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Volumn 404, Issue 1-2, 2015, Pages 193-201

Antioxidant capacity and structural changes of human serum albumin from patients in advanced stages of diabetic nephropathy and the effect of the dialysis

Author keywords

Albumin conformational changes; Diabetes; Diabetic nephropathy; Hemodialysis; Human serum albumin; Oxidative stress

Indexed keywords

HUMAN SERUM ALBUMIN; THIOL GROUP; TRYPTOPHAN; SERUM ALBUMIN;

EID: 84941741965     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-015-2378-2     Document Type: Article
Times cited : (11)

References (42)
  • 3
    • 2942572700 scopus 로고    scopus 로고
    • Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean
    • COI: 1:CAS:528:DC%2BD2cXkvVyks7w%3D
    • Halliwell B, Whiteman M (2004) Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean. Brit J Pharmacol 142:231–255
    • (2004) Brit J Pharmacol , vol.142 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 4
    • 44449128155 scopus 로고    scopus 로고
    • The antioxidant properties of serum albumin
    • COI: 1:CAS:528:DC%2BD1cXms1Witrk%3D, PID: 18474236
    • Roche M, Rondeau P, Singh NR, Tarnus E, Bourdon E (2008) The antioxidant properties of serum albumin. FEBS Lett 582:1783–1787
    • (2008) FEBS Lett , vol.582 , pp. 1783-1787
    • Roche, M.1    Rondeau, P.2    Singh, N.R.3    Tarnus, E.4    Bourdon, E.5
  • 5
    • 65249134948 scopus 로고    scopus 로고
    • Pharmaceutically important pre- and posttranslational modifications on human serum albumin
    • COI: 1:CAS:528:DC%2BD1MXmsVGmur0%3D, PID: 19336879
    • Otagiri M, Chuang VT (2009) Pharmaceutically important pre- and posttranslational modifications on human serum albumin. Biol Pharm Bull 32:527–534
    • (2009) Biol Pharm Bull , vol.32 , pp. 527-534
    • Otagiri, M.1    Chuang, V.T.2
  • 6
    • 0028094666 scopus 로고
    • A new structural transition of serum albumin dependent on the state of Cys34
    • COI: 1:CAS:528:DyaK2cXmslCksbc%3D, PID: 7925457
    • Christodoulou J, Sadler PJ, Tucker A (1994) A new structural transition of serum albumin dependent on the state of Cys34. Eur J Biochem 225:363–368
    • (1994) Eur J Biochem , vol.225 , pp. 363-368
    • Christodoulou, J.1    Sadler, P.J.2    Tucker, A.3
  • 7
    • 79952218756 scopus 로고    scopus 로고
    • Elimination of endogenous toxin, creatinine from blood plasma depends on albumin conformation: site specific uremic toxicity and impaired drug binding
    • Varshney A, Rehan M, Subbarao N, Rabbani G, Khan RH (2011) Elimination of endogenous toxin, creatinine from blood plasma depends on albumin conformation: site specific uremic toxicity and impaired drug binding. PLoS ONE 6:1–15
    • (2011) PLoS ONE , vol.6 , pp. 1-15
    • Varshney, A.1    Rehan, M.2    Subbarao, N.3    Rabbani, G.4    Khan, R.H.5
  • 8
    • 34347324020 scopus 로고    scopus 로고
    • Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties
    • COI: 1:CAS:528:DC%2BD2sXntFemsbo%3D, PID: 17471184
    • Oettl K, Stauber RE (2007) Physiological and pathological changes in the redox state of human serum albumin critically influence its binding properties. Br J Pharmacol 151:580–590
