메뉴 건너뛰기




Volumn 88, Issue 10, 2006, Pages 1467-1477

Effects of oxidative modifications induced by the glycation of bovine serum albumin on its structure and on cultured adipose cells

Author keywords

Adipocytes; Albumin; Bovine serum albumin; Diabetes; Glycation; Oxidation; Oxidative stress

Indexed keywords

BORONIC ACID DERIVATIVE; BOVINE SERUM ALBUMIN; CARBONYL DERIVATIVE; ISOPROSTANE; THIOL GROUP; ISOPROSTANE DERIVATIVE; THIOL DERIVATIVE;

EID: 33750614168     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2006.05.011     Document Type: Article
Times cited : (78)

References (47)
  • 1
    • 0030843890 scopus 로고    scopus 로고
    • Association of serum albumin and mortality risk
    • Goldwasser P., and Feldman J. Association of serum albumin and mortality risk. J. Clin. Epidemiol. 50 (1997) 693-703
    • (1997) J. Clin. Epidemiol. , vol.50 , pp. 693-703
    • Goldwasser, P.1    Feldman, J.2
  • 3
    • 0025069762 scopus 로고
    • How to characterize a biological antioxidant
    • Halliwell B. How to characterize a biological antioxidant. Free Radic. Res. Commun. 9 (1990) 1-32
    • (1990) Free Radic. Res. Commun. , vol.9 , pp. 1-32
    • Halliwell, B.1
  • 4
    • 0028085940 scopus 로고
    • Antioxidant potential of anaerobic human plasma: role of serum albumin and thiols as scavengers of carbon radicals
    • Soriani M., Pietraforte D., and Minetti M. Antioxidant potential of anaerobic human plasma: role of serum albumin and thiols as scavengers of carbon radicals. Arch. Biochem. Biophys. 312 (1994) 180-188
    • (1994) Arch. Biochem. Biophys. , vol.312 , pp. 180-188
    • Soriani, M.1    Pietraforte, D.2    Minetti, M.3
  • 6
    • 0142122027 scopus 로고    scopus 로고
    • Intervention strategies to prevent pathogenetic effects of glycated albumin
    • Cohen M.P. Intervention strategies to prevent pathogenetic effects of glycated albumin. Arch. Biochem. Biophys. 419 (2003) 25-30
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 25-30
    • Cohen, M.P.1
  • 7
    • 0037386574 scopus 로고    scopus 로고
    • Glycated albumin increases oxidative stress, activates NF-kappa B and extracellular signal-regulated kinase (ERK), and stimulates ERK-dependent transforming growth factor-beta 1 production in macrophage RAW cells
    • Cohen M.P., Shea E., Chen S., and Shearman C.W. Glycated albumin increases oxidative stress, activates NF-kappa B and extracellular signal-regulated kinase (ERK), and stimulates ERK-dependent transforming growth factor-beta 1 production in macrophage RAW cells. J. Lab. Clin. Med. 141 (2003) 242-249
    • (2003) J. Lab. Clin. Med. , vol.141 , pp. 242-249
    • Cohen, M.P.1    Shea, E.2    Chen, S.3    Shearman, C.W.4
  • 8
    • 0032544387 scopus 로고    scopus 로고
    • Transition metals bind to glycated proteins forming redox active "glycochelates": implications for the pathogenesis of certain diabetic complications
    • Qian M., Liu M., and Eaton J.W. Transition metals bind to glycated proteins forming redox active "glycochelates": implications for the pathogenesis of certain diabetic complications. Biochem. Biophys. Res. Commun. 250 (1998) 385-389
    • (1998) Biochem. Biophys. Res. Commun. , vol.250 , pp. 385-389
    • Qian, M.1    Liu, M.2    Eaton, J.W.3
  • 10
    • 0037468396 scopus 로고    scopus 로고
    • CD36-mediated endocytic uptake of advanced glycation end products (AGE) in mouse 3T3-L1 and human subcutaneous adipocytes
    • Kuniyasu A., Ohgami N., Hayashi S., Miyazaki A., Horiuchi S., and Nakayama H. CD36-mediated endocytic uptake of advanced glycation end products (AGE) in mouse 3T3-L1 and human subcutaneous adipocytes. FEBS Lett. 537 (2003) 85-90
    • (2003) FEBS Lett. , vol.537 , pp. 85-90
    • Kuniyasu, A.1    Ohgami, N.2    Hayashi, S.3    Miyazaki, A.4    Horiuchi, S.5    Nakayama, H.6
