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Volumn 43, Issue 2, 1999, Pages 81-89

Aminoguanidine inhibits albuminuria, but not the formation of advanced glycation end-products in skin collagen of diabetic rats

Author keywords

Advanced glycation end products (AGE); Albuminuria; Aminoguanidine; Collagen; N( ) (carboxymethyl)lysine; Pentosidine

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ALBUMIN; AMINOGUANIDINE; COLLAGEN; HEMOGLOBIN; HEMOGLOBIN A1C; LYSINE DERIVATIVE; PENTOSIDINE;

EID: 0032892660     PISSN: 01688227     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-8227(98)00121-1     Document Type: Article
Times cited : (35)

References (51)
  • 1
    • 0028469809 scopus 로고
    • Recent progress on the biologic and clinical significance of advanced glycosylation end products
    • Vlassara H. Recent progress on the biologic and clinical significance of advanced glycosylation end products. J. Lab. Clin. Med. 124:1994;19-30.
    • (1994) J. Lab. Clin. Med. , vol.124 , pp. 19-30
    • Vlassara, H.1
  • 2
    • 0028923810 scopus 로고
    • Advanced glycosylation endproducts in diabetic renal disease: Clinical measurement, pathophysiological significance, and prospects for pharmacological inhibition
    • Bucala R., Vlassara H. Advanced glycosylation endproducts in diabetic renal disease: clinical measurement, pathophysiological significance, and prospects for pharmacological inhibition. Blood Purif. 13:1995;160-170.
    • (1995) Blood Purif. , vol.13 , pp. 160-170
    • Bucala, R.1    Vlassara, H.2
  • 3
    • 0028068046 scopus 로고
    • Cellular receptors for advanced glycation end products: Implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions
    • Schmidt A.M., Hori O., Brett J., Yan S.D., Wautier J.-L., Stern D. Cellular receptors for advanced glycation end products: implications for induction of oxidant stress and cellular dysfunction in the pathogenesis of vascular lesions. Arterioscler. Thromb. 14:1994;1521-1528.
    • (1994) Arterioscler. Thromb. , vol.14 , pp. 1521-1528
    • Schmidt, A.M.1    Hori, O.2    Brett, J.3    Yan, S.D.4    Wautier, J.-L.5    Stern, D.6
  • 4
    • 0022644227 scopus 로고
    • Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking
    • Brownlee M., Vlassara H., Kooney T., Ulrich P., Cerami A. Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science. 232:1986;1629-1632.
    • (1986) Science , vol.232 , pp. 1629-1632
    • Brownlee, M.1    Vlassara, H.2    Kooney, T.3    Ulrich, P.4    Cerami, A.5
  • 5
    • 0026782087 scopus 로고
    • Role of oxygen in crosslinking and chemical modification of collagen by glucose
    • Fu M.X., Knecht K.J., Thorpe S.R., Baynes J.W. Role of oxygen in crosslinking and chemical modification of collagen by glucose. Diabetes. 41:1992;42-48.
    • (1992) Diabetes , vol.41 , pp. 42-48
    • Fu, M.X.1    Knecht, K.J.2    Thorpe, S.R.3    Baynes, J.W.4
  • 6
    • 0028223128 scopus 로고
    • Glycation, glycoxidation and cross-linking of collagen by glucose: Kinetics, mechanisms, and inhibition of late stages of the Maillard reaction
    • Fu M.X., Wells-Knecht K.J., Blackledge J.A., Lyons T.J., Thorpe S.R., Baynes J.W. Glycation, glycoxidation and cross-linking of collagen by glucose: kinetics, mechanisms, and inhibition of late stages of the Maillard reaction. Diabetes. 43:1994;676-683.
    • (1994) Diabetes , vol.43 , pp. 676-683
    • Fu, M.X.1    Wells-Knecht, K.J.2    Blackledge, J.A.3    Lyons, T.J.4    Thorpe, S.R.5    Baynes, J.W.6
  • 8
    • 0026063185 scopus 로고
    • Retardation by aminoguanidine of development of albuminuria, mesangial expansion, and tissue fluorescence in streptozotocin-induced diabetic rat
    • Soulis-Liparota T., Cooper M., Papazoglou D., Clarke B., Jerums G. Retardation by aminoguanidine of development of albuminuria, mesangial expansion, and tissue fluorescence in streptozotocin-induced diabetic rat. Diabetes. 40:1991;1328-1334.