    • (2007) Br J Pharmacol , vol.151 , pp. 580-590
    • Oettl, K.1    Stauber, R.E.2
  • 9
    • 65549092679 scopus 로고    scopus 로고
    • Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment
    • COI: 1:CAS:528:DC%2BD1MXls1ynsbk%3D, PID: 19330257
    • Turell L, Carballal S, Botti H, Radi R, Alvarez B (2009) Oxidation of the albumin thiol to sulfenic acid and its implications in the intravascular compartment. Braz J Med Biol Res 42:305–311
    • (2009) Braz J Med Biol Res , vol.42 , pp. 305-311
    • Turell, L.1    Carballal, S.2    Botti, H.3    Radi, R.4    Alvarez, B.5
  • 10
    • 0034951428 scopus 로고    scopus 로고
    • Albumin is the major plasma protein target of oxidant stress in uremia
    • COI: 1:CAS:528:DC%2BD3MXltlKnu7o%3D, PID: 11422772
    • Himmelfarb J, McMonagle E (2001) Albumin is the major plasma protein target of oxidant stress in uremia. Kidney Int 60:358–363
    • (2001) Kidney Int , vol.60 , pp. 358-363
    • Himmelfarb, J.1    McMonagle, E.2
  • 11
    • 44449138990 scopus 로고    scopus 로고
    • Impairment of serum albumin antioxidant properties in obstructive sleep apnoea syndrome
    • COI: 1:CAS:528:DC%2BD1cXmvV2lt7c%3D, PID: 18256067
    • Faure P, Tamisier R, Baguet JP, Favier A, Halimi S, Levy PE, Pepin J (2008) Impairment of serum albumin antioxidant properties in obstructive sleep apnoea syndrome. Eur Respir J 31:1046–1053
    • (2008) Eur Respir J , vol.31 , pp. 1046-1053
    • Faure, P.1    Tamisier, R.2    Baguet, J.P.3    Favier, A.4    Halimi, S.5    Levy, P.E.6    Pepin, J.7
  • 12
    • 1642276935 scopus 로고    scopus 로고
    • Problems in serum albumin measurement and clinical significance of albumin microheterogeneity in cirrhotics
    • COI: 1:CAS:528:DC%2BD2cXisVemtLs%3D, PID: 15043850
    • Watanabe A, Matsuzaki S, Moriwaki H, Suzuki K, Nishiguchi S (2004) Problems in serum albumin measurement and clinical significance of albumin microheterogeneity in cirrhotics. Nutrition 20:351–357
    • (2004) Nutrition , vol.20 , pp. 351-357
    • Watanabe, A.1    Matsuzaki, S.2    Moriwaki, H.3    Suzuki, K.4    Nishiguchi, S.5
  • 13
    • 17744380261 scopus 로고    scopus 로고
    • Albumin antioxidant capacity is modified by methylglyoxal
    • COI: 1:CAS:528:DC%2BD2MXlt1Ojsbs%3D, PID: 15959423
    • Faure P, Troncy L, Lecomte Wiernsperger MN, Lagarde M, Ruggiero D, Halimi S (2005) Albumin antioxidant capacity is modified by methylglyoxal. Diabetes Metab 31:169–177
    • (2005) Diabetes Metab , vol.31 , pp. 169-177
    • Faure, P.1    Troncy, L.2    Lecomte, W.M.N.3    Lagarde, M.4    Ruggiero, D.5    Halimi, S.6
  • 14
    • 79953041507 scopus 로고    scopus 로고
    • Decrease in reduced-form albumin among chronic kidney disease patients: new insights in cardiovascular complications
    • COI: 1:CAS:528:DC%2BC3MXms1GksLY%3D, PID: 21426508
    • Terawaki H, Era S, Nakayama M, Hosoya T (2011) Decrease in reduced-form albumin among chronic kidney disease patients: new insights in cardiovascular complications. Ther Apher Dial 15:156–160
    • (2011) Ther Apher Dial , vol.15 , pp. 156-160
    • Terawaki, H.1    Era, S.2    Nakayama, M.3    Hosoya, T.4
  • 15
    • 68749120642 scopus 로고    scopus 로고
