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Volumn 16, Issue 6, 2009, Pages 653-659

Inhibitory effects of β-Cyclodextrin and trehalose on nanofibril and AGE formation during glycation of human serum albumin

Author keywords

cyclodextrin; Diabetes; Glucose; Glycation; HSA; Trehalose

Indexed keywords

ADVANCED GLYCATION END PRODUCT; BETA CYCLODEXTRIN; BETA CYCLODEXTRIN DERIVATIVE; GLUCOSE; SERUM ALBUMIN; TREHALOSE;

EID: 67650141704     PISSN: 09298665     EISSN: None     Source Type: Journal    
DOI: 10.2174/092986609788490212     Document Type: Article
Times cited : (16)

References (35)
  • 1
    • 11144324314 scopus 로고    scopus 로고
    • Advanced glycation endproducts-role in pathology of diabetic complications
    • Ahmed, N. Advanced glycation endproducts-role in pathology of diabetic complications. Diabetes Res. Clin. Pract., 2005, 67(1), 3- 21.
    • (2005) Diabetes Res. Clin. Pract , vol.67 , Issue.1 , pp. 3-21
    • Ahmed, N.1
  • 2
    • 0344443743 scopus 로고    scopus 로고
    • Modification of proteins in vitro by physiological levels of glucose: Pyridoxamine inhibits conversion of Amadori intermediate to advanced glycation end-products through binding of redox metal ions
    • Voziyan, P.A.; Khalifah, R.G.; Thibaudeau, C.; Yildiz, A.; Jacob, J.; Serianni A.S.; Hudson, B.G. Modification of proteins in vitro by physiological levels of glucose: pyridoxamine inhibits conversion of Amadori intermediate to advanced glycation end-products through binding of redox metal ions. J. Biol. Chem., 2003, 278 , 46616-46624.
    • (2003) J. Biol. Chem , vol.278 , pp. 46616-46624
    • Voziyan, P.A.1    Khalifah, R.G.2    Thibaudeau, C.3    Yildiz, A.4    Jacob, J.5    Serianni, A.S.6    Hudson, B.G.7
  • 3
    • 14644397841 scopus 로고    scopus 로고
    • Characterization of advanced glycation end products for biochemical studies: Side chain modifications and fluorescence characteristics
    • Schmitt, A.; Schmitt, J.; Münch, G.; Gasic-Milencovic, J. Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics. J. Anal. Biochem., 2005, 338, 201-215.
    • (2005) J. Anal. Biochem , vol.338 , pp. 201-215
    • Schmitt, A.1    Schmitt, J.2    Münch, G.3    Gasic-Milencovic, J.4
  • 4
    • 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., 2003, 419, 25-30.
    • (2003) Arch. Biochem. Biophys , vol.419 , pp. 25-30
    • Cohen, M.P.1
  • 5
    • 0021365056 scopus 로고
    • Nonenzymatic glycosylation of human serum albumin alters its conformation and function
    • Shaklai, N.; Garlick, R. L.; Franklin Bunn, H. Nonenzymatic glycosylation of human serum albumin alters its conformation and function. J. Biol. Chem., 1984, 259(6), 3812-3817.
    • (1984) J. Biol. Chem , vol.259 , Issue.6 , pp. 3812-3817
    • Shaklai, N.1    Garlick, R.L.2    Franklin Bunn, H.3
  • 6
    • 0026664548 scopus 로고    scopus 로고
    • He, X.M.; Carter, D.C. Atomic structure and chemistry of human serum albumin. Nature, 1992, 358(6435), 209-215.
    • He, X.M.; Carter, D.C. Atomic structure and chemistry of human serum albumin. Nature, 1992, 358(6435), 209-215.
  • 7
    • 0032966525 scopus 로고    scopus 로고
    • Glucose and free radicals impair the antioxidant properties of serum albumin
    • Bourdon, E.; Loreau, N.; Blache, D. Glucose and free radicals impair the antioxidant properties of serum albumin. FASEB J.,1999, 13, 233-244.
    • (1999) FASEB J , vol.13 , pp. 233-244
    • Bourdon, E.1    Loreau, N.2    Blache, D.3
  • 8
    • 33645969616 scopus 로고    scopus 로고
    • Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus
    • Amr Darwish, M.; Othman, A.S. Protective ability and binding affinity of captopril towards serum albumin in an in vitro glycation model of diabetes mellitus. J. Pharm. Biomed. Anal., 2006, 41, 571-575.
    • (2006) J. Pharm. Biomed. Anal , vol.41 , pp. 571-575
    • Amr Darwish, M.1    Othman, A.S.2
  • 9
    • 0021231172 scopus 로고
    • Nonenzymic glycosylation and the pathogenesis of diabetic complications
    • Brownlee, M.; Vlassara, H.; Cerami A. Nonenzymic glycosylation and the pathogenesis of diabetic complications. Ann. Intern. Med.,1984, 101, 527-537.
