메뉴 건너뛰기




Volumn 19, Issue 4, 2008, Pages 378-384

Glycation as an atherogenic modification of LDL

Author keywords

Cardiovascular disease; Glycation of LDL; Oxidation of LDL; Small dense LDL

Indexed keywords

ADVANCED GLYCATION END PRODUCT; AMINOGUANIDINE; GLUCOSE; HYDRALAZINE; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; KAEMPFEROL; LOW DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN RECEPTOR; LYSINE; MORIN; MYRICETIN; QUERCETIN; RUTOSIDE; SCAVENGER RECEPTOR; LOW DENSITY LIPOPROTEIN CHOLESTEROL;

EID: 53149109790     PISSN: 09579672     EISSN: None     Source Type: Journal    
DOI: 10.1097/MOL.0b013e328306a057     Document Type: Review
Times cited : (82)

References (85)
  • 1
    • 0019796775 scopus 로고
    • Reaction of monosaccharides with proteins: Possible evolutionary significance
    • Bunn HF, Higgins PJ. Reaction of monosaccharides with proteins: possible evolutionary significance. Science 1981; 213:222-224.
    • (1981) Science , vol.213 , pp. 222-224
    • Bunn, H.F.1    Higgins, P.J.2
  • 2
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • Thornalley PJ, Langborg A, Minhas HS. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem J 1999; 344:109-116.
    • (1999) Biochem J , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 3
    • 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 PA, Khalifah RG, Thibaudeau C, et al. 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
  • 4
    • 33644832991 scopus 로고    scopus 로고
    • Hydrazine compounds inhibit glycation of low-density lipoproteins and prevent the in vitro formation of model foam cells from glycolaldehyde-modified low-density lipoproteins
    • Brown BE, Mahroof FM, Cook NL, et al. Hydrazine compounds inhibit glycation of low-density lipoproteins and prevent the in vitro formation of model foam cells from glycolaldehyde-modified low-density lipoproteins. Diabetologia 2006; 49:775-783.
    • (2006) Diabetologia , vol.49 , pp. 775-783
    • Brown, B.E.1    Mahroof, F.M.2    Cook, N.L.3
  • 5
    • 4043058031 scopus 로고    scopus 로고
    • Advanced glycation end products and vascular inflammation: Implications for accelerated atherosclerosis in diabetes
    • Basta G, Schmidt AM, De Caterina R. Advanced glycation end products and vascular inflammation: implications for accelerated atherosclerosis in diabetes. Cardiovasc Res 2004; 63:582-592.
    • (2004) Cardiovasc Res , vol.63 , pp. 582-592
    • Basta, G.1    Schmidt, A.M.2    De Caterina, R.3
  • 6
    • 33646744719 scopus 로고    scopus 로고
    • Elimination of damaged proteins during differentiation of embryonic stem cells
    • Hernebring M, Brolen G, Aguilaniu H, et al. Elimination of damaged proteins during differentiation of embryonic stem cells. Proc Natl Acad Sci U S A 2006; 103:7700-7705.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7700-7705
    • Hernebring, M.1    Brolen, G.2    Aguilaniu, H.3
  • 7
    • 0026786580 scopus 로고
    • The assay of methylglyoxal in biological systems by derivatization with 1, 2-diamino-4,5-dimethoxybenzene
    • McLellan AC, Phillips SA, Thornalley PJ. The assay of methylglyoxal in biological systems by derivatization with 1, 2-diamino-4,5-dimethoxybenzene. Anal Biochem 1992; 206:17-23.
    • (1992) Anal Biochem , vol.206 , pp. 17-23
    • McLellan, A.C.1    Phillips, S.A.2    Thornalley, P.J.3
  • 8
    • 0038659947 scopus 로고    scopus 로고
    • Fetal or neonatal low-glycotoxin environment prevents autoimmune diabetes in NOD mice
    • Peppa M, He C, Hattori M, et al. Fetal or neonatal low-glycotoxin environment prevents autoimmune diabetes in NOD mice. Diabetes 2003; 52:1441-1448.
    • (2003) Diabetes , vol.52 , pp. 1441-1448
    • Peppa, M.1    He, C.2    Hattori, M.3
  • 9
    • 0017105005 scopus 로고
    • Hemoglobin AIcas an indicator of the degree of glucose intolerance in diabetes
    • Koenig RJ, Peterson CM, Kilo C, et al. Hemoglobin AIcas an indicator of the degree of glucose intolerance in diabetes. Diabetes 1976; 25:230-232.
    • (1976) Diabetes , vol.25 , pp. 230-232
    • Koenig, R.J.1    Peterson, C.M.2    Kilo, C.3
  • 10
    • 0019251060 scopus 로고
    • Increased glycosylation of serum albumin in diabetes mellitus
    • Dolhofer R, Wieland OH. Increased glycosylation of serum albumin in diabetes mellitus. Diabetes 1980; 29:417-422.
    • (1980) Diabetes , vol.29 , pp. 417-422
    • Dolhofer, R.1    Wieland, O.H.2
  • 11
    • 34347215814 scopus 로고    scopus 로고
    • Increased serum glycated albumin level is associated with the presence and severity of coronary artery disease in type 2 diabetic patients
    • Pu LJ, Lu L, Shen WF, et al. Increased serum glycated albumin level is associated with the presence and severity of coronary artery disease in type 2 diabetic patients. Circ J 2007; 71:1067-1073.
