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Volumn 51, Issue 9, 2011, Pages 1727-1735

Proteasome alterations during adipose differentiation and aging: Links to impaired adipocyte differentiation and development of oxidative stress

Author keywords

Adipocyte; Aging; Free radicals; Insulin resistance; Obesity; Pathology; Proteolysis; Ubiquitin

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; UBIQUITIN;

EID: 80053578494     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2011.08.001     Document Type: Article
Times cited : (30)

References (58)
  • 1
    • 0033643742 scopus 로고    scopus 로고
    • The ubiquitin-mediated proteolytic pathway: Mode of action and clinical implications
    • DOI 10.1002/(SICI)1097-4644(2000)77: 34+<40::AID-JCB9>3.0.CO;2-6
    • A. Ciechanover, A. Orian, and A.L. Schwartz The ubiquitin-mediated proteolytic pathway: mode of action and clinical implications J. Cell. Biochem. Suppl. 34 2000 40 51 (Pubitemid 30176732)
    • (2000) Journal of Cellular Biochemistry , vol.77 , Issue.SUPPL. 34 , pp. 40-51
    • Ciechanover, A.1    Orian, A.2    Schwartz, A.L.3
  • 2
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • DOI 10.1146/annurev.biochem.70.1.503
    • C.M. Pickart Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533 (Pubitemid 32663902)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 3
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • O. Coux, K. Tanaka, and A.L. Goldberg Structure and functions of the 20S and 26S proteasomes Annu. Rev. Biochem. 65 1996 801 847 (Pubitemid 26255262)
    • (1996) Annual Review of Biochemistry , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 4
    • 0029039632 scopus 로고
    • Studies on the activation by ATP of the 26 S proteasome complex from rat skeletal muscle
    • B. Dahlmann, L. Kuehn, and H. Reinauer Studies on the activation by ATP of the 26 S proteasome complex from rat skeletal muscle Biochem. J. 309 1995 195 202
    • (1995) Biochem. J. , vol.309 , pp. 195-202
    • Dahlmann, B.1    Kuehn, L.2    Reinauer, H.3
  • 5
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • DOI 10.1016/0968-0004(96)10012-8
    • W. Hilt, and D.H. Wolf Proteasomes: destruction as a programme Trends Biochem. Sci. 21 1996 96 102 (Pubitemid 26085981)
    • (1996) Trends in Biochemical Sciences , vol.21 , Issue.3 , pp. 96-102
    • Hilt, W.1    Wolf, D.H.2
  • 6
    • 0029984892 scopus 로고    scopus 로고
    • Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome
    • DOI 10.1074/jbc.271.26.15504
    • T. Grune, T. Reinheckel, and K.J. Davies Degradation of oxidized proteins in K562 human hematopoietic cells by proteasome J. Biol. Chem. 271 1996 15504 15509 (Pubitemid 26225322)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.26 , pp. 15504-15509
    • Grune, T.1    Reinheckel, T.2    Davies, K.J.A.3
  • 8
    • 0034087369 scopus 로고    scopus 로고
    • Decreased levels of proteasome activity and proteasome expression in aging spinal cord
    • DOI 10.1016/S0306-4522(00)00067-1, PII S0306452200000671
    • J.N. Keller, F.F. Huang, and W.R. Markesbery Decreased levels of proteasome activity and proteasome expression in aging spinal cord Neuroscience 98 2000 149 156 (Pubitemid 30349153)
    • (2000) Neuroscience , vol.98 , Issue.1 , pp. 149-156
    • Keller, J.N.1    Huang, F.F.2    Markesbery, W.R.3
  • 9
    • 9744222883 scopus 로고    scopus 로고
    • Protein quality control in Alzheimer's disease by the ubiquitin proteasome system
