogen-activated protein kinase and collagen alpha 5(IV) in experimental diabetic nephropathy and in glucose-stimulated podocytes
    • Kang S-W, Natarajan R, Shahed A et al. Role of 12-lipoxygenase in the stimulation of p38 mitogen-activated protein kinase and collagen alpha 5(IV) in experimental diabetic nephropathy and in glucose-stimulated podocytes. J Am Soc Nephrol 2003; 14: 3178-3187.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 3178-3187
    • Kang, S.-W.1    Natarajan, R.2    Shahed, A.3
  • 11
    • 0036974791 scopus 로고    scopus 로고
    • The relationship between glucose control and the development and progression of diabetic nephropathy
    • Phillips CA, Molitch ME. The relationship between glucose control and the development and progression of diabetic nephropathy. Curr Diab Rep 2002; 2: 523-529.
    • (2002) Curr Diab Rep , vol.2 , pp. 523-529
    • Phillips, C.A.1    Molitch, M.E.2
  • 12
    • 0024205254 scopus 로고
    • Role of advanced glycosylation products in complications of diabetes
    • Cerami A, Vlassara H, Brownlee M. Role of advanced glycosylation products in complications of diabetes. Diabetes Care 1988; 11: S73-S79.
    • (1988) Diabetes Care , vol.11
    • Cerami, A.1    Vlassara, H.2    Brownlee, M.3
  • 13
    • 0037339778 scopus 로고    scopus 로고
    • The response of antioxidant genes to hyperglycemia is abnormal in patients with type 1 diabetes and diabetic nephropathy
    • Hodgkinson AD, Bartlett T, Oates PJ et al. The response of antioxidant genes to hyperglycemia is abnormal in patients with type 1 diabetes and diabetic nephropathy. Diabetes 2003; 52: 846-851.
    • (2003) Diabetes , vol.52 , pp. 846-851
    • Hodgkinson, A.D.1    Bartlett, T.2    Oates, P.J.3
  • 14
    • 0033651497 scopus 로고    scopus 로고
    • Defective intracellular antioxidant enzyme production in type 1 diabetic patients with nephropathy
    • Ceriello A, Morocutti A, Mercuri F et al. Defective intracellular antioxidant enzyme production in type 1 diabetic patients with nephropathy. Diabetes 2000; 49: 2170-2177.
    • (2000) Diabetes , vol.49 , pp. 2170-2177
    • Ceriello, A.1    Morocutti, A.2    Mercuri, F.3
  • 15
    • 0032750960 scopus 로고    scopus 로고
    • Effects of taurine and vitamin e on microalbuminuria, plasma metalloproteinase-9, and serum type IV collagen concentrations in patients with diabetic nephropathy
    • Nakamura T, Ushiyama C, Suzuki S et al. Effects of taurine and vitamin E on microalbuminuria, plasma metalloproteinase-9, and serum type IV collagen concentrations in patients with diabetic nephropathy. Nephron 1999; 83: 361-362.
    • (1999) Nephron , vol.83 , pp. 361-362
    • Nakamura, T.1    Ushiyama, C.2    Suzuki, S.3
  • 16
    • 0038512591 scopus 로고    scopus 로고
    • Podocyte differentiation and hereditary proteinuria/nephrotic syndromes
    • Gubler MC. Podocyte differentiation and hereditary proteinuria/nephrotic syndromes. J Am Soc Nephrol 2003; 14: S22-S26.
    • (2003) J Am Soc Nephrol , vol.14
    • Gubler, M.C.1
  • 17
    • 0035134740 scopus 로고    scopus 로고
    • Regulation of glomerular basement membrane collagen expression by LMX1B contributes to renal disease in nail patella syndrome
    • Morello R, Zhou G, Dreyer SD et al. Regulation of glomerular basement membrane collagen expression by LMX1B contributes to renal disease in nail patella syndrome. Nat Genet 2001; 27: 205-208.
    • (2001) Nat Genet , vol.27 , pp. 205-208
    • Morello, R.1    Zhou, G.2    Dreyer, S.D.3
  • 18
    • 2342557359 scopus 로고    scopus 로고
    • Role of heat shock protein 27 in cytoskeletal remodeling of the airway smooth muscle cell
    • An SS, Fabry B, Mellema M et al. Role of heat shock protein 27 in cytoskeletal remodeling of the airway smooth muscle cell. J Appl Physiol 2004; 96: 1701-1713.
