메뉴 건너뛰기




Volumn 48, Issue 5-6, 2002, Pages 125-136

Experimental studies on the role of fructose in the development of diabetic complications

Author keywords

Diabetic complications; Fructose; Glycation; Oxidative stress; Polyol pathway

Indexed keywords

3 DEOXYGLUCOSONE; ADVANCED GLYCATION END PRODUCT; AMINOGUANIDINE; CARBONYL DERIVATIVE; COLLAGEN TYPE 4; EPALRESTAT; FREE RADICAL; FRUCTOSE; GLUCOSE; GLYCOSYLATED COLLAGEN; LOW DENSITY LIPOPROTEIN; LYSINE; LYSOZYME; POLYOL; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 0037983622     PISSN: 00232513     EISSN: 18830498     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (73)

References (26)
  • 1
    • 0025853670 scopus 로고
    • Protein glycation and oxidative stress in diabetes mellitus and aging
    • Wolff, S.P., Jiang, Z.Y., and Hunt, J.V. 1991. Protein glycation and oxidative stress in diabetes mellitus and aging. Free Radical Biol. Med. 10:339-352.
    • (1991) Free Radical Biol. Med. , vol.10 , pp. 339-352
    • Wolff, S.P.1    Jiang, Z.Y.2    Hunt, J.V.3
  • 2
    • 0032835194 scopus 로고    scopus 로고
    • Hyperglycemia: The bridge between non-enzymatic glycation and oxidative stress in the pathogenesis of diabetic complications
    • Ceriello, A. 1999. Hyperglycemia: the bridge between non-enzymatic glycation and oxidative stress in the pathogenesis of diabetic complications. Diabetes Nutr. Metab. 12:42-46.
    • (1999) Diabetes Nutr. Metab. , vol.12 , pp. 42-46
    • Ceriello, A.1
  • 3
    • 0028936121 scopus 로고
    • Diabetic late complications: Will aldose reductase inhibitors or inhibitors of advanced glycosylation end-product formation hold promise?
    • Boel, E., Selmer, J., and Jensen, T. 1995. Diabetic late complications: will aldose reductase inhibitors or inhibitors of advanced glycosylation end-product formation hold promise? Diabetes Complications 9:104-129.
    • (1995) Diabetes Complications , vol.9 , pp. 104-129
    • Boel, E.1    Selmer, J.2    Jensen, T.3
  • 4
    • 0002726092 scopus 로고
    • Structure of collagen from human tendon as influenced by age and sex
    • Labella, F.S. and Paul, G. 1965. Structure of collagen from human tendon as influenced by age and sex. J. Gerontol. 20:54-59.
    • (1965) J. Gerontol. , vol.20 , pp. 54-59
    • Labella, F.S.1    Paul, G.2
  • 5
    • 0014690791 scopus 로고
    • The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis
    • Weber, K. and Osborn, M. 1969. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244:4406-4412.
    • (1969) J. Biol. Chem. , vol.244 , pp. 4406-4412
    • Weber, K.1    Osborn, M.2
  • 6
    • 0023259759 scopus 로고
    • Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes
    • Wolff, S.P. and Dean, R.T. 1987. Glucose autoxidation and protein modification. The potential role of 'autoxidative glycosylation' in diabetes. Biochem. J. 245:234-250.
    • (1987) Biochem. J. , vol.245 , pp. 234-250
    • Wolff, S.P.1    Dean, R.T.2
  • 7
    • 0023708392 scopus 로고
    • Hydroxyl radical production and autoxidative glycosylation: Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and aging
    • Hunt, J.V., Dean, R.T., and Wolff, S.P. 1988. Hydroxyl radical production and autoxidative glycosylation: glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and aging. Biochem. J. 256:205-212.
    • (1988) Biochem. J. , vol.256 , pp. 205-212
    • Hunt, J.V.1    Dean, R.T.2    Wolff, S.P.3
  • 8
    • 0014379086 scopus 로고
    • Practical methods for plasma lipoprotein analysis
    • Hatch, F.T. and Lees, R.S. 1968. Practical methods for plasma lipoprotein analysis. Adv. Lipid Res. 6:1-68.