    • (1991) Diabetes , vol.40 , pp. 1328-1334
    • Soulis-Liparota, T.1    Cooper, M.2    Papazoglou, D.3    Clarke, B.4    Jerums, G.5
  • 9
    • 0026584035 scopus 로고
    • Aminoguanidine ameliorates albuminuria in diabetic hypertensive rats
    • Edelstein D., Brownlee M. Aminoguanidine ameliorates albuminuria in diabetic hypertensive rats. Diabetologia. 35:1992;96-97.
    • (1992) Diabetologia , vol.35 , pp. 96-97
    • Edelstein, D.1    Brownlee, M.2
  • 10
    • 0026323337 scopus 로고
    • Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy
    • Hammes H.P., Martin S., Federlin K., Geisen K., Brownlee M. Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy. Proc. Natl. Acad. Sci. USA. 88:1991;11555-11558.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11555-11558
    • Hammes, H.P.1    Martin, S.2    Federlin, K.3    Geisen, K.4    Brownlee, M.5
  • 11
    • 0028107538 scopus 로고
    • Aminoguanidine inhibits the development of accelerated diabetic retinopathy in the spontaneous hypertensive rat
    • Hammes H.P., Brownlee M., Edelstein D., Saleck M., Martin S., Federlin K. Aminoguanidine inhibits the development of accelerated diabetic retinopathy in the spontaneous hypertensive rat. Diabetologia. 37:1994;32-35.
    • (1994) Diabetologia , vol.37 , pp. 32-35
    • Hammes, H.P.1    Brownlee, M.2    Edelstein, D.3    Saleck, M.4    Martin, S.5    Federlin, K.6
  • 13
    • 0026571089 scopus 로고
    • Effect of aminoguanidine on functional and structural abnormalities in peripheral nerve of STZ-induced diabetic rats
    • Yagihashi S., Kamijo M., Baba M., Yagihashi N., Nagai K. Effect of aminoguanidine on functional and structural abnormalities in peripheral nerve of STZ-induced diabetic rats. Diabetes. 41:1992;47-52.
    • (1992) Diabetes , vol.41 , pp. 47-52
    • Yagihashi, S.1    Kamijo, M.2    Baba, M.3    Yagihashi, N.4    Nagai, K.5
  • 14
    • 0026728117 scopus 로고
    • Effects of aminoguanidine on peripheral nerve function and polyol pathway metabolites in streptozotocin-diabetic rats
    • Cameron N.E., Cotter M.A., Dines K., Love A. Effects of aminoguanidine on peripheral nerve function and polyol pathway metabolites in streptozotocin-diabetic rats. Diabetologia. 35:1992;946-950.
    • (1992) Diabetologia , vol.35 , pp. 946-950
    • Cameron, N.E.1    Cotter, M.A.2    Dines, K.3    Love, A.4
  • 16
    • 0030785422 scopus 로고    scopus 로고
    • Aminoguanidine inhibits semicarbazide-sensitive amine oxidase activity: Implications for advanced glycation and diabetic complications
    • Yu H.P., Zou D.M. Aminoguanidine inhibits semicarbazide-sensitive amine oxidase activity: implications for advanced glycation and diabetic complications. Diabetologia. 40:1997;1243-1250.
    • (1997) Diabetologia , vol.40 , pp. 1243-1250
    • Yu, H.P.1    Zou, D.M.2
  • 19
    • 0026625832 scopus 로고
    • Aminoguanidine inhibits oxidative modification of low density lipoprotein and the subsequent increase in uptake by macrophage scavenger receptor
    • Picard S., Parthasarathy S., Fruebis J., Witztum J.L. Aminoguanidine inhibits oxidative modification of low density lipoprotein and the subsequent increase in uptake by macrophage scavenger receptor. Proc. Natl. Acad. Sci. USA. 89:1992;6876-6880.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6876-6880
    • Picard, S.1    Parthasarathy, S.2    Fruebis, J.3    Witztum, J.L.4
  • 20
    • 0027020608 scopus 로고
    • Aminoguanidine inhibits the modification of proteins by lipid peroxidation derived aldehydes: A possible antiatherogenic agent
    • Requena J.R., Vidal P., Cabezas-Cerrato J. Aminoguanidine inhibits the modification of proteins by lipid peroxidation derived aldehydes: a possible antiatherogenic agent. Diabetes Res. 20:1992;43-49.