    • (2007) Circ J , vol.71 , pp. 1067-1073
    • Pu, L.J.1    Lu, L.2    Shen, W.F.3
  • 13
    • 0026681734 scopus 로고
    • Nonenzymatic glycation of apolipo-protein B in the sera of diabetic and nondiabetic subjects
    • Tames FJ, Mackness MI, Arrol S, et al. Nonenzymatic glycation of apolipo-protein B in the sera of diabetic and nondiabetic subjects. Atherosclerosis 1992; 93:237-244.
    • (1992) Atherosclerosis , vol.93 , pp. 237-244
    • Tames, F.J.1    Mackness, M.I.2    Arrol, S.3
  • 14
    • 0028895643 scopus 로고
    • Nonenzymatic glycation of peripheral nerve proteins in human diabetics
    • Ryle C, Donaghy M. Nonenzymatic glycation of peripheral nerve proteins in human diabetics. J Neurol Sci 1995; 129:62-68.
    • (1995) J Neurol Sci , vol.129 , pp. 62-68
    • Ryle, C.1    Donaghy, M.2
  • 15
    • 0027160460 scopus 로고
    • Accumulation of Maillard reaction products in skin collagen in diabetes and aging
    • Dyer DG, Dunn JA, Thorpe SR, et al. Accumulation of Maillard reaction products in skin collagen in diabetes and aging. J Clin Invest 1993; 91:2463-2469.
    • (1993) J Clin Invest , vol.91 , pp. 2463-2469
    • Dyer, D.G.1    Dunn, J.A.2    Thorpe, S.R.3
  • 16
    • 0025939381 scopus 로고
    • Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus
    • Lyons TJ, Bailie KE, Dyer DG, et al. Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus. J Clin Invest 1991; 87:1910-1915.
    • (1991) J Clin Invest , vol.87 , pp. 1910-1915
    • Lyons, T.J.1    Bailie, K.E.2    Dyer, D.G.3
  • 17
    • 0041328599 scopus 로고    scopus 로고
    • Nonenzymatic glycation in corneas from normal and diabetic donors and its effects on epithelial cell attachment in vitro
    • McDermott AM, Xiao TL, Kern TS, Murphy CJ. Nonenzymatic glycation in corneas from normal and diabetic donors and its effects on epithelial cell attachment in vitro. Optometry 2003; 74:443-452.
    • (2003) Optometry , vol.74 , pp. 443-452
    • McDermott, A.M.1    Xiao, T.L.2    Kern, T.S.3    Murphy, C.J.4
  • 18
    • 0033953072 scopus 로고    scopus 로고
    • Advanced glycation end products in diabetic corneas
    • Kaji Y, Usui T, Oshika T, et al. Advanced glycation end products in diabetic corneas. Invest Ophthalmol Vis Sci 2000; 41:362-368.
    • (2000) Invest Ophthalmol Vis Sci , vol.41 , pp. 362-368
    • Kaji, Y.1    Usui, T.2    Oshika, T.3
  • 19
    • 0019475899 scopus 로고
    • Nonenzymatic browning in vivo: Possible process for aging of long-lived proteins
    • Monnier VM, Cerami A. Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science 1981; 211:491-493.
    • (1981) Science , vol.211 , pp. 491-493
    • Monnier, V.M.1    Cerami, A.2
  • 20
    • 0021683315 scopus 로고
    • Nonenzymatic glycation of human lens crystalline. Effect of aging and diabetes mellitus
    • Garlick RL, Mazer JS, Chylack LT Jr, et al. Nonenzymatic glycation of human lens crystalline. Effect of aging and diabetes mellitus. J Clin Invest 1984; 74:1742-1749.
    • (1984) J Clin Invest , vol.74 , pp. 1742-1749
    • Garlick, R.L.1    Mazer, J.S.2    Chylack Jr, L.T.3
  • 21
    • 0034625075 scopus 로고    scopus 로고
    • Molecular basis for a link between complement and the vascular complications of diabetes
    • Acosta J, Hettinga J, Fluckiger R, et al. Molecular basis for a link between complement and the vascular complications of diabetes. Proc Natl Acad Sci U S A 2000; 97:5450-5455.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5450-5455
    • Acosta, J.1    Hettinga, J.2    Fluckiger, R.3
  • 22
    • 0034283577 scopus 로고    scopus 로고
    • Age-related accumulation of Maillard reaction products in human articular cartilage collagen
    • Verzijl N, DeGroot J, Oldehinkel E, et al. Age-related accumulation of Maillard reaction products in human articular cartilage collagen. Biochem J 2000; 350:381-387.
    • (2000) Biochem J , vol.350 , pp. 381-387
    • Verzijl, N.1    DeGroot, J.2    Oldehinkel, E.3
  • 23
    • 0035847269 scopus 로고    scopus 로고
    • Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease
    • Sasaki N, Toki S, Chowei H, et al. Immunohistochemical distribution of the receptor for advanced glycation end products in neurons and astrocytes in Alzheimer's disease. Brain Res 2001; 888:256-262.
    • (2001) Brain Res , vol.888 , pp. 256-262
    • Sasaki, N.1    Toki, S.2    Chowei, H.3
  • 24
    • 29144482502 scopus 로고    scopus 로고
    • Advanced glycation end product modification of bone proteins and bone remodelling: Hypothesis and preliminary immunohistochemical findings
    • Hein G, Weiss C, Lehmann G, et al. Advanced glycation end product modification of bone proteins and bone remodelling: hypothesis and preliminary immunohistochemical findings. Ann Rheum Dis 2006; 65:101-104.
