메뉴 건너뛰기




Volumn 104, Issue 7, 1996, Pages 797-806

Contributions to senescence: Non-enzymatic glycosylation of proteins

Author keywords

degenerative changes; diabetes mellitus; non enzymatic glycosylation; senescence

Indexed keywords

LENS PROTEIN; LIPOPROTEIN; MATRIX PROTEIN; NERVE PROTEIN; PLASMA PROTEIN;

EID: 0030436952     PISSN: 13813455     EISSN: None     Source Type: Journal    
DOI: 10.1076/apab.104.7.797.13107     Document Type: Review
Times cited : (14)

References (76)
  • 1
    • 0022569845 scopus 로고
    • Non-enzymatic glycosylation influences HbS polymerization
    • ABRAHAM, E.G. & ELSEWEIDY, M.M. (1986) Non-enzymatic glycosylation influences HbS polymerization. Haemoglobin 10, 173-183.
    • (1986) Haemoglobin , vol.10 , pp. 173-183
    • Abraham, E.G.1    Elseweidy, M.M.2
  • 2
    • 0028020990 scopus 로고
    • Effects of matrix glycation on mesangial cell adhesion, spreading and proliferation
    • ANDERSON, S.S., KIM, Y. & TSILIBURY, E.G. (1994) Effects of matrix glycation on mesangial cell adhesion, spreading and proliferation. Kidney Int. 46, 1359-1367.
    • (1994) Kidney Int. , vol.46 , pp. 1359-1367
    • Anderson, S.S.1    Kim, Y.2    Tsilibury, E.G.3
  • 3
    • 0023215445 scopus 로고
    • Changes in collagen and elastin of the rat aorta induced by experimental diabetes and food restriction
    • ANDREASSEN, T.T. & OXLUND, H. (1987) Changes in collagen and elastin of the rat aorta induced by experimental diabetes and food restriction. Acta Endocrinol. Copenh. 115,338-344.
    • (1987) Acta Endocrinol. Copenh. , vol.115 , pp. 338-344
    • Andreassen, T.T.1    Oxlund, H.2
  • 4
    • 0026672970 scopus 로고
    • Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging
    • ARAKI, N., VENO, N., CHAKRABARTI, B., MARINO, Y. & HORIUCHI, S. (1992) Immunochemical evidence for the presence of advanced glycation end products in human lens proteins and its positive correlation with aging. J. . Biol. Cliem. 267, 10211-10214
    • (1992) J. . Biol. Cliem. , vol.267 , pp. 10211-10214
    • Araki, N.1    Veno, N.2    Chakrabarti, B.3    Marino, Y.4    Horiuchi, S.5
  • 5
    • 0024387514 scopus 로고
    • Non-enzymatic glycosylation of fibrous and basement membrane collagens
    • BAILEY, A.J. & KENT, M.J. (1989) Non-enzymatic glycosylation of fibrous and basement membrane collagens. Prog. Clin. Biol. Res. 304, 109-122.
    • (1989) Prog. Clin. Biol. Res. , vol.304 , pp. 109-122
    • Bailey, A.J.1    Kent, M.J.2
  • 7
    • 84976512673 scopus 로고
    • Pharmacology of alpha-glucosidase inhibition
    • BISCOFF, H. (1994) Pharmacology of alpha-glucosidase inhibition. Eitr. J. Clin. Invest. 24, 3-10.
    • (1994) Eitr. J. Clin. Invest. , vol.24 , pp. 3-10
    • Biscoff, H.1
  • 8
    • 0027979397 scopus 로고
    • Alpha 1-adrenergic and arginine vasopressin stimulation of inositide hydrolysis in rat hepatocytes is unaltered in senescence
    • BORST, S.E., OLIVER, R.J. & SCARPACE, P.J. (1994) Alpha 1-adrenergic and arginine vasopressin stimulation of inositide hydrolysis in rat hepatocytes is unaltered in senescence. J .Gerontol. 49, B18-21.
    • (1994) J .Gerontol. , vol.49
    • Borst, S.E.1    Oliver, R.J.2    Scarpace, P.J.3
  • 9
    • 0025906718 scopus 로고
    • Glycosylated products as toxic mediators of diabetic complications
    • BROWNLEE, M. (1991) Glycosylated products as toxic mediators of diabetic complications. Aim. Rev. Med. 42, 159-166.