    • (1992) Diabetes Res. , vol.20 , pp. 43-49
    • Requena, J.R.1    Vidal, P.2    Cabezas-Cerrato, J.3
  • 21
    • 0028198838 scopus 로고
    • A critical assessment of the effects of aminoguanidine and ascorbate on the oxidative modification of LDL: Evidence for interference with some assays of lipoprotein oxidation by aminoguanidine
    • Scaccini C., Chiesa G., Jialal I. A critical assessment of the effects of aminoguanidine and ascorbate on the oxidative modification of LDL: evidence for interference with some assays of lipoprotein oxidation by aminoguanidine. J. Lipid Res. 35:1994;1085-1092.
    • (1994) J. Lipid Res. , vol.35 , pp. 1085-1092
    • Scaccini, C.1    Chiesa, G.2    Jialal, I.3
  • 23
    • 0031022947 scopus 로고    scopus 로고
    • Discordant effects of guanidines on renal structure and function and on regional vascular dysfunction and collagen changes in diabetic rats
    • Nyengaard J.R., Chang K., Berhorst S., Reiser K.M., Williamson J.R., Tilton R.G. Discordant effects of guanidines on renal structure and function and on regional vascular dysfunction and collagen changes in diabetic rats. Diabetes. 46:1997;94-106.
    • (1997) Diabetes , vol.46 , pp. 94-106
    • Nyengaard, J.R.1    Chang, K.2    Berhorst, S.3    Reiser, K.M.4    Williamson, J.R.5    Tilton, R.G.6
  • 24
    • 0030811664 scopus 로고    scopus 로고
    • Advanced glycation end products and their receptors co-localise in rat organs susceptible to diabetic microvascular injury
    • Soulis T., Thallas V., Youssef S., Gilbert R.E., McWilliam B.G., Murray-McIntosh R.P., Cooper M.E. Advanced glycation end products and their receptors co-localise in rat organs susceptible to diabetic microvascular injury. Diabetologia. 40:1997;619-628.
    • (1997) Diabetologia , vol.40 , pp. 619-628
    • Soulis, T.1    Thallas, V.2    Youssef, S.3    Gilbert, R.E.4    McWilliam, B.G.5    Murray-McIntosh, R.P.6    Cooper, M.E.7
  • 25
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix: Implication of pentoses in the aging process
    • Sell D.R., Monnier V.M. Structure elucidation of a senescence cross-link from human extracellular matrix: implication of pentoses in the aging process. J. Biol. Chem. 264:1989;21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 26
    • 0025945553 scopus 로고
    • Formation of pentosidine during non-enzymatic browning of proteins by glucose
    • Dyer D.G., Blackledge J.A., Thorpe S.R., Baynes J.W. Formation of pentosidine during non-enzymatic browning of proteins by glucose. J. Biol. Chem. 266:1991;1654-1660.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1654-1660
    • Dyer, D.G.1    Blackledge, J.A.2    Thorpe, S.R.3    Baynes, J.W.4
  • 27
    • 0022931516 scopus 로고
    • ε-(carboxymethyl)lysine as a degradation product of fructoselysine in glycated protein
    • ε-(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
  • 29
    • 0014438677 scopus 로고
    • A specific and sensitive assay for aminoguanidine: Its implication to a study of the disposition of aminoguanidine in animal tissues
    • Beaven M.A., Gordon J.W., Jacobsen S., Severs W.B. A specific and sensitive assay for aminoguanidine: its implication to a study of the disposition of aminoguanidine in animal tissues. J. Pharmacol. Exp. Ther. 165:1969;14-22.
    • (1969) J. Pharmacol. Exp. Ther. , vol.165 , pp. 14-22
    • Beaven, M.A.1    Gordon, J.W.2    Jacobsen, S.3    Severs, W.B.4
  • 34
    • 0026541454 scopus 로고
    • Aminoguanidine treatment reduces the increase in collagen stability of rats with experimental diabetes mellitus
    • Oxlund H., Andreassen T.T. Aminoguanidine treatment reduces the increase in collagen stability of rats with experimental diabetes mellitus. Diabetologia. 35:1992;19-25.