    • Albumin thiol oxidation and serum protein carbonyl formation are progressively enhanced with advancing stages of chronic kidney disease
    • COI: 1:CAS:528:DC%2BD1MXhtF2isbjN, PID: 19363646
    • Matsuyama Y, Terawaki H, Terada T, Era S (2009) Albumin thiol oxidation and serum protein carbonyl formation are progressively enhanced with advancing stages of chronic kidney disease. Clin Exp Nephrol 13:308–315
    • (2009) Clin Exp Nephrol , vol.13 , pp. 308-315
    • Matsuyama, Y.1    Terawaki, H.2    Terada, T.3    Era, S.4
  • 17
    • 0142122027 scopus 로고    scopus 로고
    • Intervention strategies to prevent pathogenetic effects of glycated albumin
    • COI: 1:CAS:528:DC%2BD3sXotVCjur8%3D, PID: 14568005
    • Cohen MP (2003) Intervention strategies to prevent pathogenetic effects of glycated albumin. Arch Biochem Biophys 419:25–30
    • (2003) Arch Biochem Biophys , vol.419 , pp. 25-30
    • Cohen, M.P.1
  • 18
    • 33947723675 scopus 로고    scopus 로고
    • Assessment of temperature effects on beta-aggregation of native and glycated albumin by FTIR spectroscopy and PAGE: relations between structural changes and antioxidant properties
    • COI: 1:CAS:528:DC%2BD2sXjslSlsrY%3D, PID: 17320036
    • Rondeau P, Armenta S, Caillens H, Chesne S, Bourdon E (2007) Assessment of temperature effects on beta-aggregation of native and glycated albumin by FTIR spectroscopy and PAGE: relations between structural changes and antioxidant properties. Arch Biochem Biophys 460:141–150
    • (2007) Arch Biochem Biophys , vol.460 , pp. 141-150
    • Rondeau, P.1    Armenta, S.2    Caillens, H.3    Chesne, S.4    Bourdon, E.5
  • 19
    • 0034916487 scopus 로고    scopus 로고
    • Oxidation of albumin is enhanced in the presence of uremic toxins
    • COI: 1:CAS:528:DC%2BD3MXmtFequrk%3D, PID: 11499570
    • Wratten ML, Sereni L, Tetta C (2001) Oxidation of albumin is enhanced in the presence of uremic toxins. Ren Fail 23:563–571
    • (2001) Ren Fail , vol.23 , pp. 563-571
    • Wratten, M.L.1    Sereni, L.2    Tetta, C.3
  • 20
    • 0036233828 scopus 로고    scopus 로고
    • Useful markers for detecting decreased serum antioxidant activity in hemodialysis patients
    • COI: 1:CAS:528:DC%2BD38XktFWmsL0%3D, PID: 11979348
    • Soejima A, Kaneda F, Manno S, Matsuzawa N, Kouji H, Nagasawa T, Era S, Takakuwa Y (2002) Useful markers for detecting decreased serum antioxidant activity in hemodialysis patients. Am J Kidney Dis 39:1040–1046
    • (2002) Am J Kidney Dis , vol.39 , pp. 1040-1046
    • Soejima, A.1    Kaneda, F.2    Manno, S.3    Matsuzawa, N.4    Kouji, H.5    Nagasawa, T.6    Era, S.7    Takakuwa, Y.8
  • 21
    • 84871995815 scopus 로고    scopus 로고
    • Standards of medical care in diabetes–2013
    • American Diabetes Association (2013) Standards of medical care in diabetes–2013. Diabetes Care 36:S11–S66
    • (2013) Diabetes Care , vol.36 , pp. 11-66
    • American Diabetes Association1
  • 22
    • 0036318194 scopus 로고    scopus 로고
    • Quick measurement of protein sulfhydryls with Ellman’s reagent and with 4, 4′-dithiodipyridine
    • COI: 1:CAS:528:DC%2BD38XltVehs78%3D, PID: 12110978
    • Riener CK, Kada G, Gruber HJ (2002) Quick measurement of protein sulfhydryls with Ellman’s reagent and with 4, 4′-dithiodipyridine. Anal Bioanal Chem 373:266–276