    • (1991) Aim. Rev. Med. , vol.42 , pp. 159-166
    • Brownlee, M.1
  • 10
    • 0026062122 scopus 로고
    • Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilation in experimental diabetes
    • BUCALA, R., TRACEY, K.J. & CERAMI, A. (1991) Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilation in experimental diabetes. J. Clin. Invest. 87,432-438.
    • (1991) J. Clin. Invest. , vol.87 , pp. 432-438
    • Bucala, R.1    Tracey, K.J.2    Cerami, A.3
  • 11
    • 0021734343 scopus 로고
    • Post-translational modifications of haemoglobin
    • BUNN, H.F. (1984) Post-translational modifications of haemoglobin. Haematologia-Budap. 17, 179-186.
    • (1984) Haematologia-Budap. , vol.17 , pp. 179-186
    • Bunn, H.F.1
  • 12
    • 0022326929 scopus 로고    scopus 로고
    • I985 Protein glycosylation and the pathogenesis of atherosclerosis
    • CERAMI, A., VLASSARA, H. & BROWNLEE, M. (I985) Protein glycosylation and the pathogenesis of atherosclerosis. Metabolism 34, 37-42.
    • Metabolism , vol.34 , pp. 37-42
    • Cerami, A.1    Vlassara, H.2    Brownlee, M.3
  • 13
    • 0022574276 scopus 로고
    • Role of non-enzymatic glycosylation in atherogenesis
    • CERAMI, A., VLASSARA, H. & BROWNLEE, M. (1986) Role of non-enzymatic glycosylation in atherogenesis. J. Cell Biochem. 30, 111-120.
    • (1986) J. Cell Biochem. , vol.30 , pp. 111-120
    • Cerami, A.1    Vlassara, H.2    Brownlee, M.3
  • 14
    • 0024205254 scopus 로고
    • Role of advanced glycosylation products in complications of diabetes
    • CERAMI, A., VLASSARA, H. & BROWNLEE, M. (1988) Role of advanced glycosylation products in complications of diabetes. Diabetes Care 11, 73-79.
    • (1988) Diabetes Care , vol.11 , pp. 73-79
    • Cerami, A.1    Vlassara, H.2    Brownlee, M.3
  • 15
    • 0021090003 scopus 로고
    • Decreased antithrombin III activity in diabetes may be due to non-enzymatic glycosylation - A preliminary report
    • CERIELLO, A., DELLO-RUSSO, P., Zuccom, C., FLORIO, A., NAZZARO, S., PIETRANTUONO, C. & ROSATO, G.B. (1983) Decreased antithrombin III activity in diabetes may be due to non-enzymatic glycosylation - a preliminary report. Thromb. Haemost. 50, 633-634.
    • (1983) Thromb. Haemost. , vol.50 , pp. 633-634
    • Ceriello, A.1    Dello-Russo, P.2    Zuccom, C.3    Florio, A.4    Nazzaro, S.5    Pietrantuono, C.6    Rosato, G.B.7
  • 16
    • 0026562860 scopus 로고
    • New insights on non-enzymatic glycosylation may lead to therapeutic approaches for the prevention of diabetic complications
    • CERIELLO, A., QUATRARO, A. & GIUGLIANO, D. (1992) New insights on non-enzymatic glycosylation may lead to therapeutic approaches for the prevention of diabetic complications. Diabet. Med. 9, 297-9.
    • (1992) Diabet. Med. , vol.9 , pp. 297-299
    • Ceriello, A.1    Quatraro, A.2    Giugliano, D.3
  • 17
    • 0027367204 scopus 로고
    • Coagulation activation in diabetes mellitus, the role of hyperglycaemia and therapeutic prospects
    • CERIELLO, A. (1993) Coagulation activation in diabetes mellitus, the role of hyperglycaemia and therapeutic prospects. Diabetologia 36, 1119-1125.
    • (1993) Diabetologia , vol.36 , pp. 1119-1125
    • Ceriello, A.1
  • 18
    • 0021019253 scopus 로고
    • Age-related changes in non-enzymatic glycosylation of human basement membranes
    • COHEN, M.P. & Yu-Wu, V. (1983) Age-related changes in non-enzymatic glycosylation of human basement membranes. Exp. Gerontol. 18, 461-469.