    • (1992) Diabetologia , vol.35 , pp. 19-25
    • Oxlund, H.1    Andreassen, T.T.2
  • 35
    • 0024788007 scopus 로고
    • Changes in solubility, non-enzymatic glycation, and fluorescence of collagen in tail tendons from diabetic rats
    • Brennan M. Changes in solubility, non-enzymatic glycation, and fluorescence of collagen in tail tendons from diabetic rats. J. Biol. Chem. 264:1989;20947-20952.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20947-20952
    • Brennan, M.1
  • 36
    • 0024829260 scopus 로고
    • Changes in the cross-linking of collagen from rat tail tendons due to diabetes
    • Brennan M. Changes in the cross-linking of collagen from rat tail tendons due to diabetes. J. Biol. Chem. 264:1989;20953-20960.
    • (1989) J. Biol. Chem. , vol.264 , pp. 20953-20960
    • Brennan, M.1
  • 37
    • 0026675759 scopus 로고
    • Pentosidine formation in skin correlates with severity of complications in individuals with long-standing IDDM
    • Sell D.R., Lapolla A., Odetti P., Fogarty J., Monnier V.M. Pentosidine formation in skin correlates with severity of complications in individuals with long-standing IDDM. Diabetes. 41:1992;1286-1292.
    • (1992) Diabetes , vol.41 , pp. 1286-1292
    • Sell, D.R.1    Lapolla, A.2    Odetti, P.3    Fogarty, J.4    Monnier, V.M.5
  • 39
    • 0028826628 scopus 로고
    • Pathways of formation of glycoxidation products during glycation of collagen
    • Wells-Knecht M.C., Thorpe S.R., Baynes J.W. Pathways of formation of glycoxidation products during glycation of collagen. Biochemistry. 34:1995;15134-15141.
    • (1995) Biochemistry , vol.34 , pp. 15134-15141
    • Wells-Knecht, M.C.1    Thorpe, S.R.2    Baynes, J.W.3
  • 40
    • 0026575313 scopus 로고
    • Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine
    • Edelstein D., Brownlee M. Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine. Diabetes. 41:1992;26-29.
    • (1992) Diabetes , vol.41 , pp. 26-29
    • Edelstein, D.1    Brownlee, M.2
  • 41
    • 0025939381 scopus 로고
    • Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus
    • Lyons T.J., Bailie K.E., Dyer D.G., Dunn J.A., Baynes J.W. Decrease in skin collagen glycation with improved glycemic control in patients with insulin-dependent diabetes mellitus. J. Clin. Invest. 87:1991;1910-1915.
    • (1991) J. Clin. Invest. , vol.87 , pp. 1910-1915
    • Lyons, T.J.1    Bailie, K.E.2    Dyer, D.G.3    Dunn, J.A.4    Baynes, J.W.5
  • 42
    • 0028934990 scopus 로고
    • Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction
    • Glomb M.A., Monnier V.M. Mechanism of protein modification by glyoxal and glycolaldehyde, reactive intermediates of the Maillard reaction. J. Biol. Chem. 270:1995;10017-10026.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10017-10026
    • Glomb, M.A.1    Monnier, V.M.2
  • 43
    • 0029995384 scopus 로고    scopus 로고
    • Kinetics of non-enzymatic glycation of ribonuclease a leading to advanced glycation end products. Paradoxical inhibition by ribose leads to facile isolation of protein intermediate for rapid post-Amadori studies
    • Khalifah R.G., Todd P., Booth A.A., Yang S.X., Mott J.D., Hudson B.G. Kinetics of non-enzymatic glycation of ribonuclease a leading to advanced glycation end products. Paradoxical inhibition by ribose leads to facile isolation of protein intermediate for rapid post-Amadori studies. Biochemistry. 35:1996;4645-4654.