    • (2004) J Appl Physiol , vol.96 , pp. 1701-1713
    • An, S.S.1    Fabry, B.2    Mellema, M.3
  • 19
    • 0032508660 scopus 로고    scopus 로고
    • A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini
    • Schafer C, Ross SE, Bragado MJ et al. A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini. J Biol Chem 1998; 273(37): 24173-24180.
    • (1998) J Biol Chem , vol.273 , Issue.37 , pp. 24173-24180
    • Schafer, C.1    Ross, S.E.2    Bragado, M.J.3
  • 20
    • 0035831438 scopus 로고    scopus 로고
    • Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: Phosphorylation-induced actin polymerization caused by HSP27 mutants
    • Butt E, Immler D, Meyer HE et al. Heat shock protein 27 is a substrate of cGMP-dependent protein kinase in intact human platelets: phosphorylation- induced actin polymerization caused by HSP27 mutants. J Biol Chem 2001; 276: 7108-7113.
    • (2001) J Biol Chem , vol.276 , pp. 7108-7113
    • Butt, E.1    Immler, D.2    Meyer, H.E.3
  • 21
    • 0029994019 scopus 로고    scopus 로고
    • Altered expression of glomerular heat shock protein 27 in experimental nephrotic syndrome
    • Smoyer WE, Gupta A, Mundel P et al. Altered expression of glomerular heat shock protein 27 in experimental nephrotic syndrome. J Clin Invest 1996; 97: 2697-2704.
    • (1996) J Clin Invest , vol.97 , pp. 2697-2704
    • Smoyer, W.E.1    Gupta, A.2    Mundel, P.3
  • 22
    • 0036183944 scopus 로고    scopus 로고
    • HSP27 regulates podocyte cytoskeletal changes in an in vitro model of podocyte process retraction
    • Smoyer WE, Ransom RF. HSP27 regulates podocyte cytoskeletal changes in an in vitro model of podocyte process retraction. FASEB J 2002; 16: 315-326.
    • (2002) FASEB J , vol.16 , pp. 315-326
    • Smoyer, W.E.1    Ransom, R.F.2
  • 23
    • 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 et al. Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci 1997; 110(Part 3): 357-368.
    • (1997) J Cell Sci , vol.110 , Issue.3 PART , pp. 357-368
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3
  • 24
    • 0032583203 scopus 로고    scopus 로고
    • SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis
    • Huot J, Houle F, Rouseeau S et al. SAPK2/p38-dependent F-actin reorganization regulates early membrane blebbing during stress-induced apoptosis. J Cell Biol 1998; 143: 1361-1373.
    • (1998) J Cell Biol , vol.143 , pp. 1361-1373
    • Huot, J.1    Houle, F.2    Rouseeau, S.3
  • 25
    • 0032508660 scopus 로고    scopus 로고
    • A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini
    • Schafer C, Ross SE, Bragago MJ et al. A role for the p38 mitogen-activated protein kinase/Hsp 27 pathway in cholecystokinin-induced changes in the actin cytoskeleton in rat pancreatic acini. J Biol Chem 1998; 273: 24173-24180.
    • (1998) J Biol Chem , vol.273 , pp. 24173-24180
    • Schafer, C.1    Ross, S.E.2    Bragago, M.J.3
  • 26
    • 0032858218 scopus 로고    scopus 로고
    • HSP27 in signal transduction and association with contractile proteins in smooth muscle cells
    • Bitayo Al, Sladick J, Tuteja S et al. HSP27 in signal transduction and association with contractile proteins in smooth muscle cells. Am J Physiol 1999; 277(2 Part 1): G445-G454.
    • (1999) Am J Physiol , vol.277 , Issue.2 PART 1
    • Bitayo, Al.1    Sladick, J.2    Tuteja, S.3
  • 27
    • 0033840150 scopus 로고    scopus 로고
    • Molecular chaperones in the kidney: Distribution, putative roles, and regulation
    • Beck FX, Neuhofer W, Muller E. Molecular chaperones in the kidney: distribution, putative roles, and regulation. Am J Physiol Renal Physiol 2000; 279: F203-F215.