    • (1983) Exp. Gerontol. , vol.18 , pp. 461-469
    • Cohen, M.P.1    Yu-Wu, V.2
  • 19
    • 0026025487 scopus 로고
    • The role of the polyol pathway in diabetes mellitus
    • COLLIER, A. & SMALL, M. (1991) The role of the polyol pathway in diabetes mellitus. Br. J. Hasp. Med. 45,38-40.
    • (1991) Br. J. Hasp. Med. , vol.45 , pp. 38-40
    • Collier, A.1    Small, M.2
  • 21
    • 0027445113 scopus 로고
    • Protein fructosylation, fructose and the Maillard reaction
    • DILLS, W.J. JR. (1993) Protein fructosylation, fructose and the Maillard reaction. Am. J. Clin. Ntitr. 58, 779-787.
    • (1993) Am. J. Clin. Ntitr. , vol.58 , pp. 779-787
    • Dills Jr., W.J.1
  • 22
    • 0025335026 scopus 로고
    • Increased glycation and pigmentation of collagen in aged and young parabiotic rats and mice
    • DEYL. Z., BUTENKO, G.M., HAUSMANN, J., HORAKOVA, M. & MACEK, K. (1990) Increased glycation and pigmentation of collagen in aged and young parabiotic rats and mice. Mech. Ageing Dev. 55, 39-47.
    • (1990) Mech. Ageing Dev. , vol.55 , pp. 39-47
    • Deyl, Z.1    Butenko, G.M.2    Hausmann, J.3    Horakova, M.4    Macek, K.5
  • 24
    • 0024468052 scopus 로고
    • Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties
    • EXPOSITO, C, GERLACH, H., BRETT, J., STREN, D. & VLASSARA, H. (1989) Endothelial receptor-mediated binding of glucose-modified albumin is associated with increased monolayer permeability and modulation of cell surface coagulant properties. J. Exp. Med. 170, 1387-1407.
    • (1989) J. Exp. Med. , vol.170 , pp. 1387-1407
    • Exposito, C.1    Gerlach, H.2    Brett, J.3    Stren, D.4    Vlassara, H.5
  • 26
    • 0028010810 scopus 로고
    • Differential aging pattern of cerebral accumulation of radiolabeled glucose and amino acid in the senescence accelerated mouse (SAM), a new model for the study of memory impairment
    • FUJIBAYASHI.K., WAKI, A.,WADA,K., UENO,M.,MAGATA, Y., YONEKURA, Y., KONISHI, J., TAKEDA, T. & YOKOYAMA, A. (1994) Differential aging pattern of cerebral accumulation of radiolabeled glucose and amino acid in the senescence accelerated mouse (SAM), a new model for the study of memory impairment. Biol. Pharm. Bull. 17, 102-105.
    • (1994) Biol. Pharm. Bull. , vol.17 , pp. 102-105
    • Waki, A.1    Wada, K.2    Ueno, M.3    Magata, Y.4    Yonekura, Y.5    Konishi, J.6    Takeda, T.7    Yokoyama, A.8
  • 27
    • 0025313580 scopus 로고
    • Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate
    • GILCREASE, M.Z. & HOOVER, R.L. (1990) Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate. Diabetologia 33, 329-333.
    • (1990) Diabetologia , vol.33 , pp. 329-333
    • Gilcrease, M.Z.1    Hoover, R.L.2
  • 28
    • 0021170321 scopus 로고
    • Influence of in vitro non-enzymatic glycosylation on the physiochemical parameters of type i collagen
    • GUITTON, J.D., LE-PAPE, A. & MUH, J.P. (1984) Influence of in vitro non-enzymatic glycosylation on the physiochemical parameters of type I collagen. Coll. Relat. Res. 4, 253-264.
    • (1984) Coll. Relat. Res. , vol.4 , pp. 253-264
    • Guitton, J.D.1    Le-Pape, A.2    Muh, J.P.3
  • 29
    • 0029111529 scopus 로고
    • Nonenzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent
    • HIPKISS, A.R., MICHAELIS, J. & SYRRIS, P. (1995) Nonenzymatic glycosylation of the dipeptide L-carnosine, a potential anti-protein-cross-linking agent. FEES Lett. 371,81-85
    • (1995) FEES Lett. , vol.371 , pp. 81-85
    • Hipkiss, A.R.1    Michaelis, J.2    Syrris, P.3
  • 30
    • 0028245083 scopus 로고
    • Advanced glycation end products of the Maillard reaction and their relation to aging
    • HORIUCHI, S. & ARAKI, N. (1994) Advanced glycation end products of the Maillard reaction and their relation to aging. Gerontology 40, 10-15.