    • DOI 10.1016/j.pneurobio.2004.10.001, PII S0301008204001650
    • F.M. de Vrij, D.F. Fischer, F.W. van Leeuwen, and E.M. Hol Protein quality control in Alzheimer's disease by the ubiquitin proteasome system Prog. Neurobiol. 74 2004 249 270 (Pubitemid 39586719)
    • (2004) Progress in Neurobiology , vol.74 , Issue.5 , pp. 249-270
    • De Vrij, F.M.S.1    Fischer, D.F.2    Van Leeuwen, F.W.3    Hol, E.M.4
  • 10
    • 33751269641 scopus 로고    scopus 로고
    • The aggravating role of the ubiquitin-proteasome system in neurodegenerative disease
    • DOI 10.1042/BST0340743
    • C.C. Hung, E.J. Davison, P.A. Robinson, and H.C. Ardley The aggravating role of the ubiquitin-proteasome system in neurodegenerative disease Biochem. Soc. Trans. 34 2006 743 745 (Pubitemid 44796410)
    • (2006) Biochemical Society Transactions , vol.34 , Issue.5 , pp. 743-745
    • Hung, C.-C.1    Davison, E.J.2    Robinson, P.A.3    Ardley, H.C.4
  • 11
    • 33644639061 scopus 로고    scopus 로고
    • Proteasomal defense of oxidative protein modifications
    • DOI 10.1089/ars.2006.8.173
    • D. Poppek, and T. Grune Proteasomal defense of oxidative protein modifications Antioxid. Redox Signal. 8 2006 173 184 (Pubitemid 43324544)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.1-2 , pp. 173-184
    • Poppek, D.1    Grune, T.2
  • 12
    • 58149350129 scopus 로고    scopus 로고
    • The proteasome and its role in the degradation of oxidized proteins
    • T. Jung, and T. Grune The proteasome and its role in the degradation of oxidized proteins IUBMB Life 60 2008 743 752
    • (2008) IUBMB Life , vol.60 , pp. 743-752
    • Jung, T.1    Grune, T.2
  • 13
    • 0037414834 scopus 로고    scopus 로고
    • Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome
    • DOI 10.1074/jbc.M206279200
    • R. Shringarpure, T. Grune, J. Mehlhase, and K.J. Davies Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome J. Biol. Chem. 278 2003 311 318 (Pubitemid 36043578)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.1 , pp. 311-318
    • Shringarpure, R.1    Grune, T.2    Mehlhase, J.3    Davies, K.J.A.4
  • 14
    • 64949099855 scopus 로고    scopus 로고
    • Protein homeostasis and aging: Taking care of proteins from the cradle to the grave
    • R.I. Morimoto, and A.M. Cuervo Protein homeostasis and aging: taking care of proteins from the cradle to the grave J. Gerontol. A Biol. Sci. Med. Sci. 64 2009 167 170
    • (2009) J. Gerontol. A Biol. Sci. Med. Sci. , vol.64 , pp. 167-170
    • Morimoto, R.I.1    Cuervo, A.M.2
  • 16
    • 79251498807 scopus 로고    scopus 로고
    • Protein homeostasis and aging: The importance of exquisite quality control
    • H. Koga, S. Kaushik, and A.M. Cuervo Protein homeostasis and aging: the importance of exquisite quality control Ageing Res. Rev. 10 2011 205 215
    • (2011) Ageing Res. Rev. , vol.10 , pp. 205-215
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 18
    • 33745977756 scopus 로고    scopus 로고
    • Proteasome inhibition induces reversible impairments in protein synthesis
    • DOI 10.1096/fj.05-5495com
    • Q. Ding, E. Dimayuga, W.R. Markesbery, and J.N. Keller Proteasome inhibition induces reversible impairments in protein synthesis FASEB J. 20 2006 1055 1063 (Pubitemid 44943901)
    • (2006) FASEB Journal , vol.20 , Issue.8 , pp. 1055-1063
    • Ding, Q.1    Dimayuga, E.2    Markesbery, W.R.3    Keller, J.N.4
  • 19
    • 0033972037 scopus 로고    scopus 로고
    • Possible involvement of proteasome inhibition in aging: Implications for oxidative stress
