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Volumn 247, Issue 3, 1997, Pages 1000-1008

Heparin-induced structural modifications and oxidative cleavage of human serum albumin in the absence and presence of glucose - Implications for transcapillary leakage of albumin in hyperglycaemia

Author keywords

Albumin; Glucose; Heparin; Oxidation; Protein structure

Indexed keywords

GLUCOSE; HEPARIN; HUMAN SERUM ALBUMIN; LOW MOLECULAR WEIGHT HEPARIN;

EID: 0030789489     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1432-1033.1997.01000.x     Document Type: Article
Times cited : (15)

References (46)
  • 1
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D. C. & Ho, J. K. (1994) Structure of serum albumin, Adv. Prot. Chem. 45, 153-203.
    • (1994) Adv. Prot. Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.K.2
  • 2
    • 0002820899 scopus 로고
    • Albumin interacts specifically with a 60-kDa microvascular endothelial glycoprotein
    • Schnitzer, J. E., Carley, W. W. & Palade, G. E. (1988) Albumin interacts specifically with a 60-kDa microvascular endothelial glycoprotein, Proc. Natl Acad. Sci. USA 85, 6773-6777.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 6773-6777
    • Schnitzer, J.E.1    Carley, W.W.2    Palade, G.E.3
  • 3
    • 0027940138 scopus 로고
    • Cell-bond albumin is the 70-kDa peptidoglycanlipopolysaccharide- and lipoteichoic acid-binding protein on lymphocytes and macrophages
    • Dziarski, R. (1994) Cell-bond albumin is the 70-kDa peptidoglycanlipopolysaccharide- and lipoteichoic acid-binding protein on lymphocytes and macrophages, J. Biol. Chem. 269, 20431-20436.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20431-20436
    • Dziarski, R.1
  • 4
    • 0030060322 scopus 로고    scopus 로고
    • Isolation and characterization of a cell surface albumin-binding protein from vascular endothelial cells
    • Tiruppathi, C., Finnegan, A. & Malik, A. B. (1996) Isolation and characterization of a cell surface albumin-binding protein from vascular endothelial cells, Proc. Natl Acad. Sci. USA 93, 250-254.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 250-254
    • Tiruppathi, C.1    Finnegan, A.2    Malik, A.B.3
  • 5
    • 0027049697 scopus 로고
    • Exogenous advanced glycosylation end products induce complex vascular disfunction in normal animals: A model for diabetic and aging complications
    • Vlassara, H., Fuh, H., Makita, Z., Krungkrai, S., Cerami, A. & Bucala, R. (1992) Exogenous advanced glycosylation end products induce complex vascular disfunction in normal animals: a model for diabetic and aging complications, Proc. Natl Acad. Sci. USA 89, 12043-12047.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 12043-12047
    • Vlassara, H.1    Fuh, H.2    Makita, Z.3    Krungkrai, S.4    Cerami, A.5    Bucala, R.6
  • 6
    • 0029073216 scopus 로고
    • Increased transendothelial permeation of albumin by high glucose concentration
    • Yamashita, T., Mimura, K., Umeda, F., Kobayashi, K., Hashimoto, T. & Nawata, H. (1995) Increased transendothelial permeation of albumin by high glucose concentration, Metabolism 44, 739-744.
    • (1995) Metabolism , vol.44 , pp. 739-744
    • Yamashita, T.1    Mimura, K.2    Umeda, F.3    Kobayashi, K.4    Hashimoto, T.5    Nawata, H.6
  • 8
    • 0020586544 scopus 로고
    • The principal site of nonenzymatic glycosylation of human serum albumin in vivo
    • Garlick, R. L. & Mazer, J. S. (1983) The principal site of nonenzymatic glycosylation of human serum albumin in vivo. J. Biol. Chem. 258, 6142-6146.
    • (1983) J. Biol. Chem. , vol.258 , pp. 6142-6146
    • Garlick, R.L.1    Mazer, J.S.2
  • 9
    • 0029165873 scopus 로고
    • Molecular characteristics of methyglyoxal-modified bovine and human serum albumin. Comparison with glucose-derivate advanced glycation endproduct-modified serum albumins