    • (1994) Gerontology , vol.40 , pp. 10-15
    • Horiuchi, S.1    Araki, N.2
  • 31
    • 0023731241 scopus 로고
    • The fluoresence of serum proteins in diabetic patients with and without retinopathy
    • JONES, A.F., JENNINS, P.E., WAKEFIELD.A., WINKLES, J.W., LUNEC, J. & BARNETT, A.H. (1988) The fluoresence of serum proteins in diabetic patients with and without retinopathy. Diabetic Med. 5, 547-551.
    • (1988) Diabetic Med. , vol.5 , pp. 547-551
    • Jones, A.F.1    Jennins, P.E.2    Winkles, J.W.3    Lunec, J.4    Barnett, A.H.5
  • 32
    • 0028203656 scopus 로고
    • The interactions of modified lipoproteins with human erythrocyte membranes
    • JOSWIAK, Z., PALECZ, D. & BARTOSZ, G. (1994)The interactions of modified lipoproteins with human erythrocyte membranes. Biochem. Mol. Biol. Int. 32, 259-267.
    • (1994) Biochem. Mol. Biol. Int. , vol.32 , pp. 259-267
    • Joswiak, Z.1    Palecz, D.2    Bartosz, G.3
  • 33
    • 0022505868 scopus 로고
    • The accumulation of myoinositol and rubidium ions in galactose-exposed rat lens
    • KAWABA, T., CHENG, H.M. & KINOSHITA, J.H. (1986) The accumulation of myoinositol and rubidium ions in galactose-exposed rat lens. Invest. Opthalmol. Vis. Sei. 27, 1522-1526.
    • (1986) Invest. Opthalmol. Vis. Sei. , vol.27 , pp. 1522-1526
    • Kawaba, T.1    Cheng, H.M.2    Kinoshita, J.H.3
  • 34
    • 0024540829 scopus 로고
    • Non-enzymatic glycosylation
    • KENNEDY, L. & LYONS, T.J. (1989) Non-enzymatic glycosylation. Br. Med. Bull. 45, 174-190.
    • (1989) Br. Med. Bull. , vol.45 , pp. 174-190
    • Kennedy, L.1    Lyons, T.J.2
  • 35
    • 0025203319 scopus 로고
    • Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor, role in vascular disease of diabetes and aging
    • KIRSTEIN, M., BRETT, J., RADOFF, S., OGAWA, S., STERN, D. & VLASSARA, H. (1990) Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor, role in vascular disease of diabetes and aging. Proc. Nail. Acad. Sei. USA 87, 9010-9014.
    • (1990) Proc. Nail. Acad. Sei. USA , vol.87 , pp. 9010-9014
    • Kirstein, M.1    Brett, J.2    Radoff, S.3    Ogawa, S.4    Stern, D.5    Vlassara, H.6
  • 36
    • 0020564387 scopus 로고
    • Altered glycosylation and sialylation of serum proteins and lipid bound sialic acids in chronic renal failure
    • KISHORE, B.K., GEJYO, F. & ARAKAWA, M. (1983) Altered glycosylation and sialylation of serum proteins and lipid bound sialic acids in chronic renal failure. Postgrad. Med. J. 59,551-555.
    • (1983) Postgrad. Med. J. , vol.59 , pp. 551-555
    • Kishore, B.K.1    Gejyo, F.2    Arakawa, M.3
  • 37
    • 0022754288 scopus 로고
    • Non-enzymatic glycosylation of proteins
    • LAPOLLA, A., POLI, T. & FEDELE, D. (1986) Non-enzymatic glycosylation of proteins. Minerva Endocrinol. 11, 191-204.
    • (1986) Minerva Endocrinol. , vol.11 , pp. 191-204
    • Lapolla, A.1    Poli, T.2    Fedele, D.3
  • 38
    • 0021258203 scopus 로고
    • Distribution of non-enzymatically bound glucose in in vivo and in vitro glycosylated type i collagen molecules
    • LE-PAPE, A., GUITTON, J.D. & MUH, J.P. (1984) Distribution of non-enzymatically bound glucose in in vivo and in vitro glycosylated type I collagen molecules. FEBS Lett. 170, 23-27.