    • DOI 10.1016/S0047-6374(99)00101-3, PII S0047637499001013
    • J.N. Keller, K.B. Hanni, and W.R. Markesbery Possible involvement of proteasome inhibition in aging: implications for oxidative stress Mech. Ageing Dev. 113 2000 61 70 (Pubitemid 30050671)
    • (2000) Mechanisms of Ageing and Development , vol.113 , Issue.1 , pp. 61-70
    • Keller, J.N.1    Hanni, K.B.2    Markesbery, W.R.3
  • 22
    • 33745675537 scopus 로고    scopus 로고
    • Ubiquitin-proteasome pathway function is required for lens cell proliferation and differentiation
    • DOI 10.1167/iovs.05-0261
    • W. Guo, F. Shang, Q. Liu, L. Urim, M. Zhang, and A. Taylor Ubiquitin-proteasome pathway function is required for lens cell proliferation and differentiation Investig. Ophthalmol. Vis. Sci. 47 2006 2569 2575 (Pubitemid 351639843)
    • (2006) Investigative Ophthalmology and Visual Science , vol.47 , Issue.6 , pp. 2569-2575
    • Guo, W.1    Shang, F.2    Liu, Q.3    Urim, L.4    Zhang, M.5    Taylor, A.6
  • 23
    • 0029186274 scopus 로고
    • Roles of proteasomes in cell growth
    • A. Ichihara, and K. Tanaka Roles of proteasomes in cell growth Mol. Biol. Rep. 21 1995 49 52
    • (1995) Mol. Biol. Rep. , vol.21 , pp. 49-52
    • Ichihara, A.1    Tanaka, K.2
  • 24
    • 85078372110 scopus 로고    scopus 로고
    • Roles of the ubiquitin-proteosome system in neurogenesis
    • T.C. Tuoc, and A. Stoykova Roles of the ubiquitin-proteosome system in neurogenesis Cell Cycle 15 2010 3174 3180
    • (2010) Cell Cycle , vol.15 , pp. 3174-3180
    • Tuoc, T.C.1    Stoykova, A.2
  • 25
    • 69049093712 scopus 로고    scopus 로고
    • Age-related changes in total and regional fat distribution
    • J.L. Kuk, T.J. Saunders, L.E. Davidson, and R. Ross Age-related changes in total and regional fat distribution Ageing Res. Rev. 8 2009 339 348
    • (2009) Ageing Res. Rev. , vol.8 , pp. 339-348
    • Kuk, J.L.1    Saunders, T.J.2    Davidson, L.E.3    Ross, R.4
  • 26
    • 18944365906 scopus 로고    scopus 로고
    • Association of age with muscle mass, fat mass and fat distribution in non-diabetic haemodialysis patients
    • DOI 10.1093/ndt/gfh643
    • S. Ohkawa, M. Odamaki, N. Ikegaya, I. Hibi, K. Miyaji, and H. Kumagai Association of age with muscle mass, fat mass and fat distribution in non-diabetic haemodialysis patients Nephrol. Dial. Transplant. 20 2005 945 951 (Pubitemid 40704031)
    • (2005) Nephrology Dialysis Transplantation , vol.20 , Issue.5 , pp. 945-951
    • Ohkawa, S.1    Odamaki, M.2    Ikegaya, N.3    Hibi, I.4    Miyaji, K.5    Kumagai, H.6
  • 27
    • 84925944353 scopus 로고    scopus 로고
    • Contribution of adipose tissue to health span and longevity
    • D.M. Huffman, and N. Barzilai Contribution of adipose tissue to health span and longevity Interdiscip. Top. Gerontol. 37 2010 1 19
    • (2010) Interdiscip. Top. Gerontol. , vol.37 , pp. 1-19
    • Huffman, D.M.1    Barzilai, N.2
  • 29
    • 34248550944 scopus 로고    scopus 로고
    • Aging in adipocytes: Potential impact of inherent, depot-specific mechanisms
    • DOI 10.1016/j.exger.2007.03.003, PII S053155650700054X
    • M.J. Cartwright, T. Tchkonia, and J.L. Kirkland Aging in adipocytes: potential impact of inherent, depot-specific mechanisms Exp. Gerontol. 42 2007 463 471 (Pubitemid 46756096)
    • (2007) Experimental Gerontology , vol.42 , Issue.6 , pp. 463-471
    • Cartwright, M.J.1    Tchkonia, T.2    Kirkland, J.L.3
  • 30
    • 23944523318 scopus 로고    scopus 로고