    • (2006) Ann Rheum Dis , vol.65 , pp. 101-104
    • Hein, G.1    Weiss, C.2    Lehmann, G.3
  • 26
    • 4644344743 scopus 로고    scopus 로고
    • Receptor for advanced glycation end products and age-related macular degeneration
    • Howes KA, Liu Y, Dunaief JL, et al. Receptor for advanced glycation end products and age-related macular degeneration. Invest Ophthalmol Vis Sci 2004; 45:3713-3720.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , pp. 3713-3720
    • Howes, K.A.1    Liu, Y.2    Dunaief, J.L.3
  • 27
    • 39549098128 scopus 로고    scopus 로고
    • RAGE signaling sustains inflammation and promotes tumor development
    • Gebhardt C, Riehl A, Durchdewald M, et al. RAGE signaling sustains inflammation and promotes tumor development. J Exp Med 2008; 205:275-285.
    • (2008) J Exp Med , vol.205 , pp. 275-285
    • Gebhardt, C.1    Riehl, A.2    Durchdewald, M.3
  • 28
    • 43049127240 scopus 로고    scopus 로고
    • V domain of RAGE interacts with AGEs on prostate carcinoma cells
    • Allmen EU, Koch M, Fritz G, Legler DF. V domain of RAGE interacts with AGEs on prostate carcinoma cells. Prostate 2008; 68:748-758.
    • (2008) Prostate , vol.68 , pp. 748-758
    • Allmen, E.U.1    Koch, M.2    Fritz, G.3    Legler, D.F.4
  • 29
    • 0021363569 scopus 로고
    • Glucosylation of low-density lipoproteins to an extent comparable to that seen in diabetes slows their catabolism
    • Steinbrecher UP, Witztum JL. Glucosylation of low-density lipoproteins to an extent comparable to that seen in diabetes slows their catabolism. Diabetes 1984; 33:130-134.
    • (1984) Diabetes , vol.33 , pp. 130-134
    • Steinbrecher, U.P.1    Witztum, J.L.2
  • 30
    • 0041823628 scopus 로고    scopus 로고
    • Glycation and glycoxidation of low-density lipoproteins by glucose and low-molecular mass aldehydes. Formation of modified and oxidized particles
    • Knott HM, Brown BE, Davies MJ, Dean RT. Glycation and glycoxidation of low-density lipoproteins by glucose and low-molecular mass aldehydes. Formation of modified and oxidized particles. Eur J Biochem 2003; 270: 3572-3582.
    • (2003) Eur J Biochem , vol.270 , pp. 3572-3582
    • Knott, H.M.1    Brown, B.E.2    Davies, M.J.3    Dean, R.T.4
  • 31
    • 17444368974 scopus 로고    scopus 로고
    • Glycation of low-density lipoproteins by methylglyoxal and glycolaldehyde gives rise to the in vitro formation of lipid-laden cells
    • Brown BE, Dean RT, Davies MJ. Glycation of low-density lipoproteins by methylglyoxal and glycolaldehyde gives rise to the in vitro formation of lipid-laden cells. Diabetologia 2005; 48:361-369.
    • (2005) Diabetologia , vol.48 , pp. 361-369
    • Brown, B.E.1    Dean, R.T.2    Davies, M.J.3
  • 32
    • 0019408430 scopus 로고
    • Nonenzymatic glycosylation of human serum lipoproteins. Elevated epsilon-lysine glycosylated low density lipoprotein in diabetic patients
    • Schleicher E, Deufel T, Wieland OH. Nonenzymatic glycosylation of human serum lipoproteins. Elevated epsilon-lysine glycosylated low density lipoprotein in diabetic patients. FEBS Lett 1981; 129:1-4.
    • (1981) FEBS Lett , vol.129 , pp. 1-4
    • Schleicher, E.1    Deufel, T.2    Wieland, O.H.3
  • 33
    • 0033033393 scopus 로고    scopus 로고
    • Detection of structural alterations in LDL isolated from type 2 diabetic patients: Application of the fructosamine assay to evaluate the extent of LDL glycation
    • Sanguinetti SM, Schreier LE, Elbert A, et al. Detection of structural alterations in LDL isolated from type 2 diabetic patients: application of the fructosamine assay to evaluate the extent of LDL glycation. Atherosclerosis 1999; 143:213-215.
    • (1999) Atherosclerosis , vol.143 , pp. 213-215
    • Sanguinetti, S.M.1    Schreier, L.E.2    Elbert, A.3
  • 34
    • 84945735124 scopus 로고
    • Glycated LDL concentrations in non-diabetic and diabetic subjects measured with monoclonal antibodies reactive with glycated apolipoprotein B epitopes
    • Cohen MP, Lautenslager G, Shea E. Glycated LDL concentrations in non-diabetic and diabetic subjects measured with monoclonal antibodies reactive with glycated apolipoprotein B epitopes. Eur J Clin Chem Clin Biochem 1993; 31:707-713.
    • (1993) Eur J Clin Chem Clin Biochem , vol.31 , pp. 707-713
    • Cohen, M.P.1    Lautenslager, G.2    Shea, E.3
  • 35
    • 0036155160 scopus 로고    scopus 로고
    • Determinants of glycated LDL levels in nondiabetic and diabetic hyperlipidaemic patients in Kuwait
    • Akanji AO, Abdella N, Mojiminiyi OA. Determinants of glycated LDL levels in nondiabetic and diabetic hyperlipidaemic patients in Kuwait. Clin Chim Acta 2002; 317:171-176.