    • (1968) Adv. Lipid Res. , vol.6 , pp. 1-68
    • Hatch, F.T.1    Lees, R.S.2
  • 9
    • 0022651365 scopus 로고
    • Use of a new methylene blue derivative for determination of lipid peroxides in food
    • Yagi, K., Kiuchi, K., Saito, Y., Miike, A., Kayahara, N., Tatano, T., and Ohihsi, N. 1986. Use of a new methylene blue derivative for determination of lipid peroxides in food. Biochem. Int. 12:367-371.
    • (1986) Biochem. Int. , vol.12 , pp. 367-371
    • Yagi, K.1    Kiuchi, K.2    Saito, Y.3    Miike, A.4    Kayahara, N.5    Tatano, T.6    Ohihsi, N.7
  • 10
    • 0001430544 scopus 로고
    • Accelerated age-related browning of human collagen in diabetes mellitus
    • Monnier, V.M., Khon, R.R., and Cerami, A. 1984. Accelerated age-related browning of human collagen in diabetes mellitus. Proc. Natl. Acad. Sci. USA. 81:583-587.
    • (1984) Proc. Natl. Acad. Sci. USA. , vol.81 , pp. 583-587
    • Monnier, V.M.1    Khon, R.R.2    Cerami, A.3
  • 11
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix
    • Sell, D.R. and Monnier, V.M. 1989. Structure elucidation of a senescence cross-link from human extracellular matrix. J. Biol. Chem. 264:21597-21602.
    • (1989) J. Biol. Chem. , vol.264 , pp. 21597-21602
    • Sell, D.R.1    Monnier, V.M.2
  • 12
    • 0026708910 scopus 로고
    • Crosslines A and B as candidates for the fluorophores in age-and diabetes-related cross-linked proteins, and their diacetates produced by Maillared reaction of a-N-acetyl-L-lysine with D-glucose
    • Nakamura, K. and Hasegawa, T. 1992. Crosslines A and B as candidates for the fluorophores in age-and diabetes-related cross-linked proteins, and their diacetates produced by Maillared reaction of a-N-acetyl-L-lysine with D-glucose. J. Chem. Soc. Chem. Commum. 14:992-994.
    • (1992) J. Chem. Soc. Chem. Commum. , vol.14 , pp. 992-994
    • Nakamura, K.1    Hasegawa, T.2
  • 13
    • 0024511940 scopus 로고
    • Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo
    • Hayase, F., Nagaraj, R.H., Miyata, S., Njoroge, G., and Monnier, V.M. 1989. Aging of proteins: Immunological detection of a glucose-derived pyrrole formed during Maillard reaction in vivo. J. Biol. Chem. 263:3758-3764.
    • (1989) J. Biol. Chem. , vol.263 , pp. 3758-3764
    • Hayase, F.1    Nagaraj, R.H.2    Miyata, S.3    Njoroge, G.4    Monnier, V.M.5
  • 14
    • 0022931516 scopus 로고
    • c-carboxymethyllysine as a degradation product of fructoselysine in glycated protein
    • c-carboxymethyllysine as a degradation product of fructoselysine in glycated protein. J. Biol. Chem. 261:4889-4894.
    • (1986) J. Biol. Chem. , vol.261 , pp. 4889-4894
    • Ahmed, M.U.1    Thorpe, S.R.2    Baynes, J.W.3
  • 15
    • 0032563120 scopus 로고    scopus 로고
    • Role of the Maillard reaction in aging of tissue proteins
    • Frye, E.B., Degenhardt, T.P., and Thorpe, S.R. 1998. Role of the Maillard reaction in aging of tissue proteins. J. Biol. Chem. 273:18714-18719.
    • (1998) J. Biol. Chem. , vol.273 , pp. 18714-18719
    • Frye, E.B.1    Degenhardt, T.P.2    Thorpe, S.R.3
  • 16
    • 0019796775 scopus 로고
    • Reaction of monosaccharides with proteins: Possible evolutionary significance
    • Bunn, H.F. and Higgins, P.J. 1981. Reaction of monosaccharides with proteins: Possible evolutionary significance. Science 213:222-224.
    • (1981) Science , vol.213 , pp. 222-224
    • Bunn, H.F.1    Higgins, P.J.2
  • 17
    • 0025055081 scopus 로고
    • Identification of fructose 3-phosphate in the lens of diabetic rats