    • Westwood, M. E. & Thornalley, P. J. (1995) Molecular characteristics of methyglyoxal-modified bovine and human serum albumin. Comparison with glucose-derivate advanced glycation endproduct-modified serum albumins, J. Protein Chem. 14, 359-372.
    • (1995) J. Protein Chem. , vol.14 , pp. 359-372
    • Westwood, M.E.1    Thornalley, P.J.2
  • 10
    • 0001112738 scopus 로고
    • Aging of protein: Isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose
    • Pongor, S., Ulrich, P. C., Bencsath, F. A. & Cerami, A. (1984) Aging of protein: isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose, Proc. Natl Acad. Sci. USA 81, 2684-2688.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 2684-2688
    • Pongor, S.1    Ulrich, P.C.2    Bencsath, F.A.3    Cerami, A.4
  • 11
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification
    • Wolff, S. P. & Dean, R. T. (1987) Glucose autoxidation and protein modification, Biochem. J. 245, 243-250.
    • (1987) Biochem. J. , vol.245 , pp. 243-250
    • Wolff, S.P.1    Dean, R.T.2
  • 12
    • 0023708392 scopus 로고
    • Hydroxyl radical production and autoxidative glycosylation
    • Hunt, M., Dean, R. T. & Wolff, S. P. (1988) Hydroxyl radical production and autoxidative glycosylation, Biochem. J. 256, 205-212.
    • (1988) Biochem. J. , vol.256 , pp. 205-212
    • Hunt, M.1    Dean, R.T.2    Wolff, S.P.3
  • 13
    • 0028951461 scopus 로고
    • Mechanism of autoxidative glycosylation: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of protein by glucose
    • Wells-Knecht, K. J., Zyzak, D. V., Litchfield, J. E., Thorpe, S. R. & Baynes, J. W. (1995) Mechanism of autoxidative glycosylation: identification of glyoxal and arabinose as intermediates in the autoxidative modification of protein by glucose, Biochemistry 34, 3702-3709.
    • (1995) Biochemistry , vol.34 , pp. 3702-3709
    • Wells-Knecht, K.J.1    Zyzak, D.V.2    Litchfield, J.E.3    Thorpe, S.R.4    Baynes, J.W.5
  • 14
    • 0025540553 scopus 로고
    • Free radical generation by early glycation products: A mechanism for accelerated atherogenesis in diabetes
    • Mullarkey, C. J., Edelstein, D. & Brownlee, H. (1990) Free radical generation by early glycation products: a mechanism for accelerated atherogenesis in diabetes, Biochem. Biophys. Res. Commun. 173, 932-939.
    • (1990) Biochem. Biophys. Res. Commun. , vol.173 , pp. 932-939
    • Mullarkey, C.J.1    Edelstein, D.2    Brownlee, H.3
  • 15
    • 0026703158 scopus 로고
    • Immunochemical detection of advanced glycosylation end product in vivo
    • Makita, Z., Vlassara, H., Cerami, A. & Bucala, R. (1992) Immunochemical detection of advanced glycosylation end product in vivo, J. Biol. Chem. 267, 5133-5138.
    • (1992) J. Biol. Chem. , vol.267 , pp. 5133-5138
    • Makita, Z.1    Vlassara, H.2    Cerami, A.3    Bucala, R.4
  • 16
    • 0026521559 scopus 로고
    • Effects of nonenzymatic glycosylation and fatty acids on tryptophan binding to human serum albumin
    • Bohney, J. P. & Feldhoff, R. C.(1992) Effects of nonenzymatic glycosylation and fatty acids on tryptophan binding to human serum albumin. Biochem. Pharmacol. 43, 1829-1834.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1829-1834
    • Bohney, J.P.1    Feldhoff, R.C.2
  • 17
    • 0027732130 scopus 로고
    • Protein binding of digitoxin, valproate and phenytoin in sera from diabetics
    • Doucet, J., Fresel, J., Hue, G. & Moore, N. (1993) Protein binding of digitoxin, valproate and phenytoin in sera from diabetics, Eur. J. Clin. Pharmacol. 45, 577-579.
    • (1993) Eur. J. Clin. Pharmacol. , vol.45 , pp. 577-579
    • Doucet, J.1    Fresel, J.2    Hue, G.3    Moore, N.4
  • 19
    • 0028816999 scopus 로고
    • Evidence for a ligand receptor system mediating the biologic effects of glycated albumin in glomerular mesangial cells
    • Wu, V. Y. & Cohen, M. P. (1995) Evidence for a ligand receptor system mediating the biologic effects of glycated albumin in glomerular mesangial cells, Biochem. Biophys. Res. Commun. 207, 521-528.