    • (2000) Am J Physiol Renal Physiol , vol.279
    • Beck, F.X.1    Neuhofer, W.2    Muller, E.3
  • 28
    • 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 et al. Phosphorylation and supramolecular organization of murine small heat shock protein HSP25 abolish its actin polymerization-inhibiting activity. J Biol Chem 1994; 269: 20780-20784.
    • (1994) J Biol Chem , vol.269 , pp. 20780-20784
    • Benndorf, R.1    Hayess, K.2    Ryazantsev, S.3
  • 29
    • 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 et al. Regulation of actin filament dynamics by p38 map kinase-mediated phosphorylation of heat shock protein 27. J Cell Sci 1997; 110(Part 3): 357-368.
    • (1997) J Cell Sci , vol.110 , Issue.3 PART , pp. 357-368
    • Guay, J.1    Lambert, H.2    Gingras-Breton, G.3
  • 30
    • 0031057892 scopus 로고    scopus 로고
    • Oxidative stress-induced actin reorganization mediated by the p38 mitogen-activated 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 kinase/heat shock protein 27 pathway in vascular endothelial cells. Circ Res 1997; 80: 383-392.
    • (1997) Circ Res , vol.80 , pp. 383-392
    • Huot, J.1    Houle, F.2    Marceau, F.3    Landry, J.4
  • 31
    • 0027417852 scopus 로고
    • Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization
    • Lavoie JN, Gingras-Breton G, Tanguay RM, Landry J. Induction of Chinese hamster HSP27 gene expression in mouse cells confers resistance to heat shock. HSP27 stabilization of the microfilament organization. J Biol Chem 1993; 268: 3420-3429.
    • (1993) J Biol Chem , vol.268 , pp. 3420-3429
    • Lavoie, J.N.1    Gingras-Breton, G.2    Tanguay, R.M.3    Landry, J.4
  • 32
    • 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 et al. 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.
    • (1995) Mol Cell Biol , vol.15 , pp. 505-516
    • Lavoie, J.N.1    Lambert, H.2    Hickey, E.3
  • 33
    • 0030868571 scopus 로고    scopus 로고
    • Basolateral membrane-associated 27-kDa heat shock protein and microfilament polymerization
    • Piotrowicz RS, Levin EG. Basolateral membrane-associated 27-kDa heat shock protein and microfilament polymerization. J Biol Chem 1997; 272: 25920-25927.
    • (1997) J Biol Chem , vol.272 , pp. 25920-25927
    • Piotrowicz, R.S.1    Levin, E.G.2
  • 34
    • 0035724962 scopus 로고    scopus 로고
    • Human keratinocytes respond to osmotic stress by p38 Map kinase regulated induction of HSP70 and HSP27
    • Garmyn M, Mammone T, Pupe A et al. Human keratinocytes respond to osmotic stress by p38 Map kinase regulated induction of HSP70 and HSP27. J Invest Dermatol 2001; 117: 1290-1295.
    • (2001) J Invest Dermatol , vol.117 , pp. 1290-1295
    • Garmyn, M.1    Mammone, T.2    Pupe, A.3
  • 35
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of intermediates for reactivation
    • Ehrnsperger M, Graber S, Gaestel M, Buchner J. Binding of non-native protein to Hsp25 during heat shock creates a reservoir of intermediates for reactivation. EMBO J 1997; 16: 221-229.
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Graber, S.2    Gaestel, M.3    Buchner, J.4
  • 36
    • 0030446673 scopus 로고    scopus 로고
    • Focal cerebral ischaemia increases the levels of several classes of heat shock proteins and their corresponding mRNAs
    • Wagstaff MJ, Collaco-Moraes Y, Aspey BS et al. Focal cerebral ischaemia increases the levels of several classes of heat shock proteins and their corresponding mRNAs. Brain Res Mol Brain Res 1996; 42: 236-244.
    • (1996) Brain Res Mol Brain Res , vol.42 , pp. 236-244
    • Wagstaff, M.J.1    Collaco-Moraes, Y.2    Aspey, B.S.3
  • 37
    • 3342977158 scopus 로고    scopus 로고
    • 2-Methoxyestardiol and bortezomib/proteasome-inhibitor overcome dexamethasone-resistance in multiple myeloma cells by modulating heat shock protein-27
    • Chauhan D, Li G, Auclair D et al. 2-Methoxyestardiol and bortezomib/proteasome-inhibitor overcome dexamethasone-resistance in multiple myeloma cells by modulating heat shock protein-27. Apoptosis 2004; 9: 149-155.