    • (2002) Clin Chim Acta , vol.317 , pp. 171-176
    • Akanji, A.O.1    Abdella, N.2    Mojiminiyi, O.A.3
  • 36
    • 3042551222 scopus 로고    scopus 로고
    • Increased plasma glycated low-density lipoprotein concentrations in diabetes: A marker of atherogenic risk
    • Cohen MP, Jin Y, Lautenslager GT. Increased plasma glycated low-density lipoprotein concentrations in diabetes: a marker of atherogenic risk. Diabetes Technol Ther 2004; 6:348-356.
    • (2004) Diabetes Technol Ther , vol.6 , pp. 348-356
    • Cohen, M.P.1    Jin, Y.2    Lautenslager, G.T.3
  • 37
    • 0025768213 scopus 로고
    • Correlation between glycated lipoproteins and fructosamine level in serum
    • Kobayashi K, Ogasahara N, Sakoguchi T, et al. Correlation between glycated lipoproteins and fructosamine level in serum. Chem Pharm Bull (Tokyo) 1991; 39:2149-2151.
    • (1991) Chem Pharm Bull (Tokyo) , vol.39 , pp. 2149-2151
    • Kobayashi, K.1    Ogasahara, N.2    Sakoguchi, T.3
  • 38
    • 0037898380 scopus 로고    scopus 로고
    • Diabetic dyslipidaemia: From basic research to clinical practice
    • Taskinen MR. Diabetic dyslipidaemia: from basic research to clinical practice. Diabetologia 2003; 46:733-749.
    • (2003) Diabetologia , vol.46 , pp. 733-749
    • Taskinen, M.R.1
  • 39
    • 2542492541 scopus 로고    scopus 로고
    • Lipids and lipoproteins in patients with type 2 diabetes
    • Krauss RM. Lipids and lipoproteins in patients with type 2 diabetes. Diabetes Care 2004; 27:1496-1504.
    • (2004) Diabetes Care , vol.27 , pp. 1496-1504
    • Krauss, R.M.1
  • 40
    • 0030056807 scopus 로고    scopus 로고
    • Small, dense low density lipoproteins, the insulin resistance syndrome and noninsulin-dependent diabetes
    • Austin MA, Edwards KL. Small, dense low density lipoproteins, the insulin resistance syndrome and noninsulin-dependent diabetes. Curr Opin Lipidol 1996; 7:167-171.
    • (1996) Curr Opin Lipidol , vol.7 , pp. 167-171
    • Austin, M.A.1    Edwards, K.L.2
  • 41
    • 0027502421 scopus 로고
    • Susceptibility of small, dense, low-density lipoproteins to oxidative modification in subjects with the atherogenic lipoprotein phenotype, pattern B
    • Chait A, Brazg R, Tribble D, Krauss R. Susceptibility of small, dense, low-density lipoproteins to oxidative modification in subjects with the atherogenic lipoprotein phenotype, pattern B. Am J Med 1993; 94:350-356.
    • (1993) Am J Med , vol.94 , pp. 350-356
    • Chait, A.1    Brazg, R.2    Tribble, D.3    Krauss, R.4
  • 42
    • 57649213676 scopus 로고    scopus 로고
    • Glycation of LDL in nonpeople: Small dense LDL is preferentially glycated both In vivo and in vitro
    • This is the first report that small dense LDL is preferentially glycated in people without diabetes and that it has greater susceptibility to undergo glycation when compared with other LDL subclasses in vitro, in press, doi:10.1016/j.atherosclerosis.2008. 04.036
    • Younis N, Charlton-Menys V, Sharma R, et al. Glycation of LDL in nonpeople: small dense LDL is preferentially glycated both In vivo and in vitro. Atherosclerosis (in press) (2008), doi:10.1016/j.atherosclerosis.2008. 04.036. This is the first report that small dense LDL is preferentially glycated in people without diabetes and that it has greater susceptibility to undergo glycation when compared with other LDL subclasses in vitro.
    • (2008) Atherosclerosis
    • Younis, N.1    Charlton-Menys, V.2    Sharma, R.3
  • 43
    • 0031555853 scopus 로고    scopus 로고
    • Acid-stable fluorescent advanced glycation end products: Vesperlysines A, B, and C are formed as crosslinked products in the Maillard reaction between lysine or proteins with glucose
    • Nakamura K, Nakazawa Y, Ienaga K. Acid-stable fluorescent advanced glycation end products: vesperlysines A, B, and C are formed as crosslinked products in the Maillard reaction between lysine or proteins with glucose. Biochem Biophys Res Commun 1997; 232:227-230.
    • (1997) Biochem Biophys Res Commun , vol.232 , pp. 227-230
    • Nakamura, K.1    Nakazawa, Y.2    Ienaga, K.3
  • 44
    • 0025945553 scopus 로고
    • Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo
    • Dyer DG, Blackledge JA, Thorpe SR, Baynes JW. Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo. J Biol Chem 1991; 266:11654-11660.
    • (1991) J Biol Chem , vol.266 , pp. 11654-11660
    • Dyer, D.G.1    Blackledge, J.A.2    Thorpe, S.R.3    Baynes, J.W.4
  • 45
    • 0014358088 scopus 로고
    • Electrophoretic separation of plasma lipoproteins in agarose gel
    • Noble RP. Electrophoretic separation of plasma lipoproteins in agarose gel. J Lipid Res 1968; 9:693-700.