    • (1984) FEBS Lett. , vol.170 , pp. 23-27
    • Le-Pape, A.1    Guitton, J.D.2    Muh, J.P.3
  • 39
    • 0022627827 scopus 로고
    • Non-enzymatic glycosylation in human diabetic lens crystallins
    • LIANG, J.N., HERSHORIN, L.L. & CHYLACK, L.T. (1986) Non-enzymatic glycosylation in human diabetic lens crystallins. Diabetologla 29, 225-228.
    • (1986) Diabetologla , vol.29 , pp. 225-228
    • Liang, J.N.1    Hershorin, L.L.2    Chylack, L.T.3
  • 41
    • 0023269449 scopus 로고
    • The polyol pathway and glucose6-phosphate in human endothelial cells cultured in high glucose concentrations
    • LORENZI, M., TOLEDO, S., Boss, G.R., LANE, M.J. & MONTISANO, D.F. (1987) The polyol pathway and glucose6-phosphate in human endothelial cells cultured in high glucose concentrations. Diabetologia 30, 222-227.
    • (1987) Diabetologia , vol.30 , pp. 222-227
    • Lorenzi, M.1    Toledo, S.2    Boss, G.R.3    Lane, M.J.4    Montisano, D.F.5
  • 42
    • 0021932625 scopus 로고
    • Non-enzymatic glycosylation of skin collagen in patients with type i (insulin-dependent) diabetes mellitus and limited joint mobility
    • LYONS, T.J. & KENNEDY, L. (1985) Non-enzymatic glycosylation of skin collagen in patients with type I (insulin-dependent) diabetes mellitus and limited joint mobility. Diabetologia 28, 2-5.
    • (1985) Diabetologia , vol.28 , pp. 2-5
    • Lyons, T.J.1    Kennedy, L.2
  • 43
    • 0000916315 scopus 로고
    • Action des acides aminés sur les sucres, formation des mélanoidines par voie méthodique
    • MAILLARD, L.C. (1912) Action des acides aminés sur les sucres, formation des mélanoidines par voie méthodique. C.R. Se. Acad. Sei. 154, 66-68.
    • (1912) C.R. Se. Acad. Sei. , vol.154 , pp. 66-68
    • Maillard, L.C.1
  • 44
    • 0024585280 scopus 로고
    • Evidence for the glycation hypothesis of aging from the food-restricted rodent model
    • MASORO, E.J., KATZ, M.S. & MCMAHAN, C.A. (1989) Evidence for the glycation hypothesis of aging from the food-restricted rodent model. J. Gerontol. 44, 20-22.
    • (1989) J. Gerontol. , vol.44 , pp. 20-22
    • Masoro, E.J.1    Katz, M.S.2    Mcmahan, C.A.3
  • 45
    • 0027233741 scopus 로고
    • Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus
    • McCANCE, D.R., DYER, D.G., DUNN, J.A., BAILIE, K.E., THORPE, S.R., BAYNES, J.W. & LYONS, T.J. (1993) Maillard reaction products and their relation to complications in insulin-dependent diabetes mellitus. J. Clin. Invest. 91, 2470-2478.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2470-2478
    • McCance, D.R.1    Dyer, D.G.2    Dunn, J.A.3    Bailie, K.E.4    Thorpe, S.R.5    Baynes, J.W.6    Lyons, T.J.7
  • 47
    • 0027750568 scopus 로고
    • Genetic influences on glucose neurotoxicity, aging, and diabetes: A possible role for glucose hysteresis
    • MOBBS, C.V. (1993) Genetic influences on glucose neurotoxicity, aging, and diabetes: a possible role for glucose hysteresis. Genetica 91, 239-253.
    • (1993) Genetica , vol.91 , pp. 239-253
    • Mobbs, C.V.1
  • 49
    • 0026646758 scopus 로고
    • Maillard reaction mediated molecular damage to extracellular matrix and other tissue proteins in diabetes, aging, and uremia
    • MONNIER, V.M., SELL, D.R., NAGARAJ, R.H., MIYATA, S., GRONDHEE, S., ODETTI, P. & IBRAHIM, S.A. (1992) Maillard reaction mediated molecular damage to extracellular matrix and other tissue proteins in diabetes, aging, and uremia. Diabetes 41, 36-41.
