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Volumn 59, Issue 3, 2010, Pages 670-678

Hyperglycemia impairs proteasome function by methylglyoxal

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT; LACTOYLGLUTATHIONE LYASE; METHYLGLYOXAL; PROTEASOME; ALBUMINOID; CHYMOTRYPSIN; GLUCOSE; INSULIN; POLYUBIQUITIN;

EID: 77950362951     PISSN: 00121797     EISSN: 1939327X     Source Type: Journal    
DOI: 10.2337/db08-1565     Document Type: Article
Times cited : (154)

References (39)
  • 1
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • DOI 10.1038/414813a
    • Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 2001;414:813-820 (Pubitemid 34000785)
    • (2001) Nature , vol.414 , Issue.6865 , pp. 813-820
    • Brownlee, M.1
  • 2
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • Thornalley PJ, Langborg A, Minhas HS. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 1999;344:109-116
    • (1999) Biochem J , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 3
    • 23744447530 scopus 로고    scopus 로고
    • Dicarbonyl intermediates in the maillard reaction
    • Thornalley PJ. Dicarbonyl intermediates in the maillard reaction. Ann N Y Acad Sci 2005;1043:111-117
    • (2005) Ann N Y Acad Sci , vol.1043 , pp. 111-117
    • Thornalley, P.J.1
  • 4
    • 0348049805 scopus 로고    scopus 로고
    • Accumulation of fructosyl-lysine and advanced glycation end products in the kidney, retina and peripheral nerve of streptozotocin-induced diabetic rats
    • Karachalias N, Babaei-Jadidi R, Ahmed N, Thornalley PJ. Accumulation of fructosyl-lysine and advanced glycation end products in the kidney, retina and peripheral nerve of streptozotocin-induced diabetic rats. Biochem Soc Trans 2003;31:1423-1425 (Pubitemid 38030991)
    • (2003) Biochemical Society Transactions , vol.31 , Issue.6 , pp. 1423-1425
    • Karachalias, N.1    Babaei-Jadidi, R.2    Ahmed, N.3    Thornalley, P.J.4
  • 6
    • 0030763201 scopus 로고    scopus 로고
    • Increased accumulation of the glycoxidation product N(epsilon)- (carboxymethyl)lysine in human tissues in diabetes and aging
    • Schleicher ED, Wagner E, Nerlich AG. Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl)lysine in human tissues in diabetes and aging. J Clin Invest 1997;99:457-468 (Pubitemid 27414803)
    • (1997) Journal of Clinical Investigation , vol.99 , Issue.3 , pp. 457-468
    • Schleicher, E.D.1    Wagner, E.2    Nerlich, A.G.3
  • 7
    • 0028304845 scopus 로고
    • Nonenzymatic glycosylation in vitro and in bovine endothelial cells alters basic fibroblast growth factor activity. a model for intracellular glycosylation in diabetes
    • Giardino I, Edelstein D, Brownlee M. Nonenzymatic glycosylation in vitro and in bovine endothelial cells alters basic fibroblast growth factor activity: a model for intracellular glycosylation in diabetes. J Clin Invest 1994;94:110-117 (Pubitemid 24218083)
    • (1994) Journal of Clinical Investigation , vol.94 , Issue.1 , pp. 110-117
    • Giardino, I.1    Edelstein, D.2    Brownlee, M.3
  • 9
    • 85047691537 scopus 로고    scopus 로고
    • Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells
    • Du X, Matsumura T, Edelstein D, Rossetti L, Zsengeller Z, Szabo C, Brownlee M. Inhibition of GAPDH activity by poly(ADP-ribose) polymerase activates three major pathways of hyperglycemic damage in endothelial cells. J Clin Invest 2003;112:1049-1057
    • (2003) J Clin Invest , vol.112 , pp. 1049-1057
    • Du, X.1    Matsumura, T.2    Edelstein, D.3    Rossetti, L.4    Zsengeller, Z.5    Szabo, C.6    Brownlee, M.7
  • 11
    • 0035072229 scopus 로고    scopus 로고
    • Degradation of oxidized proteins by the 20S proteasome