    • (1995) Biochem. Biophys. Res. Commun. , vol.207 , pp. 521-528
    • Wu, V.Y.1    Cohen, M.P.2
  • 21
  • 22
    • 0029071294 scopus 로고
    • Reduction of heparan sulphate-associated anionic sites in the glomerular basement membrane of rats with streptozotocin-incubated diabetic nephropathy
    • Van den Born, J., Van Kraats, A. A., Bakker, M. A. H., Assmann, K. J. M., Dijkman, H. B. P. M., Van Der Laak, J. A. W. M. & Berden, J. H. M. (1995) Reduction of heparan sulphate-associated anionic sites in the glomerular basement membrane of rats with streptozotocin-incubated diabetic nephropathy, Diabetologia 38, 1169-1175.
    • (1995) Diabetologia , vol.38 , pp. 1169-1175
    • Van Den Born, J.1    Van Kraats, A.A.2    Bakker, M.A.H.3    Assmann, K.J.M.4    Dijkman, H.B.P.M.5    Van Der Laak, J.A.W.M.6    Berden, J.H.M.7
  • 24
    • 0028006546 scopus 로고
    • Heparin, sulfated heparinoids, and lipoteichoic acid bind to the 70-kDa peptidoglycan/lipopolysaccharide receptor protein on lymphocytes
    • Dziarski, R. & Gupta, D. (1994) Heparin, sulfated heparinoids, and lipoteichoic acid bind to the 70-kDa peptidoglycan/lipopolysaccharide receptor protein on lymphocytes, J. Biol. Chem. 269, 2100-2110.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2100-2110
    • Dziarski, R.1    Gupta, D.2
  • 25
    • 0024345442 scopus 로고
    • Phosphate promotes glycation of antithrombin III which interferes with heparin binding
    • Hall, P. K. & Roberts, R. C. (1989) Phosphate promotes glycation of antithrombin III which interferes with heparin binding, Biochim. Biophys. Acta 993, 217-223.
    • (1989) Biochim. Biophys. Acta , vol.993 , pp. 217-223
    • Hall, P.K.1    Roberts, R.C.2
  • 27
    • 0028304845 scopus 로고
    • Nonenzymatic glycosylation in vitro in bovine endothelial cells alters basic fibroblast grown factor activity
    • Giardino, I., Edelstein, D. & Brownlee, M. (1994) Nonenzymatic glycosylation in vitro in bovine endothelial cells alters basic fibroblast grown factor activity, J. Clin. Invest. 94, 110-117.
    • (1994) J. Clin. Invest. , vol.94 , pp. 110-117
    • Giardino, I.1    Edelstein, D.2    Brownlee, M.3
  • 28
  • 29
    • 0028108226 scopus 로고
    • Heparin-induced structural and functional alterations of bovine trypsin
    • Finotti, P. & Manente, S. (1994) Heparin-induced structural and functional alterations of bovine trypsin, Biochim. Biophys. Acta 1207, 80-87.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 80-87
    • Finotti, P.1    Manente, S.2
  • 30
    • 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. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 74, 248-254.
    • (1976) Anal. Biochem. , vol.74 , pp. 248-254
    • Bradford, M.M.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 8544223620 scopus 로고
    • Tests based on method of randomization
    • Prentice Hall, Englewood Cliffs, NJ
    • Bradley, J. V. (1968) Tests based on method of randomization, in Distribution free statistical tests, pp. 96-129, Prentice Hall, Englewood Cliffs, NJ.
    • (1968) Distribution Free Statistical Tests , pp. 96-129
    • Bradley, J.V.1
  • 34
    • 0001394390 scopus 로고
    • Preparation of phenyl thiohydantoins from some natural animo acids
    • Edman, P. (1950) Preparation of phenyl thiohydantoins from some natural animo acids, Acta Chem. Scand. 4, 277-293.
    • (1950) Acta Chem. Scand. , vol.4 , pp. 277-293
    • Edman, P.1
  • 35
    • 0000722070 scopus 로고
    • Spectral methods of characterizing protein conformation and conformutional changes
    • (Creighton, T. E., ed.) IRL Press, Oxford, UK
    • Schmid, F. X. (1990) Spectral methods of characterizing protein conformation and conformutional changes, in Protein structure: a practical approach (Creighton, T. E., ed.) pp. 251-285, IRL Press, Oxford, UK.
    • (1990) Protein Structure: A Practical Approach , pp. 251-285
    • Schmid, F.X.1