    • (1968) J Lipid Res , vol.9 , pp. 693-700
    • Noble, R.P.1
  • 46
    • 0033758785 scopus 로고    scopus 로고
    • Why is glycated LDL more sensitive to oxidation than native LDL? A comparative study
    • Sobal G, Menzel J, Sinzinger H. Why is glycated LDL more sensitive to oxidation than native LDL? A comparative study. Prostaglandins Leukot Essent Fatty Acids 2000; 63:177-186.
    • (2000) Prostaglandins Leukot Essent Fatty Acids , vol.63 , pp. 177-186
    • Sobal, G.1    Menzel, J.2    Sinzinger, H.3
  • 47
    • 33847222132 scopus 로고    scopus 로고
    • Carnosine and its constituents inhibit glycation of low-density lipoproteins that promotes foam cell formation in vitro
    • Rashid I, van Reyk DM, Davies MJ. Carnosine and its constituents inhibit glycation of low-density lipoproteins that promotes foam cell formation in vitro. FEBS Lett 2007; 581:1067-1070.
    • (2007) FEBS Lett , vol.581 , pp. 1067-1070
    • Rashid, I.1    van Reyk, D.M.2    Davies, M.J.3
  • 48
    • 0013889689 scopus 로고
    • Determination of free amino groups in proteins by trinitrobenzenesulfonic acid
    • Habeeb AF. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal Biochem 1966; 14:328-336.
    • (1966) Anal Biochem , vol.14 , pp. 328-336
    • Habeeb, A.F.1
  • 49
    • 0025038731 scopus 로고
    • Nonenzymatic glycosylation of HDL resulting in inhibition of high-affinity binding to cultured human fibroblasts
    • Duell PB, Oram JF, Bierman EL. Nonenzymatic glycosylation of HDL resulting in inhibition of high-affinity binding to cultured human fibroblasts. Diabetes 1990; 39:1257-1263.
    • (1990) Diabetes , vol.39 , pp. 1257-1263
    • Duell, P.B.1    Oram, J.F.2    Bierman, E.L.3
  • 50
    • 0345034617 scopus 로고    scopus 로고
    • Glycated low-density lipoprotein attenuates shear stress-induced nitric oxide synthesis by inhibition of shear stress-activated L-arginine uptake in endothelial cells
    • Posch K, Simecek S, Wascher TC, et al. Glycated low-density lipoprotein attenuates shear stress-induced nitric oxide synthesis by inhibition of shear stress-activated L-arginine uptake in endothelial cells. Diabetes 1999; 48:1331-1337.
    • (1999) Diabetes , vol.48 , pp. 1331-1337
    • Posch, K.1    Simecek, S.2    Wascher, T.C.3
  • 51
    • 0035408204 scopus 로고    scopus 로고
    • Lipoprotein lipase mediates the uptake of glycated LDL in fibroblasts, endothelial cells, and macrophages
    • Zimmermann R, Panzenbock U, Wintersperger A, et al. Lipoprotein lipase mediates the uptake of glycated LDL in fibroblasts, endothelial cells, and macrophages. Diabetes 2001; 50:1643-1653.
    • (2001) Diabetes , vol.50 , pp. 1643-1653
    • Zimmermann, R.1    Panzenbock, U.2    Wintersperger, A.3
  • 52
    • 0023956447 scopus 로고
    • Nonenzymatic glycosylation of low-density lipoprotein. Results of an affinity chromatography method
    • Jack CM, Sheridan B, Kennedy L, Stout RW. Nonenzymatic glycosylation of low-density lipoprotein. Results of an affinity chromatography method. Diabetologia 1988; 31:126-127.
    • (1988) Diabetologia , vol.31 , pp. 126-127
    • Jack, C.M.1    Sheridan, B.2    Kennedy, L.3    Stout, R.W.4
  • 53
    • 1242283934 scopus 로고    scopus 로고
    • In vivo oxidizability of LDL in type2 diabetic patients in good and poor glycemic control
    • Gambino R, Uberti B, Alemanno N, et al. In vivo oxidizability of LDL in type2 diabetic patients in good and poor glycemic control. Atherosclerosis 2004; 173:103-107.
    • (2004) Atherosclerosis , vol.173 , pp. 103-107
    • Gambino, R.1    Uberti, B.2    Alemanno, N.3
  • 54
    • 0024791971 scopus 로고
    • A simple method for the measurement of total and glycated apolipoprotein B and its relevance to apolipoprotein-B metabolism in diabetes mellitus
    • Kortlandt W, Benschop C, Erkelens DW, Thijssen JH. A simple method for the measurement of total and glycated apolipoprotein B and its relevance to apolipoprotein-B metabolism in diabetes mellitus. Clin Chim Acta 1989; 186:109-117.
    • (1989) Clin Chim Acta , vol.186 , pp. 109-117
    • Kortlandt, W.1    Benschop, C.2    Erkelens, D.W.3    Thijssen, J.H.4
  • 55
    • 0027940481 scopus 로고
    • Determination of glycated apolipoprotein B in serum by a combination of affinity chromatography and immunonephelometry
    • Panteghini M, Bonora R, Pagani F. Determination of glycated apolipoprotein B in serum by a combination of affinity chromatography and immunonephelometry. Ann Clin Biochem 1994; 31:544-549.
    • (1994) Ann Clin Biochem , vol.31 , pp. 544-549
    • Panteghini, M.1    Bonora, R.2    Pagani, F.3
  • 56
    • 0029792866 scopus 로고    scopus 로고
    • Effect of alpha-tocopherol on LDL oxidation and glycation: In vitro and In vivo studies
    • Li D, Devaraj S, Fuller C, et al. Effect of alpha-tocopherol on LDL oxidation and glycation: in vitro and In vivo studies. J Lipid Res 1996; 37:1978-1986.
