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Volumn 63, Issue 1, 2011, Pages 26-29

Physicochemical analysis of poly-L-lysine: An insight into the changes induced in lysine residues of proteins on modification with glucose

Author keywords

electrophoresis; glucose; glycation; hyperglycemia; lysine; spectroscopy

Indexed keywords

GLUCOSE; LYSINE; NITROBLUE TETRAZOLIUM; POLYLYSINE; POLYMER; TETRAZOLIUM;

EID: 79952000922     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.410     Document Type: Article
Times cited : (22)

References (26)
  • 1
    • 0025373091 scopus 로고
    • Nonenzymatic glycosylation, the Maillard reaction and the aging process
    • Monnier, V. M., (1990) Nonenzymatic glycosylation, the Maillard reaction and the aging process. J. Gerontol. 45, B105-B111. (Pubitemid 20224052)
    • (1990) Journals of Gerontology , vol.45 , Issue.4
    • Monnier, V.M.1
  • 2
    • 0022251563 scopus 로고
    • Glycation of amino groups in protein
    • Watkins, N. G., Thorpe, S. R., and, Baynes, J. W., (1985) Glycation of amino groups in protein. J. Biol. Chem. 260, 10629-10636.
    • (1985) J. Biol. Chem. , vol.260 , pp. 10629-10636
    • Watkins, N.G.1    Thorpe, S.R.2    Baynes, J.W.3
  • 4
    • 38349009152 scopus 로고    scopus 로고
    • The improvement effect of L-Lys as a chemical chaperone on STZ-induced diabetic rats, protein structure and function
    • DOI 10.1002/dmrr.769
    • Jafarnejad, A., Bathaie, S. J., Nakhjavani, M., Hassan, M. J., and, Banasadegh, S., (2008) The improvement effect of l -lysine as a chemical chaperone on STZ-induced diabetic rats, protein structure and function. Diabetes Metab. Res. Rev. 24, 64-73. (Pubitemid 351176002)
    • (2008) Diabetes/Metabolism Research and Reviews , vol.24 , Issue.1 , pp. 64-73
    • Jafarnejad, A.1    Bathaie, S.Z.2    Nakhjavani, M.3    Hassan, M.Z.4    Banasadegh, S.5
  • 5
    • 79951989375 scopus 로고    scopus 로고
    • Inhibition of protein glycation with varying concentrations of lysine
    • Sims, H. M., Birdwell, A. L., O'Reilley, K. E., Bwashi, A., and, Wing, B. D., (2008) Inhibition of protein glycation with varying concentrations of lysine. FASEB J. 22, 1123.15.
    • (2008) FASEB J. , vol.22 , pp. 112315
    • Sims, H.M.1    Birdwell, A.L.2    O'Reilley, K.E.3    Bwashi, A.4    Wing, B.D.5
  • 6
    • 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
  • 7
    • 26444478269 scopus 로고    scopus 로고
    • Advanced glycation end products and RAGE: A common thread in aging, diabetes, neurodegeneration, and inflammation
    • DOI 10.1093/glycob/cwi053
    • Ramasamy, R., Vannucci, S. J., Yan, S. S. D., Herold, K., Yan, S. F., and, Schmidt, A. M., (2005) Advanced glycation end products and RAGE: a common thread in aging, diabetes, neurodegeneration, and inflammation. Glycobiology 15, 16R-28R. (Pubitemid 41417992)
    • (2005) Glycobiology , vol.15 , Issue.7
    • Ramasamy, R.1    Vannucci, S.J.2    Yan, S.S.D.3    Herold, K.4    Yan, S.F.5    Schmidt, A.M.6
  • 8
    • 42549126759 scopus 로고    scopus 로고
    • The role of the Amadori product in the complications of diabetes
    • DOI 10.1196/annals.1433.052, The Maillard Reaction Recent Advances in Food and Biomedical Sciences
    • Monnier, V. M., Sell, D. R., Dai, Z., Nemet, I., Collard, F., and, Zhang, J., (2008) The role of the Amadori product in complications of diabetes. Ann. N. Y. Acad. Sci. 1126, 81-88. (Pubitemid 351589314)
    • (2008) Annals of the New York Academy of Sciences , vol.1126 , pp. 81-88
    • Monnier, V.M.1    Sell, D.R.2    Dai, Z.3    Nemet, I.4    Collard, F.5    Zhang, J.6
  • 10
    • 79951973231 scopus 로고    scopus 로고
    • Advanced glycation end-products damaged IgG, a target for circulating autoantibodies in patients with type 1 diabetes mellitus