  • 36
    • 0023030789 scopus 로고    scopus 로고
    • Sequence of peptide susceptible to mixed-function oxidation
    • Farber, J. M. & Levine, R. L. (1996) Sequence of peptide susceptible to mixed-function oxidation, J. Biol. Chem. 261, 4574-4578.
    • (1996) J. Biol. Chem. , vol.261 , pp. 4574-4578
    • Farber, J.M.1    Levine, R.L.2
  • 37
    • 0027057334 scopus 로고
    • Reducing sugars can induce the oxidative inactivation of rhodanese
    • Horowitz, P. M., Butler, M. & McClure, G. D. (1992) Reducing sugars can induce the oxidative inactivation of rhodanese, J. Biol. Chem. 267, 23596-23600.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23596-23600
    • Horowitz, P.M.1    Butler, M.2    McClure, G.D.3
  • 38
    • 0028867715 scopus 로고
    • Oxidative damage of bovine serum albumin and other enzyme proteins by iron-chelate complexes
    • Ogino, T. & Okada, S. (1995) Oxidative damage of bovine serum albumin and other enzyme proteins by iron-chelate complexes, Biochim. Biophys. Acta 1245, 359-365.
    • (1995) Biochim. Biophys. Acta , vol.1245 , pp. 359-365
    • Ogino, T.1    Okada, S.2
  • 39
    • 0023473996 scopus 로고
    • Fructosamine: Structure, analysis, and clinical usefulness
    • Armbruster, D. A. (1987) Fructosamine: structure, analysis, and clinical usefulness, Clin. Chem. 33, 2153-2163.
    • (1987) Clin. Chem. , vol.33 , pp. 2153-2163
    • Armbruster, D.A.1
  • 40
    • 0025757266 scopus 로고
    • Metal-catalyzed oxidation of human serum albumin: Conformational and functional changes
    • Meucci, E., Mordente, A. & Martorana, E. (1981) Metal-catalyzed oxidation of human serum albumin: conformational and functional changes, J. Biol. Chem. 266, 4692-4699.
    • (1981) J. Biol. Chem. , vol.266 , pp. 4692-4699
    • Meucci, E.1    Mordente, A.2    Martorana, E.3
  • 41
    • 0024021040 scopus 로고
    • Conformational flexibility: A new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans
    • Casu, B., Petitou, M., Provasoli, M. & Sinaÿ, P. (1988) Conformational flexibility: a new concept for explaining binding and biological properties of iduronic acid-containing glycosaminoglycans, Trends Biochem. Sci. 13, 221-225.
    • (1988) Trends Biochem. Sci. , vol.13 , pp. 221-225
    • Casu, B.1    Petitou, M.2    Provasoli, M.3    Sinaÿ, P.4
  • 42
    • 0021365056 scopus 로고
    • Nonenzymatic glycosylation of human serum albumin alters its conformation and function
    • Shaklait, N., Garlick, R. L. & Bunn, H. F. (1984) Nonenzymatic glycosylation of human serum albumin alters its conformation and function, J. Biol. Chem. 259, 3812-3817.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3812-3817
    • Shaklait, N.1    Garlick, R.L.2    Bunn, H.F.3
  • 43
    • 0028004630 scopus 로고
    • Glycosaminoglycan-protein interactions: A question of specifity
    • Spillmann, D. & Lindahl, U. (1994) Glycosaminoglycan-protein interactions: a question of specifity, Curr. Opin. Struct. Biol. 4, 677-682.
    • (1994) Curr. Opin. Struct. Biol. , vol.4 , pp. 677-682
    • Spillmann, D.1    Lindahl, U.2
  • 44
    • 0028890715 scopus 로고
    • Protein hydroperoxides can give rise to reactive free radicals
    • Davies, M. J., Fu, S. & Dean, R. T. (1995) Protein hydroperoxides can give rise to reactive free radicals, Biochem. J. 305, 643-649.
    • (1995) Biochem. J. , vol.305 , pp. 643-649
    • Davies, M.J.1    Fu, S.2    Dean, R.T.3
  • 45
    • 0002964990 scopus 로고
    • Estimating molecular weights of polypeptides by SDS gel electrophoresis
    • (Creighton, T. E., ed.) IRL Press, Oxford, UK
    • See, Y. P. & Jackowski, G. (1990) Estimating molecular weights of polypeptides by SDS gel electrophoresis, in Protein structure: a practical approach (Creighton, T. E., ed.) pp. 1-21, IRL Press, Oxford, UK.
    • (1990) Protein Structure: A Practical Approach , pp. 1-21
    • See, Y.P.1    Jackowski, G.2


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