    • (1984) Ann. Intern. Med , vol.101 , pp. 527-537
    • Brownlee, M.1    Vlassara, H.2    Cerami, A.3
  • 10
    • 43649104868 scopus 로고    scopus 로고
    • Effect of non-enzymatic glycosylation of pea albumins on their immunoreactive properties
    • Mierzejewska, D.; Mitrowska, P.; Rudnicka, B.; Kubicka, E.; Kostyra, H. Effect of non-enzymatic glycosylation of pea albumins on their immunoreactive properties. Food Chemistry, 2008, 111(1), 127-131.
    • (2008) Food Chemistry , vol.111 , Issue.1 , pp. 127-131
    • Mierzejewska, D.1    Mitrowska, P.2    Rudnicka, B.3    Kubicka, E.4    Kostyra, H.5
  • 11
    • 33646093461 scopus 로고    scopus 로고
    • Comparison of protective effects of aspirin, Dpenicillamine and vitamin E against high glucose-mediated toxicity in cultured endothelial cells
    • Zhang, J.; Slevin, M.; Duraisamy, Y.; Gaffney, J.; Smith, C.A.; Ahmed, N. Comparison of protective effects of aspirin, Dpenicillamine and vitamin E against high glucose-mediated toxicity in cultured endothelial cells. Biochim. Biophys. Acta., 2006, 1762, 551-557.
    • (2006) Biochim. Biophys. Acta , vol.1762 , pp. 551-557
    • Zhang, J.1    Slevin, M.2    Duraisamy, Y.3    Gaffney, J.4    Smith, C.A.5    Ahmed, N.6
  • 12
    • 34447647469 scopus 로고    scopus 로고
    • Structural characterization of water-soluble polysaccharides from Opuntia monacantha cladodes in relation to their anti-glycated activities
    • Zhao, M.; Yang, N.; Yang, B.; Jiang , Y.; Zhang, G. Structural characterization of water-soluble polysaccharides from Opuntia monacantha cladodes in relation to their anti-glycated activities Food Chem., 2007, 105, 1480-1486.
    • (2007) Food Chem , vol.105 , pp. 1480-1486
    • Zhao, M.1    Yang, N.2    Yang, B.3    Jiang, Y.4    Zhang, G.5
  • 13
    • 0000795884 scopus 로고    scopus 로고
    • Utilization of cyclodextrins in industrial products and processes
    • Szejtli, J. Utilization of cyclodextrins in industrial products and processes. J. Mat. Chem., 1997, 7, 575-587.
    • (1997) J. Mat. Chem , vol.7 , pp. 575-587
    • Szejtli, J.1
  • 14
    • 0033817382 scopus 로고    scopus 로고
    • Improvements of subcutaneous bioavailability of insulin by sulfobutyl ether -cyclodextrin in rats
    • Tokihiro, K.; Arima, H.; Tajiri, S.; Irie, T.; Hirayama, F.; Uekama, K. Improvements of subcutaneous bioavailability of insulin by sulfobutyl ether -cyclodextrin in rats. J. Pharm. Pharmacol., 2000, 52, 911-917.
    • (2000) J. Pharm. Pharmacol , vol.52 , pp. 911-917
    • Tokihiro, K.1    Arima, H.2    Tajiri, S.3    Irie, T.4    Hirayama, F.5    Uekama, K.6
  • 15
    • 0002686720 scopus 로고
    • Ability of cyclodextrins to inhibit aggregation of beta-casein
    • Lee, M. J.; Fennema, O. R. Ability of cyclodextrins to inhibit aggregation of beta-casein. J. Agric. Food Chem., 1991, 39(1), 17-21.
    • (1991) J. Agric. Food Chem , vol.39 , Issue.1 , pp. 17-21
    • Lee, M.J.1    Fennema, O.R.2
  • 16
    • 48149089155 scopus 로고    scopus 로고
    • Role of trehalose in moisture-induced aggregation of bovine serum albumin
    • Nishant, K. J.; Ipsita, R. Role of trehalose in moisture-induced aggregation of bovine serum albumin. Eur. J .Pharm. Biopharm.,2008, 69(3), 824-834.
    • (2008) Eur. J .Pharm. Biopharm , vol.69 , Issue.3 , pp. 824-834
    • Nishant, K.J.1    Ipsita, R.2
  • 18
    • 0030973690 scopus 로고    scopus 로고
    • The thermodynamic mechanism of protein stabilization by trehalose
    • Xie, G.; Timasheff, S.N. The thermodynamic mechanism of protein stabilization by trehalose. Biophys. Chem., 1997, 64, 25-43.
    • (1997) Biophys. Chem , vol.64 , pp. 25-43
    • Xie, G.1    Timasheff, S.N.2
  • 23
    • 0021285458 scopus 로고
    • Nonenzymatic glucosylation of lysine residues in albumin
    • Baynes, J.W.; Thorpe, S.R.; Murtiashaw, M.H. Nonenzymatic glucosylation of lysine residues in albumin. Methods Enzymol.,1984, 106, 88-98.
    • (1984) Methods Enzymol , vol.106 , pp. 88-98
    • Baynes, J.W.1    Thorpe, S.R.2    Murtiashaw, M.H.3
  • 24
    • 0036699372 scopus 로고    scopus 로고
