메뉴 건너뛰기




Volumn 70, Issue 6, 2009, Pages 417-424

Preferential recognition of Amadori-rich lysine residues by serum antibodies in diabetes mellitus: Role of protein glycation in the disease process

Author keywords

Amadori products; Diabetes mellitus; Fructosamine; Glycation; Poly L lysine

Indexed keywords

5 HYDROXYMETHYLFURFURAL; ANTIBODY; FRUCTOSAMINE; POLYLYSINE;

EID: 65749111481     PISSN: 01988859     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.humimm.2009.03.015     Document Type: Article
Times cited : (58)

References (44)
  • 1
    • 23644456800 scopus 로고    scopus 로고
    • Diabetes mellitus
    • Kasper D.L., Braunwald E., Fauci A.S., Hauser S.L., Longo D.L., and Jameson J.L. (Eds), McGraw-Hill, New York
    • Powers A.C. Diabetes mellitus. In: Kasper D.L., Braunwald E., Fauci A.S., Hauser S.L., Longo D.L., and Jameson J.L. (Eds). Harrison's Principles of Internal Medicine (2005), McGraw-Hill, New York
    • (2005) Harrison's Principles of Internal Medicine
    • Powers, A.C.1
  • 2
    • 0022251563 scopus 로고
    • Glycation of amino groups in protein
    • Watkins N.G., Thorpe S.R., and Baynes J.W. Glycation of amino groups in protein. J Biol Chem 260 (1985) 10629-10636
    • (1985) J Biol Chem , vol.260 , pp. 10629-10636
    • Watkins, N.G.1    Thorpe, S.R.2    Baynes, J.W.3
  • 4
    • 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. Diabet Res Clin Prac 67 (2005) 3-21
    • (2005) Diabet Res Clin Prac , vol.67 , pp. 3-21
    • Ahmed, N.1
  • 6
    • 0022931516 scopus 로고
    • Identification of N epsilon-carboxymethyl lysine as a degradation product of fructoselysine in glycated protein
    • Ahmed M.U., Thorpe S.R., and Baynes J.W. Identification of N epsilon-carboxymethyl lysine as a degradation product of fructoselysine in glycated protein. J Biol Chem 261 (1986) 4889-4894
    • (1986) J Biol Chem , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 7
    • 0028287398 scopus 로고
    • Glucose oxidation and low-density lipoprotein-induced macrophage ceroid accumulation
    • Hunt J.V., Bottoms M.A., Clare K., Skamarauskas J.T., and Mitchinson M.J. Glucose oxidation and low-density lipoprotein-induced macrophage ceroid accumulation. Biochem J 300 (1994) 243-249
    • (1994) Biochem J , vol.300 , pp. 243-249
    • Hunt, J.V.1    Bottoms, M.A.2    Clare, K.3    Skamarauskas, J.T.4    Mitchinson, M.J.5
  • 8
    • 0023780475 scopus 로고
    • Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-lH-imidazole
    • Njoroge F.G., Fernandes A.A., and Monnier V.M. Mechanism of formation of the putative advanced glycosylation end product and protein cross-link 2-(2-furoyl)-4(5)-(2-furanyl)-lH-imidazole. J Biol Chem 263 (1988) 10646-10652
    • (1988) J Biol Chem , vol.263 , pp. 10646-10652
    • Njoroge, F.G.1    Fernandes, A.A.2    Monnier, V.M.3
  • 9
    • 0020655989 scopus 로고
    • Fructosamine: a new approach to the estimation of serum glycosylprotein
    • Johnson R., Metcalf P.A., and Baker J.R. Fructosamine: a new approach to the estimation of serum glycosylprotein. Clin Chim Acta 127 (1982) 87-95
    • (1982) Clin Chim Acta , vol.127 , pp. 87-95
    • Johnson, R.1    Metcalf, P.A.2    Baker, J.R.3
  • 10
  • 11
    • 0017053199 scopus 로고
    • In vitro synthesis of hemoglobin A1C
    • Fluckiger R., and Winterhalter K.H. In vitro synthesis of hemoglobin A1C. FEBS Lett 71 (1976) 356-360