    • (1996) J Lipid Res , vol.37 , pp. 1978-1986
    • Li, D.1    Devaraj, S.2    Fuller, C.3
  • 57
    • 2542497249 scopus 로고    scopus 로고
    • Antioxidative and antiglycative effects of six organosulfur compounds in low-density lipoprotein and plasma
    • Huang CN, Horng JS, Yin MC. Antioxidative and antiglycative effects of six organosulfur compounds in low-density lipoprotein and plasma. J Agric Food Chem 2004; 52:3674-3678.
    • (2004) J Agric Food Chem , vol.52 , pp. 3674-3678
    • Huang, C.N.1    Horng, J.S.2    Yin, M.C.3
  • 58
    • 3342913834 scopus 로고    scopus 로고
    • Jenkins AJ, Thorpe SR, Alderson NL, et al. In vivo glycated low-density lipoprotein is not more susceptible to oxidation than nonglycated low-density lipoprotein in type 1 diabetes. Metabolism 2004; 53:969-976.
    • Jenkins AJ, Thorpe SR, Alderson NL, et al. In vivo glycated low-density lipoprotein is not more susceptible to oxidation than nonglycated low-density lipoprotein in type 1 diabetes. Metabolism 2004; 53:969-976.
  • 59
    • 0027197140 scopus 로고
    • Immunologic detection and measurement of glycated apolipoprotein B with site specific monoclonal antibodies
    • Shea EA, Cohen MP. Immunologic detection and measurement of glycated apolipoprotein B with site specific monoclonal antibodies. J Immunol Methods 1993; 162:85-95.
    • (1993) J Immunol Methods , vol.162 , pp. 85-95
    • Shea, E.A.1    Cohen, M.P.2
  • 60
    • 0031926661 scopus 로고    scopus 로고
    • Influence of glycation on LDL-induced generation of fibrinolytic regulators in vascular endothelial cells
    • Zhang J, Ren S, Sun D, Shen GX. Influence of glycation on LDL-induced generation of fibrinolytic regulators in vascular endothelial cells. Arterioscler Thromb Vasc Biol 1998; 18:1140-1148.
    • (1998) Arterioscler Thromb Vasc Biol , vol.18 , pp. 1140-1148
    • Zhang, J.1    Ren, S.2    Sun, D.3    Shen, G.X.4
  • 61
    • 0029152174 scopus 로고
    • Glycation accelerates the oxidation of low density lipoprotein by copper ions
    • Kobayashi K, Watanabe J, Umeda F, Nawata H. Glycation accelerates the oxidation of low density lipoprotein by copper ions. Endocr J 1995; 42:461-465.
    • (1995) Endocr J , vol.42 , pp. 461-465
    • Kobayashi, K.1    Watanabe, J.2    Umeda, F.3    Nawata, H.4
  • 62
    • 0030693190 scopus 로고    scopus 로고
    • The role of oxidative stress in the long-term glycation of LDL
    • Menzel EJ, Sobal G, Staudinger A. The role of oxidative stress in the long-term glycation of LDL. Biofactors 1997; 6:111-124.
    • (1997) Biofactors , vol.6 , pp. 111-124
    • Menzel, E.J.1    Sobal, G.2    Staudinger, A.3
  • 63
    • 0034117018 scopus 로고    scopus 로고
    • In vivo and in vitro evidence for the glycoxidation of low density lipoprotein in human atherosclerotic plaques
    • Imanaga Y, Sakata N, Takebayashi S, et al. In vivo and in vitro evidence for the glycoxidation of low density lipoprotein in human atherosclerotic plaques. Atherosclerosis 2000; 150:343-355.
    • (2000) Atherosclerosis , vol.150 , pp. 343-355
    • Imanaga, Y.1    Sakata, N.2    Takebayashi, S.3
  • 64
    • 0027184474 scopus 로고
    • Lipid advanced glycosylation: Pathway for lipid oxidation in vivo
    • Bucala R, Makita Z, Koschinsky T, et al. Lipid advanced glycosylation: pathway for lipid oxidation in vivo. Proc Natl Acad Sci U S A 1993; 90:6434-6438.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 6434-6438
    • Bucala, R.1    Makita, Z.2    Koschinsky, T.3
  • 65
    • 0032514728 scopus 로고    scopus 로고
    • Oxidised LDL and malondialde-hyde-modified LDL in patients with acute coronary syndromes and stable coronary artery disease
    • Holvoet P, Vanhaecke J, Janssens S, et al. Oxidised LDL and malondialde-hyde-modified LDL in patients with acute coronary syndromes and stable coronary artery disease. Circulation 1998; 98:1487-1494.
    • (1998) Circulation , vol.98 , pp. 1487-1494
    • Holvoet, P.1    Vanhaecke, J.2    Janssens, S.3
  • 66
    • 0037419857 scopus 로고    scopus 로고
    • Temporal increases in plasma markers of oxidised low-density lipoprotein strongly reflect the presence of acute coronary syndromes
    • Tsimikas S, Bergmark C, Beyer RW, et al. Temporal increases in plasma markers of oxidised low-density lipoprotein strongly reflect the presence of acute coronary syndromes. J Am Coll Cardiol 2003; 41:360-370.