    • Relationship between body composition changes and changes in physical function and metabolic risk factors in aging
    • M.P. St-Onge Relationship between body composition changes and changes in physical function and metabolic risk factors in aging Curr. Opin. Clin. Nutr. Metab. Care 8 2005 523 528
    • (2005) Curr. Opin. Clin. Nutr. Metab. Care , vol.8 , pp. 523-528
    • St-Onge, M.P.1
  • 31
    • 70349188457 scopus 로고    scopus 로고
    • High efficiency lipid-based siRNA transfection of adipocytes in suspension
    • G. Kilroy, D.H. Burk, and Z.E. Floyd High efficiency lipid-based siRNA transfection of adipocytes in suspension PLoS One 11 2009 e6940
    • (2009) PLoS One , vol.11 , pp. 6940
    • Kilroy, G.1    Burk, D.H.2    Floyd, Z.E.3
  • 32
    • 0037040272 scopus 로고    scopus 로고
    • Interferon-γ-mediated activation and ubiquitin-proteasome-dependent degradation of PPARγ in adipocytes
    • DOI 10.1074/jbc.M108473200
    • Z.E. Floyd, and J.M. Stephens Interferon-gamma-mediated activation and ubiquitin-proteasome-dependent degradation of PPARgamma in adipocytes J. Biol. Chem. 277 2002 4062 4068 (Pubitemid 34968663)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.6 , pp. 4062-4068
    • Elizabeth Floyd, Z.1    Stephens, J.M.2
  • 33
    • 71849084532 scopus 로고    scopus 로고
    • Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver
    • K. Dasuri, L. Zhang, P. Ebenezer, Y. Liu, S.O. Fernandez-Kim, and J.N. Keller Aging and dietary restriction alter proteasome biogenesis and composition in the brain and liver Mech. Ageing Dev. 130 2009 777 783
    • (2009) Mech. Ageing Dev. , vol.130 , pp. 777-783
    • Dasuri, K.1    Zhang, L.2    Ebenezer, P.3    Liu, Y.4    Fernandez-Kim, S.O.5    Keller, J.N.6
  • 34
    • 46649083580 scopus 로고    scopus 로고
    • Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart
    • F. Li, L. Zhang, J. Craddock, A.J. Bruce-Keller, K. Dasuri, A. Nguyen, and J.N. Keller Aging and dietary restriction effects on ubiquitination, sumoylation, and the proteasome in the heart Mech. Ageing Dev. 129 2008 515 521
    • (2008) Mech. Ageing Dev. , vol.129 , pp. 515-521
    • Li, F.1    Zhang, L.2    Craddock, J.3    Bruce-Keller, A.J.4    Dasuri, K.5    Nguyen, A.6    Keller, J.N.7
  • 35
    • 36149000190 scopus 로고    scopus 로고
    • Effects of aging and dietary restriction on ubiquitination, sumoylation, and the proteasome in the spleen
    • DOI 10.1016/j.febslet.2007.10.054, PII S0014579307011222
    • L. Zhang, F. Li, E. Dimayuga, J. Craddock, and J.N. Keller Effects of aging and dietary restriction on ubiquitination, sumoylation, and the proteasome in the spleen FEBS Lett. 581 2007 5543 5547 (Pubitemid 350110436)
    • (2007) FEBS Letters , vol.581 , Issue.28 , pp. 5543-5547
    • Zhang, L.1    Li, F.2    Dimayuga, E.3    Craddock, J.4    Keller, J.N.5
  • 36
    • 3442898375 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway is a new partner for the control of insulin signaling
    • DOI 10.1097/00075197-200405000-00002
    • S. Rome, E. Meugnier, and H. Vidal The ubiquitin-proteasome pathway is a new partner for the control of insulin signaling Curr. Opin. Clin. Nutr. Metab. Care 7 2004 249 254 (Pubitemid 40340660)
    • (2004) Current Opinion in Clinical Nutrition and Metabolic Care , vol.7 , Issue.3 , pp. 249-254
    • Rome, S.1    Meugnier, E.2    Vidal, H.3
  • 37
    • 22744459667 scopus 로고    scopus 로고
    • Is insulin signaling molecules misguided in diabetes for ubiquitin-proteasome mediated degradation?