    • (2002) Anal Bioanal Chem , vol.373 , pp. 266-276
    • Riener, C.K.1    Kada, G.2    Gruber, H.J.3
  • 23
    • 77749277059 scopus 로고    scopus 로고
    • Protein antioxidant response to the stress and relationship between molecular structure and antioxidant function
    • Medina-Navarro R, Durán-Reyes G, Díaz-Flores M, Vilar-Rojas C (2010) Protein antioxidant response to the stress and relationship between molecular structure and antioxidant function. PLoS ONE 5:1–10
    • (2010) PLoS ONE , vol.5 , pp. 1-10
    • Medina-Navarro, R.1    Durán-Reyes, G.2    Díaz-Flores, M.3    Vilar-Rojas, C.4
  • 24
    • 0023741303 scopus 로고    scopus 로고
    • Oxidation of cyanide to the cyanyl radical by peroxidase/H2O2 systems as determined by spin trapping
    • Moreno SN, Stolze K, Janzen EG, Mason RP (1998) Oxidation of cyanide to the cyanyl radical by peroxidase/H2O2 systems as determined by spin trapping. Arch Biochem Biophys 265:267–271
    • (1998) Arch Biochem Biophys , vol.265 , pp. 267-271
    • Moreno, S.N.1    Stolze, K.2    Janzen, E.G.3    Mason, R.P.4
  • 26
    • 0021954649 scopus 로고
    • Spin trapping of the azidyl radical in azide/catalase/H2O2 and various azide/peroxidase/H2O2 peroxidizing systems
    • COI: 1:CAS:528:DyaL2MXitVShsLs%3D, PID: 2984193
    • Kalyanaraman B, Janzen EG, Mason RP (1985) Spin trapping of the azidyl radical in azide/catalase/H2O2 and various azide/peroxidase/H2O2 peroxidizing systems. J Biol Chem 260:4003–4006
    • (1985) J Biol Chem , vol.260 , pp. 4003-4006
    • Kalyanaraman, B.1    Janzen, E.G.2    Mason, R.P.3
  • 27
    • 0030800233 scopus 로고    scopus 로고
    • Enhanced chemiluminescent assay for measuring the total antioxidant capacity of serum, saliva and crevicular fluid
    • COI: 1:CAS:528:DyaK2sXltlWksrY%3D, PID: 9247675
    • Chapple I, Mason GI, Garner I, Matthews JB, Thorpe GH, Maxwell SR, Whitehead TP (1997) Enhanced chemiluminescent assay for measuring the total antioxidant capacity of serum, saliva and crevicular fluid. Ann Clin Biochem 34:412–421
    • (1997) Ann Clin Biochem , vol.34 , pp. 412-421
    • Chapple, I.1    Mason, G.I.2    Garner, I.3    Matthews, J.B.4    Thorpe, G.H.5    Maxwell, S.R.6    Whitehead, T.P.7
  • 28
    • 0016916438 scopus 로고
    • Prediction of creatinine clearance from serum creatinine
    • COI: 1:STN:280:DyaE28%2FnsF2isw%3D%3D, PID: 1244564
    • Cockcroft DW, Gault MH (1976) Prediction of creatinine clearance from serum creatinine. Nephron 16:31–41
    • (1976) Nephron , vol.16 , pp. 31-41
    • Cockcroft, D.W.1    Gault, M.H.2
  • 29
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • COI: 1:CAS:528:DyaK2MXpsVGqt7k%3D, PID: 8563639
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411–2423
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 30
    • 0018903487 scopus 로고
    • Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinamide fluorescence quenching
    • COI: 1:CAS:528:DyaL3cXntFehug%3D%3D, PID: 7188848
    • Peterman BF, Laidler KJ (1980) Study of reactivity of tryptophan residues in serum albumins and lysozyme by N-bromosuccinamide fluorescence quenching. Arch Biochem Biophys 199:158–164