    • (1976) FEBS Lett , vol.71 , pp. 356-360
    • Fluckiger, R.1    Winterhalter, K.H.2
  • 14
    • 24344446907 scopus 로고    scopus 로고
    • Immunological studies on peroxynitrite modified human DNA
    • Dixit K., Moinuddin, and Ali A. Immunological studies on peroxynitrite modified human DNA. Life Sci 77 (2005) 2626-2642
    • (2005) Life Sci , vol.77 , pp. 2626-2642
    • Dixit, K.1    Moinuddin2    Ali, A.3
  • 15
  • 16
    • 16244375903 scopus 로고    scopus 로고
    • Acquired antigenicity of DNA after modification with peroxynitrite
    • Habib S., Moinuddin, and Ali R. Acquired antigenicity of DNA after modification with peroxynitrite. Int J Biol Macromol 35 (2005) 221-225
    • (2005) Int J Biol Macromol , vol.35 , pp. 221-225
    • Habib, S.1    Moinuddin2    Ali, R.3
  • 17
    • 1242314348 scopus 로고    scopus 로고
    • Role of nitric oxide modified DNA in the etiopathogenesis of systemic lupus erythematosus
    • Dixit K., and Ali R. Role of nitric oxide modified DNA in the etiopathogenesis of systemic lupus erythematosus. Lupus 13 (2004) 95-100
    • (2004) Lupus , vol.13 , pp. 95-100
    • Dixit, K.1    Ali, R.2
  • 18
    • 0028979597 scopus 로고
    • Nepsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (age) antigen in tissue proteins
    • Reddy S., Bichler J., Wells-Knecht K.J., Thorpe S.R., and Baynes J.W. Nepsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (age) antigen in tissue proteins. Biochemistry 43 (1995) 10872-10878
    • (1995) Biochemistry , vol.43 , pp. 10872-10878
    • Reddy, S.1    Bichler, J.2    Wells-Knecht, K.J.3    Thorpe, S.R.4    Baynes, J.W.5
  • 19
    • 0020520283 scopus 로고
    • A novel method for generating region-specific monoclonal antibodies to modified proteins
    • Curtiss L.K., and Witztum J.L. A novel method for generating region-specific monoclonal antibodies to modified proteins. J Clin Invest 72 (1983) 1427-1438
    • (1983) J Clin Invest , vol.72 , pp. 1427-1438
    • Curtiss, L.K.1    Witztum, J.L.2
  • 20
    • 11844292005 scopus 로고    scopus 로고
    • Importance of measuring products of non-enzymatic glycation of proteins
    • Lapolla A., Traldi P., and Fedele D. Importance of measuring products of non-enzymatic glycation of proteins. Clin Biochem 38 (2005) 103-115
    • (2005) Clin Biochem , vol.38 , pp. 103-115
    • Lapolla, A.1    Traldi, P.2    Fedele, D.3
  • 22
    • 0023664866 scopus 로고
    • Phytic acid: A natural antioxidant
    • Graf E., Empson K.L., and Eaton J.W. Phytic acid: A natural antioxidant. J Biol Chem 262 (1987) 11647-11650
    • (1987) J Biol Chem , vol.262 , pp. 11647-11650
    • Graf, E.1    Empson, K.L.2    Eaton, J.W.3
  • 23
    • 0019843239 scopus 로고
    • The standardization of thiobarbituric acid assay for nonenzymatic glucosylation of human serum albumin
    • Ney K.A., Colley K.J., and Pizzo S.V. The standardization of thiobarbituric acid assay for nonenzymatic glucosylation of human serum albumin. Anal Biochem 118 (1981) 294
    • (1981) Anal Biochem , vol.118 , pp. 294
    • Ney, K.A.1    Colley, K.J.2    Pizzo, S.V.3
  • 24
    • 0021213557 scopus 로고
    • Nonenzymatic glucosylation of human serum albumin and its influence on binding capacity of sulfonylureas
    • Tsuchiya S., Sakurai T., and Sekiguchi S. Nonenzymatic glucosylation of human serum albumin and its influence on binding capacity of sulfonylureas. Biochem Pharmacol 33 (1984) 2967-2971