    • Rasheed, Z., Kumar, L., Abbas, S., Prasad, I., Ansari, N. A., and, Ahmad, R., (2009) Advanced glycation end-products damaged IgG, a target for circulating autoantibodies in patients with type 1 diabetes mellitus. Open Glycosci. 2, 1-8.
    • (2009) Open Glycosci. , vol.2 , pp. 1-8
    • Rasheed, Z.1    Kumar, L.2    Abbas, S.3    Prasad, I.4    Ansari, N.A.5    Ahmad, R.6
  • 11
    • 13844255024 scopus 로고    scopus 로고
    • Nuclear proteasome activation and degradation of carboxymethylated histones in human keratinocytes following glyoxal treatment
    • DOI 10.1016/j.freeradbiomed.2004.11.030
    • Cervantes-Laurean, D., Roberts, M. I., and, Jacobson, E. L., (2005) Nuclear proteasome activation and degradation of carboxymethylated histones in human keratinocytes following glyoxal treatment. Free Radic. Biol. Med. 38, 786-795. (Pubitemid 40249749)
    • (2005) Free Radical Biology and Medicine , vol.38 , Issue.6 , pp. 786-795
    • Cervantes-Laurean, D.1    Roberts, M.J.2    Jacobson, E.L.3    Jacobson, M.K.4
  • 12
    • 37749041309 scopus 로고    scopus 로고
    • A study in glycation of a therapeutic recombinant humanized monoclonal antibody: Where it is, how it got there, and how it affect charge-based behaviour
    • Quan, C., Alcala, E., Petkovska, I., Matthews, D., Canova-Davis, E., Taticek, R., and, Ma, S., (2008) A study in glycation of a therapeutic recombinant humanized monoclonal antibody: where it is, how it got there, and how it affect charge-based behaviour. Anal. Biochem. 373, 179-191.
    • (2008) Anal. Biochem. , vol.373 , pp. 179-191
    • Quan, C.1    Alcala, E.2    Petkovska, I.3    Matthews, D.4    Canova-Davis, E.5    Taticek, R.6    Ma, S.7
  • 13
    • 65749111481 scopus 로고    scopus 로고
    • Preferential recognition of Amadori-rich lysine residues by serum antibodies in diabetes mellitus: Role of protein glycation in the disease process
    • Ansari, N. A., Moinuddin, Alam, K., and, Ali, A., (2009) Preferential recognition of Amadori-rich lysine residues by serum antibodies in diabetes mellitus: role of protein glycation in the disease process. Human Immunol. 70, 417-424.
    • (2009) Human Immunol. , vol.70 , pp. 417-424
    • Ansari, N.A.1    Moinuddin Alam, K.2    Ali, A.3
  • 14
    • 0022931516 scopus 로고
    • Identification of N(ε)-carboxymethyllysine as a degradation product of fructoselysine in glycated protein
    • Ahmed, M. U., Thorpe, S. R., and, Baynes, J. W., (1986) Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J. Biol. Chem. 261, 4889-4894. (Pubitemid 17204276)
    • (1986) Journal of Biological Chemistry , vol.261 , Issue.11 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 15
    • 0020655989 scopus 로고
    • Fructosamine: A new approach to the estimation of serum glycosylprotein
    • Johnson, R., Metcalf, P. A., and, Baker, J. R., (1982) Fructosamine: a new approach to the estimation of serum glycosylprotein. Clin. Chim. Acta 127, 87-95.
    • (1982) Clin. Chim. Acta , vol.127 , pp. 87-95
    • Johnson, R.1    Metcalf, P.A.2    Baker, J.R.3
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, K. U., (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, K.U.1
  • 17
    • 0000544299 scopus 로고
    • A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels
    • Oakley, B. R., Kirsh, D. R., and, Morris, N. R., (1980) A simplified ultrasensitive silver stain for detecting proteins in polyacrylamide gels. Anal. Biochem. 105, 361-363.
    • (1980) Anal. Biochem. , vol.105 , pp. 361-363
    • Oakley, B.R.1    Kirsh, D.R.2    Morris, N.R.3
  • 18
    • 11844292005 scopus 로고    scopus 로고
    • Importance of measuring products of non-enzymatic glycation of proteins
    • DOI 10.1016/j.clinbiochem.2004.09.007, PII S0009912004002450
    • Lapolla, A., Traldi, P., and, Fedele, D., (2005) Importance of measuring products of nonenzymatic glycation of proteins. Clin. Biochem. 38, 103-115. (Pubitemid 40092452)
    • (2005) Clinical Biochemistry , vol.38 , Issue.2 , pp. 103-115