    • (1980) Arch Biochem Biophys , vol.199 , pp. 158-164
    • Peterman, B.F.1    Laidler, K.J.2
  • 33
    • 0032867556 scopus 로고    scopus 로고
    • The three recombinant domains of human serum albumin
    • COI: 1:CAS:528:DyaK1MXmslWqtbk%3D, PID: 10506189
    • Dockal M, Carter DC, Ruker F (1999) The three recombinant domains of human serum albumin. J Biol Chem 274:29303–29310
    • (1999) J Biol Chem , vol.274 , pp. 29303-29310
    • Dockal, M.1    Carter, D.C.2    Ruker, F.3
  • 34
    • 70350455500 scopus 로고    scopus 로고
    • Lessons from the crystallographic analysis of small molecule binding to human serum albumin
    • COI: 1:CAS:528:DC%2BD1MXhtlensLbL
    • Curry S (2009) Lessons from the crystallographic analysis of small molecule binding to human serum albumin. Drug Metab Pharm 24:342–357
    • (2009) Drug Metab Pharm , vol.24 , pp. 342-357
    • Curry, S.1
  • 35
    • 0033062612 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin at 2.5 Å resolution
    • COI: 1:CAS:528:DyaK1MXkslGhsb4%3D, PID: 10388840
    • Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K (1999) Crystal structure of human serum albumin at 2.5 Å resolution. Protein Eng 12:439–446
    • (1999) Protein Eng , vol.12 , pp. 439-446
    • Sugio, S.1    Kashima, A.2    Mochizuki, S.3    Noda, M.4    Kobayashi, K.5
  • 36
    • 34548041437 scopus 로고    scopus 로고
    • Analysis of the kinetics of folding of proteins and peptides using circular dichroism
    • COI: 1:CAS:528:DC%2BD2sXhtFGjtL3J, PID: 17406548
    • Greenfield NJ (2006) Analysis of the kinetics of folding of proteins and peptides using circular dichroism. Nat Protoc 1:2891–2899
    • (2006) Nat Protoc , vol.1 , pp. 2891-2899
    • Greenfield, N.J.1
  • 39
    • 0017817716 scopus 로고
    • Interaction of bilirubin with lipids studied by fluorescence quenching method
    • COI: 1:CAS:528:DyaE1cXhsVOrsr4%3D, PID: 632251
    • Nagaoka S, Cowger ML (1978) Interaction of bilirubin with lipids studied by fluorescence quenching method. J Biol Chem 253:2005–2011
    • (1978) J Biol Chem , vol.253 , pp. 2005-2011
    • Nagaoka, S.1    Cowger, M.L.2
  • 40
    • 84859716804 scopus 로고    scopus 로고
    • Structural modifications of human albumin in diabetes
    • COI: 1:CAS:528:DC%2BC38XlvVSltrs%3D, PID: 22349032
    • Guerin-Dubourg A, Catan AA, Bourdon E, Rondeau P (2012) Structural modifications of human albumin in diabetes. Diabetes Metab 38:171–178
    • (2012) Diabetes Metab , vol.38 , pp. 171-178
    • Guerin-Dubourg, A.1    Catan, A.A.2    Bourdon, E.3    Rondeau, P.4
  • 42
    • 70349916351 scopus 로고    scopus 로고
    • The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation end products restricting intramolecular movement
    • COI: 1:CAS:528:DC%2BC3cXisVGrs7o%3D, PID: 19484197
    • Zoellner H, Siddiqui S, Kelly E, Medbury H (2009) The anti-apoptotic activity of albumin for endothelium is inhibited by advanced glycation end products restricting intramolecular movement. Cell Mol Biol Lett 14:575–586
    • (2009) Cell Mol Biol Lett , vol.14 , pp. 575-586
    • Zoellner, H.1    Siddiqui, S.2    Kelly, E.3    Medbury, H.4


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