    • (2004) Apoptosis , vol.9 , pp. 149-155
    • Chauhan, D.1    Li, G.2    Auclair, D.3
  • 38
    • 1842734252 scopus 로고    scopus 로고
    • Involvement of stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK) in prostaglandin F2alpha-induced heat shock protein 27 in osteoblasts
    • Tokuda H, Niwa M, Ishisaki A et al. Involvement of stress-activated protein kinase (SAPK)/c-Jun N-terminal kinase (JNK) in prostaglandin F2alpha-induced heat shock protein 27 in osteoblasts. Prostagland Leukotr Essent Fatty Acids 2004; 70: 441-447.
    • (2004) Prostagland Leukotr Essent Fatty Acids , vol.70 , pp. 441-447
    • Tokuda, H.1    Niwa, M.2    Ishisaki, A.3
  • 39
    • 1242269235 scopus 로고    scopus 로고
    • Heat shock protein 70 or heat shock protein 27 overexpressed in human endothelial cells during posthypoxic reoxygenation can protect from delayed apoptosis
    • Kabakov AE, Budagova KR, Bryantsev AL, Latchman DS. Heat shock protein 70 or heat shock protein 27 overexpressed in human endothelial cells during posthypoxic reoxygenation can protect from delayed apoptosis. Cell Stress Chaperones 2003; 8: 335-347.
    • (2003) Cell Stress Chaperones , vol.8 , pp. 335-347
    • Kabakov, A.E.1    Budagova, K.R.2    Bryantsev, A.L.3    Latchman, D.S.4
  • 40
    • 0141953996 scopus 로고    scopus 로고
    • Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin
    • Keezer SM, Ivie SE, Krutzsch HC et al. Angiogenesis inhibitors target the endothelial cell cytoskeleton through altered regulation of heat shock protein 27 and cofilin. Cancer Res 2003; 63: 6405-6412.
    • (2003) Cancer Res , vol.63 , pp. 6405-6412
    • Keezer, S.M.1    Ivie, S.E.2    Krutzsch, H.C.3
  • 41
    • 0035070417 scopus 로고    scopus 로고
    • A Jurkat T cell variant resistant to death receptor-induced apoptosis. Correlation with heat shock protein (Hsp) 27 and 70 levels
    • Ricci JE, Maulon L, Battaglione-Hofman V et al. A Jurkat T cell variant resistant to death receptor-induced apoptosis. Correlation with heat shock protein (Hsp) 27 and 70 levels. Eur Cytokine Netw 2001; 12: 126-134.
    • (2001) Eur Cytokine Netw , vol.12 , pp. 126-134
    • Ricci, J.E.1    Maulon, L.2    Battaglione-Hofman, V.3
  • 42
    • 0039171658 scopus 로고    scopus 로고
    • Analysis of the role of Hsp25 phosphorylation reveals the importance of the oligomerization state of this small heat shock protein in its protective function against TNFalpha- and hydrogen peroxide-induced cell death
    • Preville X, Sschultz H, Knauf U et al. Analysis of the role of Hsp25 phosphorylation reveals the importance of the oligomerization state of this small heat shock protein in its protective function against TNFalpha- and hydrogen peroxide-induced cell death. J Cell Biochem 1998; 69: 436-452.
    • (1998) J Cell Biochem , vol.69 , pp. 436-452
    • Preville, X.1    Sschultz, H.2    Knauf, U.3
  • 43
    • 0007404243 scopus 로고    scopus 로고
    • Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells
    • Mehlen P, Hickey E, Weber LA, Arrigo AP. Large unphosphorylated aggregates as the active form of hsp27 which controls intracellular reactive oxygen species and glutathione levels and generates a protection against TNFalpha in NIH-3T3-ras cells. Biochem Biophys Res Commun 1997; 241: 187-192.
    • (1997) Biochem Biophys Res Commun , vol.241 , pp. 187-192
    • Mehlen, P.1    Hickey, E.2    Weber, L.A.3    Arrigo, A.P.4
  • 44
    • 2542451125 scopus 로고    scopus 로고
    • 2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27
    • 2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27. J Biol Chem 2004; 279: 23463-23471.