    • (1992) Diabetes , vol.41 , pp. 36-41
    • Monnier, V.M.1    Sell, D.R.2    Nagaraj, R.H.3    Miyata, S.4    Grondhee, S.5    Odetti, P.6    Ibrahim, S.A.7
  • 51
    • 0022544329 scopus 로고
    • Nonenzymatic glycation of human albumin does not alter its palmitate binding
    • MURTIASHAW, M.H. & WINTERHALTER, K.H. (1986) Nonenzymatic glycation of human albumin does not alter its palmitate binding. Diabetologia 29, 366-370.
    • (1986) Diabetologia , vol.29 , pp. 366-370
    • Murtiashaw, M.H.1    Winterhalter, K.H.2
  • 52
    • 0026752939 scopus 로고
    • X ray diffraction studies on human tendon show age-related changes in collagen packing
    • NARESH, M.D. & BRODSKY, B. (1992) X ray diffraction studies on human tendon show age-related changes in collagen packing. Biochem. Biophys. Acta 1122, 161-166.
    • (1992) Biochem. Biophys. Acta , vol.1122 , pp. 161-166
    • Naresh, M.D.1    Brodsky, B.2
  • 53
  • 55
    • 0028908842 scopus 로고
    • Chromatographie evidence forpyrraline formation during protein glycation in vitro and in vivo
    • PORTERO O.M., NAGARAJ, R.H. & MONNIER, V.M. (1995) Chromatographie evidence forpyrraline formation during protein glycation in vitro and in vivo. Biochim. Biophys. Acta 1247,74-80.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 74-80
    • Portero, O.M.1    Nagaraj, R.H.2    Monnier, V.M.3
  • 56
    • 0023922126 scopus 로고
    • Characterization of a solubilized cell surface binding protein on macrophages specific for proteins modified non-enzymatically by advanced glycosylated end products
    • RADOFF, S., VLASSARA, H. & CERAMI, A. (1988) Characterization of a solubilized cell surface binding protein on macrophages specific for proteins modified non-enzymatically by advanced glycosylated end products. Arch. Biochem. Biophys. 263, 418-423.
    • (1988) Arch. Biochem. Biophys. , vol.263 , pp. 418-423
    • Radoff, S.1    Vlassara, H.2    Cerami, A.3
  • 57
    • 0025689060 scopus 로고
    • Isolation of surface binding protein specific for advanced glycosylation end products from mouse macrophages-derived cell line RAW 264.7
    • RADOFF, S., CERAMI, A. & VLASSARA, H. (1990) Isolation of surface binding protein specific for advanced glycosylation end products from mouse macrophages-derived cell line RAW 264.7. Diabetes 39, 1510-1518.
    • (1990) Diabetes , vol.39 , pp. 1510-1518
    • Radoff, S.1    Cerami, A.2    Vlassara, H.3
  • 58
    • 0025064927 scopus 로고
    • Changes in glycosylated proteins in long-term complications of diabetes mellitus
    • RAHMAN, M.A., ZAFAR, G. & SHERA, A.S. (1990) Changes in glycosylated proteins in long-term complications of diabetes mellitus. Biomed. Pharmacother. 44,229-234.
    • (1990) Biomed. Pharmacother. , vol.44 , pp. 229-234
    • Rahman, M.A.1    Zafar, G.2    Shera, A.S.3
  • 59
    • 0024817657 scopus 로고
    • Increased non-enzymatic glycosylation and reduced solubility of skin collagen in insulin dependent diabetic patients
    • SALMELA, P.I., OIKARINEN, A., PIRTTIAHO, H., KNIP, M., NIEMI, M. & RYHANEN, L. (1989) Increased non-enzymatic glycosylation and reduced solubility of skin collagen in insulin dependent diabetic patients. Diabetes Res. 11,115-120.
    • (1989) Diabetes Res. , vol.11 , pp. 115-120
    • Salmela, P.I.1    Oikarinen, A.2    Pirttiaho, H.3    Knip, M.4    Niemi, M.5    Ryhanen, L.6
  • 60
    • 0028980749 scopus 로고
    • Improved metabolic control in patients with noninsulin dependent diabetes mellitus is associated with a slower accumulation of glycation products in collagen
    • SALMELA, P.I.; OIKARINEN, A.I., UKKOLA, O., KARJALAINEN, A., LlNNALUOTO, M., PUUKKA, R. & RYHANEN, L. (1995) Improved metabolic control in patients with noninsulin dependent diabetes mellitus is associated with a slower accumulation of glycation products in collagen. Eur. J. Clin. Invest. 25, 494-500.