    • DOI 10.1016/S0300-9084(01)01250-0
    • Davies KJA. Degradation of oxidized proteins by the 20S proteasome. Biochimie 2001;83:301-310 (Pubitemid 32293650)
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 301-310
    • Davies, K.J.A.1
  • 12
    • 15244361487 scopus 로고    scopus 로고
    • Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins
    • Powell SR, Wang P, Divald A, Teichberg S, Haridas V, McCloskey TW, Davies KJ, Katzeff H. Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins. Free Radic Biol Med 2005;38:1093-1101
    • (2005) Free Radic Biol Med , vol.38 , pp. 1093-1101
    • Powell, S.R.1    Wang, P.2    Divald, A.3    Teichberg, S.4    Haridas, V.5    McCloskey, T.W.6    Davies, K.J.7    Katzeff, H.8
  • 13
    • 0346727127 scopus 로고    scopus 로고
    • Protein degradation and protection against misfolded or damaged proteins
    • Goldberg AL. Protein degradation and protection against misfolded or damaged proteins. Nature 2003;426:895-899
    • (2003) Nature , vol.426 , pp. 895-899
    • Goldberg, A.L.1
  • 14
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman MH, Ciechanover A. The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction. Physiol Rev 2002;82:373-428 (Pubitemid 34654457)
    • (2002) Physiological Reviews , vol.82 , Issue.2 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 15
    • 0344944630 scopus 로고    scopus 로고
    • Protein aggregation and aggregate toxicity: New insights into protein folding, misfolding diseases and biological evolution
    • DOI 10.1007/s00109-003-0464-5
    • Stefani M, Dobson CM. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution. J Mol Med 2003;81:678-699 (Pubitemid 37491594)
    • (2003) Journal of Molecular Medicine , vol.81 , Issue.11 , pp. 678-699
    • Stefani, M.1    Dobson, C.M.2
  • 16
    • 0032867796 scopus 로고    scopus 로고
    • Degradation of hypochlorite-damaged glucose-6-phosphate dehydrogenase by the 20S proteasome
    • DOI 10.1016/S0891-5849(99)00060-X, PII S089158499900060X
    • Ullrich O, Reinheckel T, Sitte N, Grune T. Degradation of hypochlorite-damaged glucose-6-phosphate dehydrogenase by the 20S proteasome. Free Radic Biol Med 1999;27:487-492 (Pubitemid 29408633)
    • (1999) Free Radical Biology and Medicine , vol.27 , Issue.5-6 , pp. 487-492
    • Ullrich, O.1    Reinheckel, T.2    Sitte, N.3    Grune, T.4
  • 17
    • 33845958531 scopus 로고    scopus 로고
    • Oxidative stress upregulates the ubiquitin proteasome pathway in retinal endothelial cells
    • Fernandes R, Ramalho J, Pereira P. Oxidative stress upregulates ubiquitin proteasome pathway in retinal endothelial cells. Mol Vis 2006;12:1526-1535 (Pubitemid 46029773)
    • (2006) Molecular Vision , vol.12 , pp. 1526-1535
    • Fernandes, R.1    Ramalho, J.2    Pereira, P.3
  • 18
    • 53349101264 scopus 로고    scopus 로고
    • Transient high glucose causes persistent epigenetic changes and altered gene expression during subsequent normoglycemia
    • El-Osta A, Brasacchio D, Yao D, Pocai A, Jones PL, Roeder RG, Cooper ME, Brownlee M. Transient high glucose causes persistent epigenetic changes and altered gene expression during subsequent normoglycemia. J Exp Med 2008;205:2409-2417
    • (2008) J Exp Med , vol.205 , pp. 2409-2417
    • El-Osta, A.1    Brasacchio, D.2    Yao, D.3    Pocai, A.4    Jones, P.L.5    Roeder, R.G.6    Cooper, M.E.7    Brownlee, M.8
  • 20
    • 0242551536 scopus 로고    scopus 로고
    • Ratchets and clocks: The cell cycle, ubiquitylation and protein turnover
    • Reed SI. Ratchets and clocks: the cell cycle, ubiquitylation and protein turnover. Nat Rev Mol Cell Biol 2003;4:855-864
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 855-864