    • DOI 10.1007/s11010-005-1083-y
    • M. Balasubramanyam, R. Sampathkumar, and V. Mohan Is insulin signaling molecules misguided in diabetes for ubiquitin-proteasome mediated degradation? Mol. Cell. Biochem. 275 2005 117 125 (Pubitemid 41030987)
    • (2005) Molecular and Cellular Biochemistry , vol.275 , Issue.1-2 , pp. 117-125
    • Balasubramanyam, M.1    Sampathkumar, R.2    Mohan, V.3
  • 39
    • 34250011799 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases
    • J. Wang, and M.A. Maldonado The ubiquitin-proteasome system and its role in inflammatory and autoimmune diseases Cell. Mol. Immunol. 3 2006 255 261
    • (2006) Cell. Mol. Immunol. , vol.3 , pp. 255-261
    • Wang, J.1    Maldonado, M.A.2
  • 40
    • 0000085132 scopus 로고    scopus 로고
    • Insulin-induced insulin receptor substrate-1 degradation is mediated by the proteasome degradation pathway
    • DOI 10.2337/diabetes.48.7.1359
    • X.J. Sun, J.L. Goldberg, L.Y. Qiao, and J.J. Mitchell Insulin-induced insulin receptor substrate-1 degradation is mediated by the proteasome degradation pathway Diabetes 48 1999 1359 1364 (Pubitemid 29297296)
    • (1999) Diabetes , vol.48 , Issue.7 , pp. 1359-1364
    • Sun, X.J.1    Goldberg, J.L.2    Qiao, L.-Y.3    Mitchell, J.J.4
  • 41
    • 0036149984 scopus 로고    scopus 로고
    • Molecular mechanism of insulin-induced degradation of insulin receptor substrate 1
    • DOI 10.1128/MCB.22.4.1016-1026.2002
    • R. Zhande, J.J. Mitchell, J. Wu, and X.J. Sun Molecular mechanism of insulin-induced degradation of insulin receptor substrate 1 Mol. Cell. Biol. 22 2002 1016 1026 (Pubitemid 34094839)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.4 , pp. 1016-1026
    • Zhande, R.1    Mitchell, J.J.2    Wu, J.3    Sun, X.J.4
  • 42
    • 0033982719 scopus 로고    scopus 로고
    • Insulin-like growth factor I-induced degradation of insulin receptor substrate 1 is mediated by the 26S proteasome and blocked by phosphatidylinositol 3'-kinase inhibition
    • DOI 10.1128/MCB.20.5.1489-1496.2000
    • A.V. Lee, J.L. Gooch, S. Oesterreich, R.L. Guler, and D. Yee Insulin-like growth factor I-induced degradation of insulin receptor substrate 1 is mediated by the 26S proteasome and blocked by phosphatidylinositol 3′-kinase inhibition Mol. Cell. Biol. 20 2000 1489 1496 (Pubitemid 30100168)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.5 , pp. 1489-1496
    • Lee, A.V.1    Gooch, J.L.2    Oesterreich, S.3    Guler, R.L.4    Yee, D.5
  • 43
    • 0034463918 scopus 로고    scopus 로고
    • A rapamycin-sensitive pathway down-regulates insulin signaling via phosphorylation and proteasomal degradation of insulin receptor substrate-1
    • DOI 10.1210/me.14.6.783
    • T. Haruta, T. Uno, J. Kawahara, A. Takano, K. Egawa, P.M. Sharma, J.M. Olefsky, and M.A. Kobayashi Rapamycin-sensitive pathway down-regulates insulin signaling via phosphorylation and proteasomal degradation of insulin receptor substrate-1 Mol. Endocrinol. 14 2000 783 794 (Pubitemid 32260492)
    • (2000) Molecular Endocrinology , vol.14 , Issue.6 , pp. 783-794