    • (1995) Eur. J. Clin. Invest. , vol.25 , pp. 494-500
    • Salmela, P.I.1    Oikarinen, A.I.2    Ukkola, O.3    Karjalainen, A.4    Llnnaluoto, M.5    Puukka, R.6    Ryhanen, L.7
  • 61
    • 0024436687 scopus 로고
    • Phagocytosis of aged human neutrophils by macrophages is mediated by a novel charge-sensitive recognition mechanism
    • SAVILL, J.S., HENSON, P.M. & HASLETT, C. (1989) Phagocytosis of aged human neutrophils by macrophages is mediated by a novel charge-sensitive recognition mechanism. J. Clin. Invest. 84, 1518-1528.
    • (1989) J. Clin. Invest. , vol.84 , pp. 1518-1528
    • Savill, J.S.1    Henson, P.M.2    Haslett, C.3
  • 62
    • 0025171955 scopus 로고
    • Hepatocyte fine structure during maturation and senescence
    • SCHUMUCKER, D.L. (1990) Hepatocyte fine structure during maturation and senescence. J. Electron Microsc. Tech. 14, 106-125.
    • (1990) J. Electron Microsc. Tech. , vol.14 , pp. 106-125
    • Schumucker, D.L.1
  • 63
    • 0024642408 scopus 로고
    • Role of the non-enzymatic glycosylation of protein in the formation of human cataracts
    • SIMONELLI, F., PENSA, M. & RINALDI, E. (1989) Role of the non-enzymatic glycosylation of protein in the formation of human cataracts. Boll. Soc. Ital. Biol. Sper. 65,351-356.
    • (1989) Boll. Soc. Ital. Biol. Sper. , vol.65 , pp. 351-356
    • Simonelli, F.1    Pensa, M.2    Rinaldi, E.3
  • 64
    • 0022408040 scopus 로고
    • Non-enzymatic glycosylation of plasma lipoproteins in vitro
    • SMITH, C.C., DICKSON, A.C. & BETTERIDGE, D.J. (1985) Non-enzymatic glycosylation of plasma lipoproteins in vitro. Diabetes Res. 2, 277-282.
    • (1985) Diabetes Res. , vol.2 , pp. 277-282
    • Smith, C.C.1    Dickson, A.C.2    Betteridge, D.J.3
  • 65
    • 0027315839 scopus 로고
    • Modified low density lipoprotein from diabetic patients causes cholesterol accumulation in human intimai aortic cells
    • SOBENIN, I.A., TERTOV, V.V., KOSCHINSKY, T., BUNTING, C.E., SLAVINA, E.S., DEDOV, I.I. & OREKHOVA, A.N. (1993) Modified low density lipoprotein from diabetic patients causes cholesterol accumulation in human intimai aortic cells. Atherosclerosis 100, 41-54.
    • (1993) Atherosclerosis , vol.100 , pp. 41-54
    • Sobenin, I.A.1    Tertov, V.V.2    Koschinsky, T.3    Bunting, C.E.4    Slavina, E.S.5    Dedov, I.I.6    Orekhova, A.N.7
  • 66
    • 0026040517 scopus 로고
    • The late complications of diabetes mellitus./twi
    • SQUADRITO, G. & CUCINOTTA, D. (1991) The late complications of diabetes mellitus./twi. Ital. Med. Int. 6, 126-136
    • (1991) Ital. Med. Int. , vol.6 , pp. 126-136
    • Squadrito, G.1    Cucinotta, D.2
  • 67
    • 0021272815 scopus 로고
    • Possible causes of change in collagen metabolism in aging
    • STRUCK, H. (1984) Possible causes of change in collagen metabolism in aging. J. Gerontol. 17, 85-88.
    • (1984) J. Gerontol. , vol.17 , pp. 85-88
    • Struck, H.1
  • 68
    • 0024376779 scopus 로고
    • Nonenzymatic browning of proteins and the sorbitol pathway
    • SUAREZ, G. (1989) Nonenzymatic browning of proteins and the sorbitol pathway. Prog. Clin. Biol. Res. 304, 141-162.