  • 11
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 14
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 15
    • 0028291974 scopus 로고
    • Carbonyl assays for determination of oxidatively modified proteins
    • Levine R.L., Williams J.A., Stadtman E.R., and Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol. 233 (1994) 346-357
    • (1994) Methods Enzymol. , vol.233 , pp. 346-357
    • Levine, R.L.1    Williams, J.A.2    Stadtman, E.R.3    Shacter, E.4
  • 16
    • 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?
    • Halliwell B., and Whiteman M. Measuring reactive species and oxidative damage in vivo and in cell culture: how should you do it and what do the results mean?. Br. J. Pharmacol. 142 (2004) 231-255
    • (2004) Br. J. Pharmacol. , vol.142 , pp. 231-255
    • Halliwell, B.1    Whiteman, M.2
  • 17
    • 0037495999 scopus 로고    scopus 로고
    • The structure of the sugar residue in glycated human serum albumin and its molecular recognition by phenylboronate
    • Rohovec J., Maschmeyer T., Aime S., and Peters J.A. The structure of the sugar residue in glycated human serum albumin and its molecular recognition by phenylboronate. Chemistry (Easton) 9 (2003) 2193-2199
    • (2003) Chemistry (Easton) , vol.9 , pp. 2193-2199
    • Rohovec, J.1    Maschmeyer, T.2    Aime, S.3    Peters, J.A.4
  • 18
    • 0031916984 scopus 로고    scopus 로고
    • The free radical theory of aging matures
    • Beckman K.B., and Ames B.N. The free radical theory of aging matures. Physiol. Rev. 78 (1998) 547-581
    • (1998) Physiol. Rev. , vol.78 , pp. 547-581
    • Beckman, K.B.1    Ames, B.N.2
  • 19
    • 0033669936 scopus 로고    scopus 로고
    • Involvement of oxysterols and lysophosphatidylcholine in the oxidized LDL-induced impairment of serum albumin synthesis by HEPG2 cells
    • Bourdon E., Loreau N., Davignon J., Bernier L., and Blache D. Involvement of oxysterols and lysophosphatidylcholine in the oxidized LDL-induced impairment of serum albumin synthesis by HEPG2 cells. Arterioscler. Thromb. Vasc. Biol. 20 (2000) 2643-2650
    • (2000) Arterioscler. Thromb. Vasc. Biol. , vol.20 , pp. 2643-2650
    • Bourdon, E.1    Loreau, N.2    Davignon, J.3    Bernier, L.4    Blache, D.5
  • 20
    • 0038125611 scopus 로고    scopus 로고
    • Native protein glycoxidation and aging
    • Meli M., Frey J., and Perier C. Native protein glycoxidation and aging. J. Nutr. Health Aging 7 (2003) 263-266
    • (2003) J. Nutr. Health Aging , vol.7 , pp. 263-266
    • Meli, M.1    Frey, J.2    Perier, C.3
  • 21
    • 1242271236 scopus 로고    scopus 로고
    • Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering
    • Militello V., Casarino C., Emanuele A., Giostra A., Pullara F., and Leone M. Aggregation kinetics of bovine serum albumin studied by FTIR spectroscopy and light scattering. Biophys. Chem. 107 (2004) 175-187
    • (2004) Biophys. Chem. , vol.107 , pp. 175-187
    • Militello, V.1    Casarino, C.2    Emanuele, A.3    Giostra, A.4    Pullara, F.5    Leone, M.6
  • 22
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • Jackson M., and Mantsch H.H. The use and misuse of FTIR spectroscopy in the determination of protein structure. Crit. Rev. Biochem. Mol. Biol. 30 (1995) 95-120
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 23
    • 0031423671 scopus 로고    scopus 로고
    • Infrared spectroscopy: a new frontier in medicine
    • Jackson M., Sowa M.G., and Mantsch H.H. Infrared spectroscopy: a new frontier in medicine. Biophys. Chem. 68 (1997) 109-125
    • (1997) Biophys. Chem. , vol.68 , pp. 109-125
    • Jackson, M.1    Sowa, M.G.2    Mantsch, H.H.3
  • 24
    • 0025853670 scopus 로고
    • Protein glycation and oxidative stress in diabetes mellitus and ageing