    • (1984) Biochem Pharmacol , vol.33 , pp. 2967-2971
    • Tsuchiya, S.1    Sakurai, T.2    Sekiguchi, S.3
  • 25
    • 0035538939 scopus 로고    scopus 로고
    • Novel absorption and fluorescence characteristics of L-lysine
    • Homchaudhuri L., and Swaminathan R. Novel absorption and fluorescence characteristics of L-lysine. Chem Lett 30 (2001) 844-845
    • (2001) Chem Lett , vol.30 , pp. 844-845
    • Homchaudhuri, L.1    Swaminathan, R.2
  • 26
    • 2342632556 scopus 로고    scopus 로고
    • Near ultraviolet absorption arising from lysine residues in close proximity
    • Homchaudhuri L., and Swaminathan R. Near ultraviolet absorption arising from lysine residues in close proximity. Bull Chem Soc Jpn 77 (2004) 765-769
    • (2004) Bull Chem Soc Jpn , vol.77 , pp. 765-769
    • Homchaudhuri, L.1    Swaminathan, R.2
  • 27
    • 33750741900 scopus 로고    scopus 로고
    • FT-IR spectra of solid poly-L-lysine in the stretching NH mode range
    • Rozenberg M., and Shoham G. FT-IR spectra of solid poly-L-lysine in the stretching NH mode range. Biophys Chem 125 (2007) 166-171
    • (2007) Biophys Chem , vol.125 , pp. 166-171
    • Rozenberg, M.1    Shoham, G.2
  • 28
    • 0346363390 scopus 로고    scopus 로고
    • Monitoring carbonyl-amine reaction between pyruvic acid and α-amino alcohols by FTIR spectroscopy-a possible route to Amadori products
    • Wnorowsky A., and Yaylayan V.A. Monitoring carbonyl-amine reaction between pyruvic acid and α-amino alcohols by FTIR spectroscopy-a possible route to Amadori products. J Agric Food Chem 51 (2003) 6537-6543
    • (2003) J Agric Food Chem , vol.51 , pp. 6537-6543
    • Wnorowsky, A.1    Yaylayan, V.A.2
  • 29
    • 34447512796 scopus 로고    scopus 로고
    • Vinylogous Amadori rearrangement: Implications in food and biological systems
    • Yaylayan V.A., and Locas C.P. Vinylogous Amadori rearrangement: Implications in food and biological systems. Mol Nutr Food Res 51 (2007) 437-444
    • (2007) Mol Nutr Food Res , vol.51 , pp. 437-444
    • Yaylayan, V.A.1    Locas, C.P.2
  • 30
    • 0001785082 scopus 로고
    • Infrared spectra of biological macromolecules and related systems
    • Timasheff S.N., and Fasman G.D. (Eds), Marcel Dekker, New York
    • Susi H. Infrared spectra of biological macromolecules and related systems. In: Timasheff S.N., and Fasman G.D. (Eds). Structure and Stability of Biological Macromolecules (1969), Marcel Dekker, New York
    • (1969) Structure and Stability of Biological Macromolecules
    • Susi, H.1
  • 33
    • 20744450085 scopus 로고    scopus 로고
    • A correlation between the proton stretching vibration red shift and the hydrogen bond length in polycrystalline amino acids and peptides
    • Rozenberg M., Shoham G., Reva I., and Fausto R. A correlation between the proton stretching vibration red shift and the hydrogen bond length in polycrystalline amino acids and peptides. Phys Chem Chem Phys 7 (2005) 2376-2383
    • (2005) Phys Chem Chem Phys , vol.7 , pp. 2376-2383
    • Rozenberg, M.1    Shoham, G.2    Reva, I.3    Fausto, R.4
  • 36
    • 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., Twaalfhoven H., Jager A., Blaauwgeers H.G.T., Schlingemann R.O., et al. Amadori albumin in type 1 diabetic patients: Correlation with markers of endothelial function, association with diabetic nephropathy and localization in retinal capillaries. Diabetes 48 (1999) 2446-2453