    • Amadori product and age formation during nonenzymatic glycosylation of bovine serum albumin in vitro
    • Sharma, S.D.; Pandey, B.N.; Mishra, K.P.; Sivakami, S. Amadori product and age formation during nonenzymatic glycosylation of bovine serum albumin in vitro. J. Biochem. Mol. Biol. Biophys.,2002, 6, 233-242.
    • (2002) J. Biochem. Mol. Biol. Biophys , vol.6 , pp. 233-242
    • Sharma, S.D.1    Pandey, B.N.2    Mishra, K.P.3    Sivakami, S.4
  • 26
    • 0016305880 scopus 로고
    • The metabolism of alpha,alpha-trehalose
    • Elbein, A.D. The metabolism of alpha,alpha-trehalose. Adv. Carbohydrate Chem. Biochem., 1974, 30, 227-256.
    • (1974) Adv. Carbohydrate Chem. Biochem , vol.30 , pp. 227-256
    • Elbein, A.D.1
  • 27
    • 0001110679 scopus 로고
    • The chemistry of insect hymolymph
    • Wyatt, G.R.; Kalf, G.F. The chemistry of insect hymolymph. J. Gen. Physiol., 1957, 40, 833-847.
    • (1957) J. Gen. Physiol , vol.40 , pp. 833-847
    • Wyatt, G.R.1    Kalf, G.F.2
  • 29
    • 27744459448 scopus 로고    scopus 로고
    • Interactions of some modified mono- and bis-b-cyclodextrins with bovine serum albumin
    • Gao, H.; Wang, Y. N.; Fan, Y. G.; Ma, J. B. Interactions of some modified mono- and bis-b-cyclodextrins with bovine serum albumin. Bioorg. Med. Chem., 2006, 14, 131-137.
    • (2006) Bioorg. Med. Chem , vol.14 , pp. 131-137
    • Gao, H.1    Wang, Y.N.2    Fan, Y.G.3    Ma, J.B.4
  • 30
    • 48149089155 scopus 로고    scopus 로고
    • Role of trehalose in moisture-induced aggregation of bovine serum albumin
    • Jain, N.K.; Roy, I. Role of trehalose in moisture-induced aggregation of bovine serum albumin. Eur. J. Pharm. Biopharm., 2008, 69(3), 824-834.
    • (2008) Eur. J. Pharm. Biopharm , vol.69 , Issue.3 , pp. 824-834
    • Jain, N.K.1    Roy, I.2
  • 31
    • 0014411540 scopus 로고
    • Denaturation of proteins in 8 M urea as monitored by tryptophan fluorescence: Trypsin, trypsinogen and some derivatives
    • Hopkins, T.R.; Spikes, J.D. Denaturation of proteins in 8 M urea as monitored by tryptophan fluorescence: trypsin, trypsinogen and some derivatives. Biochem. Biophys. Res. Commun., 1968, 30, 540- 545.
    • (1968) Biochem. Biophys. Res. Commun , vol.30 , pp. 540-545
    • Hopkins, T.R.1    Spikes, J.D.2
  • 32
    • 0035028745 scopus 로고    scopus 로고
    • Mechanisms of tryptophan fluorescence shifts in proteins
    • Vivian, J.T.; Callis, P.R. Mechanisms of tryptophan fluorescence shifts in proteins. Biophys. J., 2001, 80, 2093-2109.
    • (2001) Biophys. J , vol.80 , pp. 2093-2109
    • Vivian, J.T.1    Callis, P.R.2
  • 33
    • 0015743401 scopus 로고
    • Studies on the tryptophan and drugbinding properties of human serum albumin fragments by affinity chromatography and circular dichroism measurements
    • Sjohlom, I.; Ljtjngstedt, I. Studies on the tryptophan and drugbinding properties of human serum albumin fragments by affinity chromatography and circular dichroism measurements. J. Biol. Chem., 1973, 248(24), 8434-8441.
    • (1973) J. Biol. Chem , vol.248 , Issue.24 , pp. 8434-8441
    • Sjohlom, I.1    Ljtjngstedt, I.2
  • 34
    • 0035397254 scopus 로고    scopus 로고
    • Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants
    • Watanabe, H.; Kragh-Hansen, U.; Tanase, S.; Nakajou, K.; Mitarai, M.; Iwao, Y.; Maruyama, T.; Otagiri, M. Conformational stability and warfarin-binding properties of human serum albumin studied by recombinant mutants. Biochem. J., 2001, 357, 269-274.
    • (2001) Biochem. J , vol.357 , pp. 269-274
    • Watanabe, H.1    Kragh-Hansen, U.2    Tanase, S.3    Nakajou, K.4    Mitarai, M.5    Iwao, Y.6    Maruyama, T.7    Otagiri, M.8
  • 35
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer?: An analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose
    • Kaushik, J.K.; Bhat, R. Why is trehalose an exceptional protein stabilizer?: an analysis of the thermal stability of proteins in the presence of the compatible osmolyte trehalose. J. Biol. Chem.,2003, 278(29), 26458-26465.
    • (2003) J. Biol. Chem , vol.278 , Issue.29 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.