    • (1996) Biochemistry , vol.35 , pp. 4645-4654
    • Khalifah, R.G.1    Todd, P.2    Booth, A.A.3    Yang, S.X.4    Mott, J.D.5    Hudson, B.G.6
  • 44
    • 0029870323 scopus 로고    scopus 로고
    • Thiamine pyrophosphate and pyridoxamine inhibit the formation of antigenic advanced glycation end-products: Comparison with aminoguanidine
    • Booth A.A., Khalifah R.G., Hudson B.G. Thiamine pyrophosphate and pyridoxamine inhibit the formation of antigenic advanced glycation end-products: comparison with aminoguanidine. Biochem. Biophys. Res. Commun. 220:1996;113-119.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 113-119
    • Booth, A.A.1    Khalifah, R.G.2    Hudson, B.G.3
  • 45
    • 0022342392 scopus 로고
    • Inhibition of in vivo histamine metabolism in rats by foodborne and pharmacologic inhibitors of diamine oxidase, histamine N-methyltransferase, and monoamine oxidase
    • Hui J.Y., Taylor S.L. Inhibition of in vivo histamine metabolism in rats by foodborne and pharmacologic inhibitors of diamine oxidase, histamine N-methyltransferase, and monoamine oxidase. Toxicol. Appl. Pharmacol. 81:1985;241-249.
    • (1985) Toxicol. Appl. Pharmacol. , vol.81 , pp. 241-249
    • Hui, J.Y.1    Taylor, S.L.2
  • 46
    • 0024408173 scopus 로고
    • Comparative sensitivities of purified preparations of lysyl oxidase and other amine oxidases to active site-directed enzyme inhibitors
    • Tang S.-S., Chichester C.O., Kagan H.M. Comparative sensitivities of purified preparations of lysyl oxidase and other amine oxidases to active site-directed enzyme inhibitors. Connect. Tissue Res. 19:1989;93-103.
    • (1989) Connect. Tissue Res. , vol.19 , pp. 93-103
    • Tang, S.-S.1    Chichester, C.O.2    Kagan, H.M.3
  • 47
    • 0026293875 scopus 로고
    • The influence of aminoguanidine on borohydride reducible collagen cross-links and wound strength
    • Seyer-Hansen M., Andreassen T.T., Oxlund H., Jorgensen P.H. The influence of aminoguanidine on borohydride reducible collagen cross-links and wound strength. Connect. Tissue Res. 26:1991;181-186.
    • (1991) Connect. Tissue Res. , vol.26 , pp. 181-186
    • Seyer-Hansen, M.1    Andreassen, T.T.2    Oxlund, H.3    Jorgensen, P.H.4
  • 48
    • 0028346288 scopus 로고
    • Effects of guanidino and uremic compounds on nitric oxide pathways
    • MacAllister R.J., Whitley G.S., Vallance P. Effects of guanidino and uremic compounds on nitric oxide pathways. Kidney Int. 45:1994;737-742.
    • (1994) Kidney Int. , vol.45 , pp. 737-742
    • MacAllister, R.J.1    Whitley, G.S.2    Vallance, P.3
  • 49
    • 0028893884 scopus 로고
    • Aminoguanidine is an isoform-selective, mechanism-based inactivator of nitric oxide synthase
    • Wolff D.J., Lubeskie A. Aminoguanidine is an isoform-selective, mechanism-based inactivator of nitric oxide synthase. Arch. Biochem. Biophys. 316:1995;290-301.
    • (1995) Arch. Biochem. Biophys. , vol.316 , pp. 290-301
    • Wolff, D.J.1    Lubeskie, A.2
  • 50
    • 0027517899 scopus 로고
    • Aminoguanidine: A drug proposed for prophylaxis in diabetes inhibits catalase and generates hydrogen peroxide in vitro
    • Ou P., Wolff S.P. Aminoguanidine: a drug proposed for prophylaxis in diabetes inhibits catalase and generates hydrogen peroxide in vitro. Biochem. Pharmacol. 46:1993;1139-1144.
    • (1993) Biochem. Pharmacol. , vol.46 , pp. 1139-1144
    • Ou, P.1    Wolff, S.P.2
  • 51
    • 0028969292 scopus 로고
    • Effects of aminoguanidine and pyridoxal phosphate on glycation reaction of aspartate aminotransferases and serum albumin
    • Okada M., Ayabe Y. Effects of aminoguanidine and pyridoxal phosphate on glycation reaction of aspartate aminotransferases and serum albumin. J. Nutr. Sci. Vitaminol. 41:1995;43-50.
    • (1995) J. Nutr. Sci. Vitaminol. , vol.41 , pp. 43-50
    • Okada, M.1    Ayabe, Y.2


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