    • (2003) J Am Coll Cardiol , vol.41 , pp. 360-370
    • Tsimikas, S.1    Bergmark, C.2    Beyer, R.W.3
  • 67
    • 0035901607 scopus 로고    scopus 로고
    • Measuring circulating oxidised low-density lipoprotein to evaluate coronary risk
    • Tsimikas S, Witztum JL. Measuring circulating oxidised low-density lipoprotein to evaluate coronary risk. Circulation 2001; 103:1930-1932.
    • (2001) Circulation , vol.103 , pp. 1930-1932
    • Tsimikas, S.1    Witztum, J.L.2
  • 68
    • 0020692981 scopus 로고
    • Receptor-mediated catabolism of low density lipoprotein in man. Quantitation using glucosylated low density lipoprotein
    • Kesaniemi YA, Witztum JL, Steinbrecher UP. Receptor-mediated catabolism of low density lipoprotein in man. Quantitation using glucosylated low density lipoprotein. J Clin Invest 1983; 71:950-959.
    • (1983) J Clin Invest , vol.71 , pp. 950-959
    • Kesaniemi, Y.A.1    Witztum, J.L.2    Steinbrecher, U.P.3
  • 69
    • 0021744155 scopus 로고
    • 14C]sucrose-labelled low-density lipoprotein in vivo
    • 14C]sucrose-labelled low-density lipoprotein in vivo. Biochem J 1984; 224:21-27.
    • (1984) Biochem J , vol.224 , pp. 21-27
    • Harkes, L.1    Van Berkel, J.C.2
  • 70
    • 0020054056 scopus 로고
    • Nonenzymatic glucosylation of low-density lipoprotein alters its biologic activity
    • Witztum JL, Mahoney EM, Branks MJ, et al. Nonenzymatic glucosylation of low-density lipoprotein alters its biologic activity. Diabetes 1982; 31:283-291.
    • (1982) Diabetes , vol.31 , pp. 283-291
    • Witztum, J.L.1    Mahoney, E.M.2    Branks, M.J.3
  • 71
    • 0020068937 scopus 로고
    • Surface binding, internalization and degradation by cultured human fibroblasts of low density lipoproteins isolated from type 1 (insulin-dependent) diabetic patients: Changes with metabolic control
    • Lopes-Virella MF, Sherer GK, Lees AM, et al. Surface binding, internalization and degradation by cultured human fibroblasts of low density lipoproteins isolated from type 1 (insulin-dependent) diabetic patients: changes with metabolic control. Diabetologia 1982; 22:430-436.
    • (1982) Diabetologia , vol.22 , pp. 430-436
    • Lopes-Virella, M.F.1    Sherer, G.K.2    Lees, A.M.3
  • 72
    • 0020694412 scopus 로고
    • Comparison of glucosylated low density lipoprotein with methylated or cyclohexanedione-treated low density lipoprotein in the measurement of receptor-independent low density lipoprotein catabolism
    • Steinbrecher UP, Witztum JL, Kesaniemi YA, Elam RL. Comparison of glucosylated low density lipoprotein with methylated or cyclohexanedione-treated low density lipoprotein in the measurement of receptor-independent low density lipoprotein catabolism. J Clin Invest 1983; 71:960-964.
    • (1983) J Clin Invest , vol.71 , pp. 960-964
    • Steinbrecher, U.P.1    Witztum, J.L.2    Kesaniemi, Y.A.3    Elam, R.L.4
  • 73
    • 0033035123 scopus 로고    scopus 로고
    • Binding of long-term glycated low density lipoprotein and AGE-albumin by peripheral monocytes and endothelial cells
    • Sobal G, Sinzinger H, Menzel EJ. Binding of long-term glycated low density lipoprotein and AGE-albumin by peripheral monocytes and endothelial cells. J Recept Signal Transduct Res 1999; 19:267-281.
    • (1999) J Recept Signal Transduct Res , vol.19 , pp. 267-281
    • Sobal, G.1    Sinzinger, H.2    Menzel, E.J.3
  • 74
    • 0032560575 scopus 로고    scopus 로고
    • Epitopes close to the apolipoprotein B low density lipoprotein receptor-binding site are modified by advanced glycation end products
    • Wang X, Bucala R, Milne R. Epitopes close to the apolipoprotein B low density lipoprotein receptor-binding site are modified by advanced glycation end products. Proc Natl Acad Sci U S A 1998; 95:7643-7647.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7643-7647
    • Wang, X.1    Bucala, R.2    Milne, R.3
  • 75
    • 0344286498 scopus 로고    scopus 로고
    • Activation of receptor for advanced glycation end products: A mechanism for chronic vascular dysfunction in diabetic vasculopathy and atherosclerosis
    • Schmidt AM, Yan SD, Wautier JL, Stern D. Activation of receptor for advanced glycation end products: a mechanism for chronic vascular dysfunction in diabetic vasculopathy and atherosclerosis. Circ Res 1999; 84:489-497.
    • (1999) Circ Res , vol.84 , pp. 489-497
    • Schmidt, A.M.1    Yan, S.D.2    Wautier, J.L.3    Stern, D.4
  • 76
    • 33847374245 scopus 로고    scopus 로고
    • Brown BE, Rashid I, van Reyk DM, Davies MJ. Glycation of low-density lipoprotein results in the time-dependent accumulation of cholesteryl esters and apolipoprotein B-100 protein in primary human monocyte-derived macrophages. FEBS J 2007; 274:1530-1541. This study confirms the more powerful effect of aldehydes compared with glucose on LDL modification as tested by the change in particle charge, aggregation and amino acid modification. It also confirms the time-dependent accumulation of cholesteryl esters and apoB100 particles in primary human monocyte-derived macrophages via scavenger receptors (SR-A and CD36).