    • Haruta, T.1    Uno, T.2    Kawahara, J.3    Takano, A.4    Egawa, K.5    Sharma, P.M.6    Olefsky, J.M.7    Kobayashi, M.8
  • 44
    • 67349249156 scopus 로고    scopus 로고
    • Proteasome subunits mRNA expressions correlate with male BMI: Implications for a role in obesity
    • K. Sakamoto, Y. Sato, T. Shinka, M. Sei, I. Nomura, M. Umeno, A.A. Ewis, and Y. Nakahori Proteasome subunits mRNA expressions correlate with male BMI: implications for a role in obesity Obesity 17 2009 1044 1049
    • (2009) Obesity , vol.17 , pp. 1044-1049
    • Sakamoto, K.1    Sato, Y.2    Shinka, T.3    Sei, M.4    Nomura, I.5    Umeno, M.6    Ewis, A.A.7    Nakahori, Y.8
  • 45
    • 77952096580 scopus 로고    scopus 로고
    • Proteasome activity correlates with male BMI and contributes to the differentiation of adipocyte in hADSC
    • K. Sakamoto, Y. Sato, M. Sei, A.A. Ewis, and Y. Nakahori Proteasome activity correlates with male BMI and contributes to the differentiation of adipocyte in hADSC Endocrine 37 2010 274 279
    • (2010) Endocrine , vol.37 , pp. 274-279
    • Sakamoto, K.1    Sato, Y.2    Sei, M.3    Ewis, A.A.4    Nakahori, Y.5
  • 46
    • 33845897434 scopus 로고    scopus 로고
    • Inhibition of human preadipocyte proteasomal activity by HIV protease inhibitors or specific inhibitor lactacystin leads to a defect in adipogenesis, which involves matrix metalloproteinase-9
    • DOI 10.1124/jpet.106.111849
    • S. De Barros, A. Zakaroff-Girard, M. Lafontan, J. Galitzky, and V. Bourlier Inhibition of human preadipocyte proteasomal activity by HIV protease inhibitors or specific inhibitor lactacystin leads to a defect in adipogenesis, which involves matrix metalloproteinase-9 J. Pharmacol. Exp. Ther. 320 2007 291 299 (Pubitemid 46025743)
    • (2007) Journal of Pharmacology and Experimental Therapeutics , vol.320 , Issue.1 , pp. 291-299
    • De Barros, S.1    Zakaroff-Girard, A.2    Lafontan, M.3    Galitzky, J.4    Bourlier, V.5
  • 49
    • 0031683542 scopus 로고    scopus 로고
    • Prolonged oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes
    • DOI 10.2337/diabetes.47.10.1562
    • A. Rudich, A. Tirosh, R. Potashnik, R. Hemi, H. Kanety, and N. Bashan Prolonged oxidative stress impairs insulin-induced GLUT4 translocation in 3T3-L1 adipocytes Diabetes 47 1998 1562 1569 (Pubitemid 28445343)
    • (1998) Diabetes , vol.47 , Issue.10 , pp. 1562-1569
    • Rudich, A.1    Tlrosh, A.2    Potashnik, R.3    Hemi, R.4    Kanety, H.5    Bashan, N.6
  • 50
    • 0033537830 scopus 로고    scopus 로고
    • Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes: A putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation
    • A. Tirosh, R. Potashnik, N. Bashan, and A. Rudich Oxidative stress disrupts insulin-induced cellular redistribution of insulin receptor substrate-1 and phosphatidylinositol 3-kinase in 3T3-L1 adipocytes: a putative cellular mechanism for impaired protein kinase B activation and GLUT4 translocation J. Biol. Chem. 274 1999 10595 10602
    • (1999) J. Biol. Chem. , vol.274 , pp. 10595-10602
    • Tirosh, A.1    Potashnik, R.2    Bashan, N.3    Rudich, A.4