    • Lapolla, A.1    Traldi, P.2    Fedele, D.3
  • 19
    • 0036194672 scopus 로고    scopus 로고
    • Nonenzymatic glycation of histones in vitro and in vivo
    • DOI 10.1002/jcb.10103
    • Talasz, H., Wasserer, S., and, Puschendorf, B., (2002) Nonenzymatic glycation of histones in vitro and in vivo. J. Cell. Biochem. 85, 24-34. (Pubitemid 34204066)
    • (2002) Journal of Cellular Biochemistry , vol.85 , Issue.1 , pp. 24-34
    • Talasz, H.1    Wasserer, S.2    Puschendorf, B.3
  • 20
    • 73049144001 scopus 로고
    • The far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation
    • Rosenheck, K., and, Doty, P., (1961) The far ultraviolet absorption spectra of polypeptide and protein solutions and their dependence on conformation. Proc. Natl. Acad. Sci. USA 47, 1775-1785.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1775-1785
    • Rosenheck, K.1    Doty, P.2
  • 21
    • 14644397841 scopus 로고    scopus 로고
    • Characterization of advanced glycation end products for biochemical studies: Side chain modifications and fluorescence characteristics
    • DOI 10.1016/j.ab.2004.12.003
    • Schmitt, A., Schmitt, J., Munch, G., and, Gasic-Milencovic, J., (2005) Characterization of advanced glycation end products for biochemical studies: side chain modifications and fluorescence characteristics. Anal. Biochem. 338, 201-215. (Pubitemid 40312584)
    • (2005) Analytical Biochemistry , vol.338 , Issue.2 , pp. 201-215
    • Schmitt, A.1    Schmitt, J.2    Munch, G.3    Gasic-Milencovic, J.4
  • 22
    • 0023214514 scopus 로고
    • Progressive changes in lens crystallin glycation and high-molecular- weight aggregate formation leading to cataract development in streptozotocin-diabetic rats
    • DOI 10.1016/S0014-4835(87)80011-8
    • Perry, R. E., Swamy, M. S., and, Abraham, E. C., (1987) Progressive changes in lens crystallin glycation and high-molecular-weight aggregate formation leading to cataract development in streptozotocin-diabetic rats. Exp. Eye Res. 44, 269-282. (Pubitemid 17060572)
    • (1987) Experimental Eye Research , vol.44 , Issue.2 , pp. 269-282
    • Perry, R.E.1    Swamy, M.S.2    Abraham, E.C.3
  • 24
    • 0035538939 scopus 로고    scopus 로고
    • Novel absorption and fluorescence characteristics of L-lysine
    • Homchaudhuri, L., and, Swaminathan, R., (2001) Novel absorption and fluorescence characteristics of L-lysine. Chem. Lett. 30, 844-845.
    • (2001) Chem. Lett. , vol.30 , pp. 844-845
    • Homchaudhuri, L.1    Swaminathan, R.2
  • 25
    • 2342632556 scopus 로고    scopus 로고
    • Near ultraviolet absorption arising from lysine residues in close proximity
    • Homchaudhuri, L., and, Swaminathan, R., (2004) Near ultraviolet absorption arising from lysine residues in close proximity. Bull. Chem. Soc. Jpn. 77, 765-769.
    • (2004) Bull. Chem. Soc. Jpn. , vol.77 , pp. 765-769
    • Homchaudhuri, L.1    Swaminathan, R.2
  • 26
    • 0033512695 scopus 로고    scopus 로고
    • Amadori albumin in type 1 diabetic patients: Correlation with markers of endothelial function, association with diabetic nephropathy, and localization in retinal capillaries
    • Schalkwijk, C. G., Ligtvoet, N., Twaafhoven, H., Jager, A., Blaauwgeers, H. G. T., Schlingemann, R. O., Tarnow, L., Parving, H-H., Stehouwer, C. D. A., and, Hinsbergh, V. W. M., (1999) Amadori albumin in type 1 diabetic patients: correlation with markers of endothelial function, association with diabetic nephropathy and localization in retinal capillaries. Diabetes 48, 2446-2453. (Pubitemid 30395438)
    • (1999) Diabetes , vol.48 , Issue.12 , pp. 2446-2453
    • Schalkwijk, C.G.1    Ligtvoet, N.2    Twaalfhoven, H.3    Jager, A.4    Blaauwgeers, H.G.T.5    Schlingemann, R.O.6    Tarnow, L.7    Parving, H.-H.8    Stehouwer, C.D.A.9    Van Hinsbergh, V.W.M.10


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