    • Wolff S.P., Jiang Z.Y., and Hunt J.V. Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Radic. Biol. Med. 10 (1991) 339-352
    • (1991) Free Radic. Biol. Med. , vol.10 , pp. 339-352
    • Wolff, S.P.1    Jiang, Z.Y.2    Hunt, J.V.3
  • 26
    • 0842346333 scopus 로고    scopus 로고
    • Free radical biology-terminology and critical thinking
    • Azzi A., Davies K.J., and Kelly F. Free radical biology-terminology and critical thinking. FEBS Lett. 558 (2004) 3-6
    • (2004) FEBS Lett. , vol.558 , pp. 3-6
    • Azzi, A.1    Davies, K.J.2    Kelly, F.3
  • 27
    • 0032966525 scopus 로고    scopus 로고
    • Glucose and free radicals impair the antioxidant properties of serum albumin
    • Bourdon E., Loreau N., and Blache D. Glucose and free radicals impair the antioxidant properties of serum albumin. FASEB J. 13 (1999) 233-244
    • (1999) FASEB J. , vol.13 , pp. 233-244
    • Bourdon, E.1    Loreau, N.2    Blache, D.3
  • 28
    • 14644412955 scopus 로고    scopus 로고
    • Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin
    • Bourdon E., Loreau N., Lagrost L., and Blache D. Differential effects of cysteine and methionine residues in the antioxidant activity of human serum albumin. Free Radic. Res. 39 (2005) 15-20
    • (2005) Free Radic. Res. , vol.39 , pp. 15-20
    • Bourdon, E.1    Loreau, N.2    Lagrost, L.3    Blache, D.4
  • 29
    • 0142138645 scopus 로고    scopus 로고
    • The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants
    • Nakajou K., Watanabe H., Kragh-Hansen U., Maruyama T., and Otagiri M. The effect of glycation on the structure, function and biological fate of human serum albumin as revealed by recombinant mutants. Biochim. Biophys. Acta 1623 (2003) 88-97
    • (2003) Biochim. Biophys. Acta , vol.1623 , pp. 88-97
    • Nakajou, K.1    Watanabe, H.2    Kragh-Hansen, U.3    Maruyama, T.4    Otagiri, M.5
  • 30
    • 0037185973 scopus 로고    scopus 로고
    • Infrared spectroscopic study of diabetes platelets
    • Liu K.Z., Bose R., and Mantsch H.H. Infrared spectroscopic study of diabetes platelets. Vibrational spectroscopy 28 (2002) 131-136
    • (2002) Vibrational spectroscopy , vol.28 , pp. 131-136
    • Liu, K.Z.1    Bose, R.2    Mantsch, H.H.3
  • 32
    • 0035009582 scopus 로고    scopus 로고
    • The importance of proteins in defense against oxidation
    • Bourdon E., and Blache D. The importance of proteins in defense against oxidation. Antioxid. Redox Signal. 3 (2001) 293-311
    • (2001) Antioxid. Redox Signal. , vol.3 , pp. 293-311
    • Bourdon, E.1    Blache, D.2
  • 33
    • 22144469136 scopus 로고    scopus 로고
    • Heterogeneity and oxidation status of commercial human albumin preparations in clinical use
    • Bar-Or D., Bar-Or R., Rael L.T., Gardner D.K., Slone D.S., and Craun M.L. Heterogeneity and oxidation status of commercial human albumin preparations in clinical use. Crit. Care Med. 33 (2005) 1638-1641
    • (2005) Crit. Care Med. , vol.33 , pp. 1638-1641
    • Bar-Or, D.1    Bar-Or, R.2    Rael, L.T.3    Gardner, D.K.4    Slone, D.S.5    Craun, M.L.6
  • 35
    • 0033950545 scopus 로고    scopus 로고
    • Increased oxidative modification of albumin when illuminated in vitro in the presence of a common sunscreen ingredient: protection by nitroxide radicals
    • Damiani E., Carloni P., Biondi C., and Greci L. Increased oxidative modification of albumin when illuminated in vitro in the presence of a common sunscreen ingredient: protection by nitroxide radicals. Free Radic. Biol. Med. 28 (2000) 193-201
    • (2000) Free Radic. Biol. Med. , vol.28 , pp. 193-201
    • Damiani, E.1    Carloni, P.2    Biondi, C.3    Greci, L.4
  • 36
    • 16444381758 scopus 로고    scopus 로고
    • Detection and determination of glyceraldehyde-derived advanced glycation end product