    • (1989) Prog. Clin. Biol. Res. , vol.304 , pp. 141-162
    • Suarez, G.1
  • 69
    • 0025997576 scopus 로고
    • Effect of non-enzymatic glycosylation and heating on browning of human stratum corneum and nail
    • SUEKI, H., NOZAKI, S., NUMAZAWA, S., AOKI, K., KUROIWA, Y. &FUJISAWA, R. (1991) Effect of non-enzymatic glycosylation and heating on browning of human stratum corneum and nail. Dennatologica 183, 197-202.
    • (1991) Dennatologica , vol.183 , pp. 197-202
    • Sueki, H.1    Nozaki, S.2    Numazawa, S.3    Aoki, K.4    Kuroiwa, Y.5    Fujisawa, R.6
  • 70
    • 17144451354 scopus 로고
    • Pathogenic aspects of diabetic macroangiopathy
    • TKAC, I. (1990) Pathogenic aspects of diabetic macroangiopathy. Vnitr-Lek. 36, 590-596.
    • (1990) Vnitr-Lek. , vol.36 , pp. 590-596
    • Tkac, I.1
  • 71
    • 0004818738 scopus 로고
    • High affinity receptor mediated uptake and degradation of glucose modified proteins, a potential mechanism for the removal of senescent macromolecules
    • VLASSARA, H., BROWNLEE, M. & CERAMI, A. (1985) High affinity receptor mediated uptake and degradation of glucose modified proteins, a potential mechanism for the removal of senescent macromolecules. Proc. Natl. Acad. Sei. USA 82, 5588-5592.
    • (1985) Proc. Natl. Acad. Sei. USA , vol.82 , pp. 5588-5592
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 72
    • 0002602893 scopus 로고
    • Nonenzymatic glycosylation in the pathogenesis of diabetic complications
    • VLASSARA, H., BROWNLEE, M. & CERAMI, A. (1986) Nonenzymatic glycosylation in the pathogenesis of diabetic complications. Clin. Chem. 32, B37-B41.
    • (1986) Clin. Chem. , vol.32
    • Vlassara, H.1    Brownlee, M.2    Cerami, A.3
  • 73
    • 0023940640 scopus 로고
    • Cachectin/TNF and IL1 induced by glucose modified proteins, role in normal tissue remodeling
    • VLASSARA, H., BROWNLEE, M., MANOGUE, K.R., DINARELLO, C.A. & PASAGIAN, A. (1988) Cachectin/TNF and IL1 induced by glucose modified proteins, role in normal tissue remodeling. Science 240, 1546-1548.
    • (1988) Science , vol.240 , pp. 1546-1548
    • Vlassara, H.1    Brownlee, M.2    Manogue, K.R.3    Dinarello, C.A.4    Pasagian, A.5
  • 74
    • 0020534909 scopus 로고
    • The thermal stability of collagen in diabetic rats, correlation with severity of diabetes and non-enzymatic glycosylation
    • YUE, O.K., MCLENNAN, S., DELBRIDGE.L., HANDELSMAN, D.J., REEVE, T. & TURTLE, J.R. (1983a) The thermal stability of collagen in diabetic rats, correlation with severity of diabetes and non-enzymatic glycosylation. Diabetologia 24, 282-285.
    • (1983) Diabetologia , vol.24 , pp. 282-285
    • Yue, O.K.1    Mclennan, S.2    Handelsman, D.J.3    Reeve, T.4    Turtle, J.R.5
  • 75
    • 0020535669 scopus 로고
    • Nonenzymatic glycosylation of tissue protein in diabetes in the rat
    • YUE, O.K., MCLENNAN, S. & TURTLE, J.R. (1983b) Nonenzymatic glycosylation of tissue protein in diabetes in the rat. Diabetologia 24, 377-381.
    • (1983) Diabetologia , vol.24 , pp. 377-381
    • Yue, O.K.1    Mclennan, S.2    Turtle, J.R.3
  • 76
    • 0028798704 scopus 로고
    • Formation of reactive intermediates from Amadori compounds under physiological conditions
    • ZYZAK, D.V., RICHARDSON, J.M., THORPE, S.R. & BAYNES, J.W. (1995) Formation of reactive intermediates from Amadori compounds under physiological conditions. Arch. Biochem. Biophys. 316, 547-554.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 547-554
    • Zyzak, D.V.1    Richardson, J.M.2    Thorpe, S.R.3    Baynes, J.W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.