    • Reed, S.I.1
  • 21
    • 0141729263 scopus 로고    scopus 로고
    • Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation
    • Lipford JR, Deshaies RJ. Diverse roles for ubiquitin-dependent proteolysis in transcriptional activation. Nat Cell Biol 2003;5:845-850
    • (2003) Nat Cell Biol , vol.5 , pp. 845-850
    • Lipford, J.R.1    Deshaies, R.J.2
  • 22
    • 0035074614 scopus 로고    scopus 로고
    • Subtypes of 20S proteasomes from skeletal muscle
    • DOI 10.1016/S0300-9084(01)01240-8
    • Dahlmann B, Ruppert T, Kloetzel PM, Kuehn L. Subtypes of 20S proteasomes from skeletal muscle. Biochimie 2001;83:295-299 (Pubitemid 32293649)
    • (2001) Biochimie , vol.83 , Issue.3-4 , pp. 295-299
    • Dahlmann, B.1    Ruppert, T.2    Kloetzel, P.M.3    Kuehn, L.4
  • 23
    • 0037181327 scopus 로고    scopus 로고
    • Qualitative determination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry peptide mapping
    • DOI 10.1021/jf011349o
    • Humeny A, Kislinger T, Becker CM, Pischetsrieder M. Qualitative determination of specific protein glycation products by matrix-assisted laser desorption/ionization mass spectrometry peptide mapping. J Agric Food Chem 2002;50:2153-2160 (Pubitemid 34260026)
    • (2002) Journal of Agricultural and Food Chemistry , vol.50 , Issue.7 , pp. 2153-2160
    • Humeny, A.1    Kislinger, T.2    Becker, C.-M.3    Pischetsrieder, M.4
  • 24
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel PM. Antigen processing by the proteasome. Nat Rev Mol Cell Biol 2001;2:179-187
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 25
    • 3042635556 scopus 로고    scopus 로고
    • High glucose down-regulates intercellular communication in retinal endothelial cells by enhancing degradation of connexin 43 by a proteasome-dependent mechanism
    • DOI 10.1074/jbc.M400446200
    • Fernandes R, Girao H, Pereira P. High glucose down-regulates intercellular communication in retinal endothelial cells by enhancing degradation of connexin 43 by a proteasome-dependent mechanism. J Biol Chem 2004;279:27219-27224 (Pubitemid 38812559)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27219-27224
    • Fernandes, R.1    Girao, H.2    Pereira, P.3
  • 26
    • 34548134851 scopus 로고    scopus 로고
    • Proteasome-dependent degradation of guanosine 5′-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus
    • Xu J, Wu Y, Song P, Zhang M, Wang S, Zou MH. Proteasome-dependent degradation of guanosine 5′-triphosphate cyclohydrolase I causes tetrahydrobiopterin deficiency in diabetes mellitus. Circulation 2007;116:944-953
    • (2007) Circulation , vol.116 , pp. 944-953
    • Xu, J.1    Wu, Y.2    Song, P.3    Zhang, M.4    Wang, S.5    Zou, M.H.6
  • 27
    • 33747619854 scopus 로고    scopus 로고
    • Insulin resistance accelerates muscle protein degradation: Activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling
    • DOI 10.1210/en.2006-0251
    • Wang X, Hu Z, Hu J, Du J, Mitch WE. Insulin resistance accelerates muscle protein degradation: activation of the ubiquitin-proteasome pathway by defects in muscle cell signaling. Endocrinology 2006;147:4160-4168 (Pubitemid 44268367)
    • (2006) Endocrinology , vol.147 , Issue.9 , pp. 4160-4168
    • Wang, X.1    Hu, Z.2    Hu, J.3    Du, J.4    Mitch, W.E.5
  • 28
    • 0032731757 scopus 로고    scopus 로고
    • Diabetes induces an impairment in the proteolytic activity against oxidized proteins and a heterogeneous effect in nonenzymatic protein modifications in the cytosol of rat liver and kidney