    • Szwergold, B.S., Kappler, F., and Brown, T.R. 1990. Identification of fructose 3-phosphate in the lens of diabetic rats. Science 247:451-454.
    • (1990) Science , vol.247 , pp. 451-454
    • Szwergold, B.S.1    Kappler, F.2    Brown, T.R.3
  • 18
    • 85004247048 scopus 로고
    • Polymerization of proteins caused by reaction with sugars and the formation of 3-deoxyglucosone under physiological conditions
    • Shin, D.B., Hayase, F., and Kato, H. 1988. Polymerization of proteins caused by reaction with sugars and the formation of 3-deoxyglucosone under physiological conditions. Agric. Biol. Chem. 52:1451-1458.
    • (1988) Agric. Biol. Chem. , vol.52 , pp. 1451-1458
    • Shin, D.B.1    Hayase, F.2    Kato, H.3
  • 19
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-DG in the glycation of proteins
    • Thornalley, P.J., Langborg, A., and Minhas, H.S. 1999. Formation of glyoxal, methylglyoxal and 3-DG in the glycation of proteins. Biochem. J. 344:109-116.
    • (1999) Biochem. J. , vol.344 , pp. 109-116
    • Thornalley, P.J.1    Langborg, A.2    Minhas, H.S.3
  • 20
    • 0032892952 scopus 로고    scopus 로고
    • Implication of carbonyl stress in long term uraemic complications
    • Wada, T., Miyata, T., and Kurokawa, K. 1999. Implication of carbonyl stress in long term uraemic complications. Nephrol. Daial. Transplant. 14:79-81.
    • (1999) Nephrol. Daial. Transplant. , vol.14 , pp. 79-81
    • Wada, T.1    Miyata, T.2    Kurokawa, K.3
  • 21
    • 0030894411 scopus 로고    scopus 로고
    • Lipid and lipoprotein modification by AGE's: Role in atherosclerosis
    • Bucala, R. 1997. Lipid and lipoprotein modification by AGE's: role in atherosclerosis. Exp. Physiol. 82:327-337.
    • (1997) Exp. Physiol. , vol.82 , pp. 327-337
    • Bucala, R.1
  • 22
    • 0034616101 scopus 로고    scopus 로고
    • Selective vulnerability of spinal motor neurons to reactive dicabonyl compounds, intermediate products of glycation, in vitro: Implication of inefficient glutathione system in spinal motor neurons
    • Shinpo, K., Kikuchi, S., and Sasaki, H. 2000. Selective vulnerability of spinal motor neurons to reactive dicabonyl compounds, intermediate products of glycation, in vitro: implication of inefficient glutathione system in spinal motor neurons. Brain Res. 861:151-159.
    • (2000) Brain Res. , vol.861 , pp. 151-159
    • Shinpo, K.1    Kikuchi, S.2    Sasaki, H.3
  • 23
    • 0034032816 scopus 로고    scopus 로고
    • The importance of lipid-derived malondialdehyde in diabetes mellitus
    • Slatter, D.A., Bolton, C.H., and Bailey, A.J. 2000. The importance of lipid-derived malondialdehyde in diabetes mellitus. Diabetologia. 43:550-557.
    • (2000) Diabetologia. , vol.43 , pp. 550-557
    • Slatter, D.A.1    Bolton, C.H.2    Bailey, A.J.3
  • 24
    • 0022644227 scopus 로고
    • Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking
    • Brownlee, M., Vlassar, H., Kooney, A., Ulrich, P., and Cerami, A. 1986. Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 232:1629-1632.
    • (1986) Science , vol.232 , pp. 1629-1632
    • Brownlee, M.1    Vlassar, H.2    Kooney, A.3    Ulrich, P.4    Cerami, A.5
  • 25
    • 0031748727 scopus 로고    scopus 로고
    • Aminoguanidine inhibits reactive oxygen species formation, lipid peroxidation and oxidant induced apotosis
    • Giardino, I., Fard, A.K., and Brownlee, M. 1998. Aminoguanidine inhibits reactive oxygen species formation, lipid peroxidation and oxidant induced apotosis. Diabetes 47:1114-1120.
    • (1998) Diabetes , vol.47 , pp. 1114-1120
    • Giardino, I.1    Fard, A.K.2    Brownlee, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.