    • (1999) Diabetes , vol.48 , 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
  • 37
    • 14644435071 scopus 로고    scopus 로고
    • Identification of Amadori-modified plasma proteins in type 2 diabetes and the effect of short-term intensive insulin treatment
    • Jaleel A., Juhasz P., Halvatsiotis P., Martin S., Williamson B., and Nair K.S. Identification of Amadori-modified plasma proteins in type 2 diabetes and the effect of short-term intensive insulin treatment. Diabetes Care 28 (2005) 645-652
    • (2005) Diabetes Care , vol.28 , pp. 645-652
    • Jaleel, A.1    Juhasz, P.2    Halvatsiotis, P.3    Martin, S.4    Williamson, B.5    Nair, K.S.6
  • 38
    • 0028800370 scopus 로고
    • Immunological detection of glycated proteins in normal and streptozotocin-induced diabetic rats using anti hexitol-lysine IgG
    • Myint T., Hoshi S., Ookawara T., Miyazawa N., Suzuki K., and Taniguchi N. Immunological detection of glycated proteins in normal and streptozotocin-induced diabetic rats using anti hexitol-lysine IgG. Biochim Biophys Acta 271 (1995) 73-79
    • (1995) Biochim Biophys Acta , vol.271 , pp. 73-79
    • Myint, T.1    Hoshi, S.2    Ookawara, T.3    Miyazawa, N.4    Suzuki, K.5    Taniguchi, N.6
  • 39
    • 4143111353 scopus 로고    scopus 로고
    • Non-enzymatic glycosylation of immuno-globulins in diabetic nephropathy
    • Kalia K., Sharma S., and Mistry K. Non-enzymatic glycosylation of immuno-globulins in diabetic nephropathy. Clin Chim Acta 347 (2004) 169-176
    • (2004) Clin Chim Acta , vol.347 , pp. 169-176
    • Kalia, K.1    Sharma, S.2    Mistry, K.3
  • 40
    • 56149110128 scopus 로고    scopus 로고
    • Amelioration of diabetes-associated abnormalities in the vitreous fluid by an inhibitor of albumin glycation
    • Cohen M.P., Hud E., Wu V.Y., and Shearman C.W. Amelioration of diabetes-associated abnormalities in the vitreous fluid by an inhibitor of albumin glycation. Invest Ophthalmol Vis Sci 49 (2008) 5089-5093
    • (2008) Invest Ophthalmol Vis Sci , vol.49 , pp. 5089-5093
    • Cohen, M.P.1    Hud, E.2    Wu, V.Y.3    Shearman, C.W.4
  • 42
    • 0030483937 scopus 로고    scopus 로고
    • Localization of glycated proteins in the glomeruli of patients with diabetic nephropathy
    • Sakai H., Jinde K., Suzuki D., Yagame M., and Nomoto Y. Localization of glycated proteins in the glomeruli of patients with diabetic nephropathy. Nephrol Dial Transplant 11 (1996) 66-71
    • (1996) Nephrol Dial Transplant , vol.11 , pp. 66-71
    • Sakai, H.1    Jinde, K.2    Suzuki, D.3    Yagame, M.4    Nomoto, Y.5
  • 43
    • 0344382052 scopus 로고    scopus 로고
    • Anti-glycated albumin therapy ameliorates early retinal microvascular pathology in db/db mice
    • Clements Jr. R.S., Robison Jr. W.G., and Cohen M.P. Anti-glycated albumin therapy ameliorates early retinal microvascular pathology in db/db mice. J Diabet Complic 12 (1998) 28-33
    • (1998) J Diabet Complic , vol.12 , pp. 28-33
    • Clements Jr., R.S.1    Robison Jr., W.G.2    Cohen, M.P.3
  • 44
    • 0023473996 scopus 로고
    • Fructosamine: Structure, analysis and clinical usefulness
    • Armbruster D.A. Fructosamine: Structure, analysis and clinical usefulness. Clin Chem 33 (1987) 2153-2163
    • (1987) Clin Chem , vol.33 , pp. 2153-2163
    • Armbruster, D.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.