    • Portero-Otin M, Pamplona R, Ruiz MC, Cabiscol E, Prat J, Bellmunt MJ. Diabetes induces an impairment in the proteolytic activity against oxidized proteins and a heterogeneous effect in nonenzymatic protein modifications in the cytosol of rat liver and kidney. Diabetes 1999;48:2215-2220
    • (1999) Diabetes , vol.48 , pp. 2215-2220
    • Portero-Otin, M.1    Pamplona, R.2    Ruiz, M.C.3    Cabiscol, E.4    Prat, J.5    Bellmunt, M.J.6
  • 30
    • 0003461658 scopus 로고    scopus 로고
    • Advanced glycated albumin impairs protein degradation in the kidney proximal tubules cell line LLC-PK1
    • Noisy-le-grand
    • Sebekova K, Schinzel R, Ling H, Simm A, Xiang G, Gekle M, Munch G, Vamvakas S, Heidland A. Advanced glycated albumin impairs protein degradation in the kidney proximal tubules cell line LLC-PK1. Cell Mol Biol (Noisy-le-grand) 1998;44:1051-1060
    • (1998) Cell Mol Biol , vol.44 , pp. 1051-1060
    • Sebekova, K.1    Schinzel, R.2    Ling, H.3    Simm, A.4    Xiang, G.5    Gekle, M.6    Munch, G.7    Vamvakas, S.8    Heidland, A.9
  • 31
  • 32
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • DOI 10.1016/S1097-2765(00)80341-X
    • Kisselev AF, Akopian TN, Castillo V, Goldberg AL. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol Cell 1999;4:395-402 (Pubitemid 29499792)
    • (1999) Molecular Cell , vol.4 , Issue.3 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 33
    • 0027321526 scopus 로고
    • Inhibitory effect of nonenzymatic glycation on ubiquitination and ubiquitin-mediated degradation of lysozyme
    • DOI 10.1006/bbrc.1993.1471
    • Takizawa N, Takada K, Ohkawa K. Inhibitory effect of nonenzymatic glycation on ubiquitination and ubiquitin-mediated degradation of lysozyme. Biochem Biophys Res Commun 1993;192:700-706 (Pubitemid 23227379)
    • (1993) Biochemical and Biophysical Research Communications , vol.192 , Issue.2 , pp. 700-706
    • Takizawa, N.1    Takada, K.2    Ohkawa, K.3
  • 34
    • 0035824663 scopus 로고    scopus 로고
    • Proteasome Inhibition in Glyoxal-treated Fibroblasts and Resistance of Glycated Glucose-6-phosphate Dehydrogenase to 20 S Proteasome Degradation in Vitro
    • DOI 10.1074/jbc.M105374200
    • Bulteau AL, Verbeke P, Petropoulos I, Chaffotte AF, Friguet B. Proteasome inhibition in glyoxal-treated fibroblasts and resistance of glycated glucose-6-phosphate dehydrogenase to 20 S proteasome degradation in vitro. J Biol Chem 2001;276:45662-45668 (Pubitemid 37370801)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.49 , pp. 45662-45668
    • Bulteau, A.-L.1    Verbeke, P.2    Petropoulos, I.3    Chaffotte, A.-F.4    Friguet, B.5
  • 37
    • 10044294918 scopus 로고    scopus 로고
    • Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal
    • Ferrington DA, Kapphahn RJ. Catalytic site-specific inhibition of the 20S proteasome by 4-hydroxynonenal. FEBS Lett 2004;578:217-223
    • (2004) FEBS Lett , vol.578 , pp. 217-223
    • Ferrington, D.A.1    Kapphahn, R.J.2
  • 38
    • 33947110425 scopus 로고    scopus 로고
    • Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina
    • DOI 10.1016/j.exer.2006.12.002, PII S0014483506004581
    • Kapphahn RJ, Bigelow EJ, Ferrington DA. Age-dependent inhibition of proteasome chymotrypsin-like activity in the retina. Exp Eye Res 2007;84:646-654 (Pubitemid 46402984)
    • (2007) Experimental Eye Research , vol.84 , Issue.4 , pp. 646-654
    • Kapphahn, R.J.1    Bigelow, E.J.2    Ferrington, D.A.3
  • 39
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • DOI 10.1016/S0092-8674(03)00974-7
    • Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 2003;115:715-725 (Pubitemid 38030300)
    • (2003) Cell , vol.115 , Issue.6 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6


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