    • Brown BE, Rashid I, van Reyk DM, Davies MJ. Glycation of low-density lipoprotein results in the time-dependent accumulation of cholesteryl esters and apolipoprotein B-100 protein in primary human monocyte-derived macrophages. FEBS J 2007; 274:1530-1541. This study confirms the more powerful effect of aldehydes compared with glucose on LDL modification as tested by the change in particle charge, aggregation and amino acid modification. It also confirms the time-dependent accumulation of cholesteryl esters and apoB100 particles in primary human monocyte-derived macrophages via scavenger receptors (SR-A and CD36).
  • 77
    • 8644230195 scopus 로고    scopus 로고
    • Glycoxidized low-density lipoprotein regulates the expression of scavenger receptors in THP-1 macrophages
    • Lam MC, Tan KC, Lam KS. Glycoxidized low-density lipoprotein regulates the expression of scavenger receptors in THP-1 macrophages. Atherosclerosis 2004; 177:313-320.
    • (2004) Atherosclerosis , vol.177 , pp. 313-320
    • Lam, M.C.1    Tan, K.C.2    Lam, K.S.3
  • 78
    • 0345117400 scopus 로고    scopus 로고
    • Effect of glycated LDL on micro-vascular tone in mice: A comparative study with LDL modified in vitro or isolated from diabetic patients
    • Nivoit P, Wiernsperger N, Moulin P, et al. Effect of glycated LDL on micro-vascular tone in mice: a comparative study with LDL modified in vitro or isolated from diabetic patients. Diabetologia 2003; 46:1550-1558.
    • (2003) Diabetologia , vol.46 , pp. 1550-1558
    • Nivoit, P.1    Wiernsperger, N.2    Moulin, P.3
  • 79
    • 0020632227 scopus 로고
    • Nonenzymatic glucosylation of homologous low density lipoprotein and albumin renders them immunogenic in the guinea pig
    • Witztum JL, Steinbrecher UP, Fisher M, Kesaniemi A. Nonenzymatic glucosylation of homologous low density lipoprotein and albumin renders them immunogenic in the guinea pig. Proc Natl Acad Sci U S A 1983; 80:2757-2761.
    • (1983) Proc Natl Acad Sci U S A , vol.80 , pp. 2757-2761
    • Witztum, J.L.1    Steinbrecher, U.P.2    Fisher, M.3    Kesaniemi, A.4
  • 80
    • 18844439409 scopus 로고    scopus 로고
    • Histidine and carnosine delay diabetic deterioration in mice and protect human low density lipoprotein against oxidation and glycation
    • Lee YT, Hsu CC, Lin MH, et al. Histidine and carnosine delay diabetic deterioration in mice and protect human low density lipoprotein against oxidation and glycation. Eur J Pharmacol 2005; 513:145-150.
    • (2005) Eur J Pharmacol , vol.513 , pp. 145-150
    • Lee, Y.T.1    Hsu, C.C.2    Lin, M.H.3
  • 81
    • 0033525849 scopus 로고    scopus 로고
    • Increase in three alpha, betadicarbonyl compound levels in human uremic plasma: Specific In vivo determination of intermediates in advanced Maillard reaction
    • Odani H, Shinzato T, Matsumoto Y, et al. Increase in three alpha, betadicarbonyl compound levels in human uremic plasma: specific In vivo determination of intermediates in advanced Maillard reaction. Biochem Biophys Res Commun 1999; 256:89-93.
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 89-93
    • Odani, H.1    Shinzato, T.2    Matsumoto, Y.3
  • 82
    • 0037071843 scopus 로고    scopus 로고
    • Subendothelial retention of atherogenic lipoproteins in early atherosclerosis
    • Skalen K, Gustafsson M, Rydberg EK, et al. Subendothelial retention of atherogenic lipoproteins in early atherosclerosis. Nature 2002; 417:750-754.
    • (2002) Nature , vol.417 , pp. 750-754
    • Skalen, K.1    Gustafsson, M.2    Rydberg, E.K.3
  • 83
    • 0038625276 scopus 로고    scopus 로고
    • Protective action on human LDL against oxidation and glycation by four organosulfur compounds derived from garlic
    • Ou CC, Tsao SM, Lin MC, Yin MC. Protective action on human LDL against oxidation and glycation by four organosulfur compounds derived from garlic. Lipids 2003; 38:219-224.
    • (2003) Lipids , vol.38 , pp. 219-224
    • Ou, C.C.1    Tsao, S.M.2    Lin, M.C.3    Yin, M.C.4
  • 84
    • 34447547880 scopus 로고    scopus 로고
    • Influence of flavonols as in vitro on low density lipoprotein glycation
    • Ghaffari MA, Mojab S. Influence of flavonols as in vitro on low density lipoprotein glycation. Iran Biomed J 2007; 11:185-191.
    • (2007) Iran Biomed J , vol.11 , pp. 185-191
    • Ghaffari, M.A.1    Mojab, S.2
  • 85
    • 0025081749 scopus 로고
    • The histidine-containing dipeptides, carnosine and anserine: Distribution, properties and biological significance
    • Boldyrev AA, Severin SE. The histidine-containing dipeptides, carnosine and anserine: distribution, properties and biological significance. Adv Enzyme Regul 1990; 30:175-194.
    • (1990) Adv Enzyme Regul , vol.30 , pp. 175-194
    • Boldyrev, A.A.1    Severin, S.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.