    • (2004) J Biol Chem , vol.279 , pp. 23463-23471
    • Theriault, J.R.1    Lambert, H.2    Chavez-Zobel, A.T.3
  • 45
    • 0032617026 scopus 로고    scopus 로고
    • Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27)
    • Landry J, Huot J. Regulation of actin dynamics by stress-activated protein kinase 2 (SAPK2)-dependent phosphorylation of heat-shock protein of 27 kDa (Hsp27). Biochem Soc Symp 1999; 64: 79-89.
    • (1999) Biochem Soc Symp , vol.64 , pp. 79-89
    • Landry, J.1    Huot, J.2
  • 46
    • 0030069517 scopus 로고    scopus 로고
    • HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress
    • Huot J, Houle F, Spitz DR, Landry J. HSP27 phosphorylation-mediated resistance against actin fragmentation and cell death induced by oxidative stress. Cancer Res 1996; 56: 273-279.
    • (1996) Cancer Res , vol.56 , pp. 273-279
    • Huot, J.1    Houle, F.2    Spitz, D.R.3    Landry, J.4
  • 47
    • 0033516660 scopus 로고    scopus 로고
    • Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation
    • Rogalla T, Ehrnsperger M, Preville X et al. Regulation of Hsp27 oligomerization, chaperone function, and protective activity against oxidative stress/tumor necrosis factor alpha by phosphorylation. J Biol Chem 1999; 274: 18947-18956.
    • (1999) J Biol Chem , vol.274 , pp. 18947-18956
    • Rogalla, T.1    Ehrnsperger, M.2    Preville, X.3
  • 48
    • 16644365383 scopus 로고    scopus 로고
    • Podocytes are firmly attached to glomerular basement membrane in kidneys with heavy proteinuria
    • Lahdenkari A-T, Lounatmaa K, Patrakka J et al. Podocytes are firmly attached to glomerular basement membrane in kidneys with heavy proteinuria. J Am Soc Nephrol 2004; 15: 2611-2618.
    • (2004) J Am Soc Nephrol , vol.15 , pp. 2611-2618
    • Lahdenkari, A.-T.1    Lounatmaa, K.2    Patrakka, J.3
  • 49
    • 0031563832 scopus 로고    scopus 로고
    • Rearrangements of the cytoskeleton and cell contacts induce process formation during differentiation of conditionally immortalized mouse podocyte cell lines
    • Mundel P, Reiser J, Zuniga MB et al. Rearrangements of the cytoskeleton and cell contacts induce process formation during differentiation of conditionally immortalized mouse podocyte cell lines. Exp Cell Res 1997; 236: 248-258.
    • (1997) Exp Cell Res , vol.236 , pp. 248-258
    • Mundel, P.1    Reiser, J.2    Zuniga, M.B.3
  • 50
    • 0018038933 scopus 로고
    • Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I
    • Blikstad I, Markey F, Carlsson L et al. Selective assay of monomeric and filamentous actin in cell extracts, using inhibition of deoxyribonuclease I. Cell 1978; 15: 935-943.
    • (1978) Cell , vol.15 , pp. 935-943
    • Blikstad, I.1    Markey, F.2    Carlsson, L.3
  • 51
    • 0029669928 scopus 로고    scopus 로고
    • +/Pi co-transport alters rapidly cytoskeletal protein polymerization dynamics in opossum kidney cells
    • +/Pi co-transport alters rapidly cytoskeletal protein polymerization dynamics in opossum kidney cells. Biochem J 1996; 315(Part 1): 241-247.
    • (1996) Biochem J , vol.315 , Issue.1 PART , pp. 241-247
    • Papakonstanti, E.A.1    Emmanouel, D.S.2    Gravanis, A.3    Stournaras, C.4
  • 52
    • 0034945789 scopus 로고    scopus 로고
    • Podocyte foot process broadening in experimental diabetic nephropathy: Amelioration with renin-angiotensin blockade
    • Mifsud SA, Allen TJ, Bertram JF et al. Podocyte foot process broadening in experimental diabetic nephropathy: amelioration with renin-angiotensin blockade. Diabetologia 2001; 44: 878-882.
    • (2001) Diabetologia , vol.44 , pp. 878-882
    • Mifsud, S.A.1    Allen, T.J.2    Bertram, J.F.3


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