  • 53
    • 0033774103 scopus 로고    scopus 로고
    • Oxidative stress-associated impairment of proteasome activity during ischemia-reperfusion injury
    • J.N. Keller, F.F. Huang, H. Zhu, J. Yu, Y.S. Ho, and T.S. Kindy Oxidative stress-associated impairment of proteasome activity during ischemia-reperfusion injury J. Cereb. Blood Flow Metab. 20 2000 1467 1473
    • (2000) J. Cereb. Blood Flow Metab. , vol.20 , pp. 1467-1473
    • Keller, J.N.1    Huang, F.F.2    Zhu, H.3    Yu, J.4    Ho, Y.S.5    Kindy, T.S.6
  • 54
    • 0030977793 scopus 로고    scopus 로고
    • Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein
    • DOI 10.1016/S0014-5793(97)00148-8, PII S0014579397001488
    • B. Friguet, and L.I. Szweda Inhibition of the multicatalytic proteinase (proteasome) by 4-hydroxy-2-nonenal cross-linked protein FEBS Lett. 405 1997 21 25 (Pubitemid 27130365)
    • (1997) FEBS Letters , vol.405 , Issue.1 , pp. 21-25
    • Friguet, B.1    Szweda, L.I.2
  • 55
    • 0033588087 scopus 로고    scopus 로고
    • 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress: Identification of proteasomes as target molecules
    • K. Okada, C. Wangpoengtrakul, T. Osawa, S. Toyokuni, K. Tanaka, and K. Uchida 4-Hydroxy-2-nonenal-mediated impairment of intracellular proteolysis during oxidative stress: identification of proteasomes as target molecules J. Biol. Chem. 274 1999 23787 23793
    • (1999) J. Biol. Chem. , vol.274 , pp. 23787-23793
    • Okada, K.1    Wangpoengtrakul, C.2    Osawa, T.3    Toyokuni, S.4    Tanaka, K.5    Uchida, K.6
  • 57
    • 79960042882 scopus 로고    scopus 로고
    • Selective vulnerability of neurons to acute toxicity after proteasome inhibitor treatment: Implications for oxidative stress and insolubility of newly synthesized proteins
    • K. Dasuri, P.J. Ebenezer, L. Zhang, S.O. Fernandez-Kim, R.M. Uranga, E. Gavilán, A. Di Blasio, and J.N. Keller Selective vulnerability of neurons to acute toxicity after proteasome inhibitor treatment: implications for oxidative stress and insolubility of newly synthesized proteins Free Radic. Biol. Med. 49 2010 1290 1297
    • (2010) Free Radic. Biol. Med. , vol.49 , pp. 1290-1297
    • Dasuri, K.1    Ebenezer, P.J.2    Zhang, L.3    Fernandez-Kim, S.O.4    Uranga, R.M.5    Gavilán, E.6    Di Blasio, A.7    Keller, J.N.8
  • 58
    • 7944226117 scopus 로고    scopus 로고
    • Inhibition of proteasome activity sensitizes dopamine neurons to protein alterations and oxidative stress
    • DOI 10.1007/s00702-004-0167-2, Parkinson's Research in Progress
    • C. Mytilineou, K.S. McNaught, P. Shashidharan, J. Yabut, R.J. Baptiste, A. Parnandi, and C.W. Olanow Inhibition of proteasome activity sensitizes dopamine neurons to protein alterations and oxidative stress J. Neural Transm. 111 2004 1237 1251 (Pubitemid 39468388)
    • (2004) Journal of Neural Transmission , vol.111 , Issue.10-11 , pp. 1237-1251
    • Mytilineou, C.1    McNaught, K.St.P.2    Shashidharan, P.3    Yabut, J.4    Baptiste, R.J.5    Parnandi, A.6    Olanow, C.W.7


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