    • Usui T., Shimohira K., Watanabe H., and Hayase F. Detection and determination of glyceraldehyde-derived advanced glycation end product. Biofactors 21 (2004) 391-394
    • (2004) Biofactors , vol.21 , pp. 391-394
    • Usui, T.1    Shimohira, K.2    Watanabe, H.3    Hayase, F.4
  • 37
    • 0034681114 scopus 로고    scopus 로고
    • Modifications of proteins by polyunsaturated fatty acid peroxidation products
    • Refsgaard H.H., Tsai L., and Stadtman E.R. Modifications of proteins by polyunsaturated fatty acid peroxidation products. Proc. Natl. Acad. Sci. USA 97 (2000) 611-616
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 611-616
    • Refsgaard, H.H.1    Tsai, L.2    Stadtman, E.R.3
  • 38
    • 0346100518 scopus 로고    scopus 로고
    • Scavenger receptors for oxidized and glycated proteins
    • Horiuchi S., Sakamoto Y., and Sakai M. Scavenger receptors for oxidized and glycated proteins. Amino Acids 25 (2003) 283-292
    • (2003) Amino Acids , vol.25 , pp. 283-292
    • Horiuchi, S.1    Sakamoto, Y.2    Sakai, M.3
  • 39
    • 0347480400 scopus 로고    scopus 로고
    • Free fatty acids and type 2 diabetes mellitus
    • Wyne K.L. Free fatty acids and type 2 diabetes mellitus. Am. J. Med. 115 Suppl 8A (2003) 29S-36S
    • (2003) Am. J. Med. , vol.115 , Issue.SUPPL. 8A
    • Wyne, K.L.1
  • 41
    • 1042289790 scopus 로고    scopus 로고
    • Cellular carbonyl stress enhances the expression of plasminogen activator inhibitor-1 in rat white adipocytes via reactive oxygen species-dependent pathway
    • Uchida Y., Ohba K., Yoshioka T., Irie K., Muraki T., and Maru Y. Cellular carbonyl stress enhances the expression of plasminogen activator inhibitor-1 in rat white adipocytes via reactive oxygen species-dependent pathway. J. Biol. Chem. 279 (2004) 4075-4083
    • (2004) J. Biol. Chem. , vol.279 , pp. 4075-4083
    • Uchida, Y.1    Ohba, K.2    Yoshioka, T.3    Irie, K.4    Muraki, T.5    Maru, Y.6
  • 43
    • 7444262475 scopus 로고    scopus 로고
    • Advanced glycation end products-modified proteins and oxidized LDL mediate down-regulation of leptin in mouse adipocytes via CD36
    • Unno Y., Sakai M., Sakamoto Y., Kuniyasu A., Nakayama H., Nagai R., and Horiuchi S. Advanced glycation end products-modified proteins and oxidized LDL mediate down-regulation of leptin in mouse adipocytes via CD36. Biochem. Biophys. Res. Commun. 325 (2004) 151-156
    • (2004) Biochem. Biophys. Res. Commun. , vol.325 , pp. 151-156
    • Unno, Y.1    Sakai, M.2    Sakamoto, Y.3    Kuniyasu, A.4    Nakayama, H.5    Nagai, R.6    Horiuchi, S.7
  • 44
    • 0037114857 scopus 로고    scopus 로고
    • Effect of high-glucose levels on protein oxidation in cultured lens cells, and in crystalline and albumin solution and its inhibition by vitamin B6 and N-acetylcysteine: its possible relevance to cataract formation in diabetes
    • Jain A.K., Lim G., Langford M., and Jain S.K. Effect of high-glucose levels on protein oxidation in cultured lens cells, and in crystalline and albumin solution and its inhibition by vitamin B6 and N-acetylcysteine: its possible relevance to cataract formation in diabetes. Free Radic. Biol. Med. 33 (2002) 1615-1621
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1615-1621
    • Jain, A.K.1    Lim, G.2    Langford, M.3    Jain, S.K.4
  • 45
    • 15244361487 scopus 로고    scopus 로고
    • Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins
    • Powell S.R., Wang P., Divald A., Teichberg S., Haridas V., McCloskey T.W., Davies K.J., and Katzeff H. Aggregates of oxidized proteins (lipofuscin) induce apoptosis through proteasome inhibition and dysregulation of proapoptotic proteins. Free Radic. Biol. Med. 38 (2005) 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.