메뉴 건너뛰기




Volumn 5, Issue 1, 2015, Pages 194-222

Advanced glycation end products and oxidative stress in type 2 diabetes mellitus

Author keywords

Advanced glycation end products; Diabetic complications; Insulin resistance; Oxidative stress; Type 2 diabetes mellitus; cell dysfunction

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ALBUMIN; GLUCOSE; INSULIN RECEPTOR SUBSTRATE; PROTEIN KINASE C ALPHA; REACTIVE OXYGEN METABOLITE; SIRTUIN; TRANSCRIPTION FACTOR PDX 1; TUMOR NECROSIS FACTOR ALPHA;

EID: 85003053594     PISSN: None     EISSN: 2218273X     Source Type: Journal    
DOI: 10.3390/biom5010194     Document Type: Review
Times cited : (825)

References (167)
  • 1
    • 84928478008 scopus 로고    scopus 로고
    • International Diabetes Federation, 6th ed.; International Diabetes Federation: Brussels, Belgium
    • International Diabetes Federation. IDF Diabetes Atlas Update Poster, 6th ed.; International Diabetes Federation: Brussels, Belgium, 2014.
    • (2014) IDF Diabetes Atlas Update Poster
  • 2
    • 84968822322 scopus 로고    scopus 로고
    • International Diabetes Federation, 6th ed.; International Diabetes Federation: Brussels, Belgium
    • International Diabetes Federation. IDF Diabetes Atlas, 6th ed.; International Diabetes Federation: Brussels, Belgium, 2013.
    • (2013) IDF Diabetes Atlas
  • 3
    • 0034844049 scopus 로고    scopus 로고
    • Mortality and causes of death in the who multinational study of vascular disease in diabetes
    • Morrish, N.; Wang, S.-L.; Stevens, L.; Fuller, J.; Keen, H. Mortality and causes of death in the who multinational study of vascular disease in diabetes. Diabetologia 2001, 44, S14–S21.
    • (2001) Diabetologia , vol.44 , pp. S14-S21
    • Morrish, N.1    Wang, S.-L.2    Stevens, L.3    Fuller, J.4    Keen, H.5
  • 4
    • 84920903716 scopus 로고    scopus 로고
    • Oxidative stress: A concept in redox biology and medicine
    • Sies, H. Oxidative stress: A concept in redox biology and medicine. Redox Biol. 2015, 4, 180–183.
    • (2015) Redox Biol , vol.4 , pp. 180-183
    • Sies, H.1
  • 6
    • 78349297565 scopus 로고    scopus 로고
    • Oxidative stress and diabetic complications
    • Giacco, F.; Brownlee, M. Oxidative stress and diabetic complications. Circ. Res. 2010, 107, 1058–1070.
    • (2010) Circ. Res , vol.107 , pp. 1058-1070
    • Giacco, F.1    Brownlee, M.2
  • 7
    • 84904182953 scopus 로고    scopus 로고
    • Oxidative stress in type 2 diabetes mellitus
    • Miwa, S., Beckman, K., Muller, F., Eds. Humana Press: Totowa, NJ, USA
    • Abdul-Ghani, M.A.; DeFronzo, R.A. Oxidative stress in type 2 diabetes mellitus. In Oxidative stress in aging, Miwa, S., Beckman, K., Muller, F., Eds. Humana Press: Totowa, NJ, USA, 2008; pp. 191–211.
    • (2008) Oxidative Stress in Aging , pp. 191-211
    • Abdul-Ghani, M.A.1    Defronzo, R.A.2
  • 8
    • 80051669138 scopus 로고    scopus 로고
    • Oxidative stress and the etiology of insulin resistance and type 2 diabetes
    • Henriksen, E.J.; Diamond-Stanic, M.K.; Marchionne, E.M. Oxidative stress and the etiology of insulin resistance and type 2 diabetes. Free Radic. Biol. Med. 2011, 51, 993–999.
    • (2011) Free Radic. Biol. Med , vol.51 , pp. 993-999
    • Henriksen, E.J.1    Diamond-Stanic, M.K.2    Marchionne, E.M.3
  • 9
    • 19944390213 scopus 로고    scopus 로고
    • Pathogenesis of type 2 diabetes mellitus
    • Leahy, J.L. Pathogenesis of type 2 diabetes mellitus. Arch. Med. Res. 2005, 36, 197–209.
    • (2005) Arch. Med. Res , vol.36 , pp. 197-209
    • Leahy, J.L.1
  • 10
    • 84896736034 scopus 로고    scopus 로고
    • Advanced glycation end products (AGE) and diabetes: Cause, effect, or both?
    • Vlassara, H.; Uribarri, J. Advanced glycation end products (AGE) and diabetes: Cause, effect, or both? Curr. Diab. Rep. 2014, doi:10.1007/s11892-013-0453-1.
    • (2014) Curr. Diab. Rep
    • Vlassara, H.1    Uribarri, J.2
  • 11
    • 0014346452 scopus 로고
    • An abnormal hemoglobin in red cells of diabetics
    • Rahbar, S. An abnormal hemoglobin in red cells of diabetics. Clin. Chim. Acta 1968, 22, 296–298.
    • (1968) Clin. Chim. Acta , vol.22 , pp. 296-298
    • Rahbar, S.1
  • 12
    • 0016827223 scopus 로고
    • Further identification of the nature and linkage of the carbohydrate in hemoglobin A1c
    • Bunn, H.F.; Haney, D.N.; Gabbay, K.H.; Gallop, P.M. Further identification of the nature and linkage of the carbohydrate in hemoglobin A1c. Biochem. Biophys. Res. Commun. 1975, 67, 103–109.
    • (1975) Biochem. Biophys. Res. Commun , vol.67 , pp. 103-109
    • Bunn, H.F.1    Haney, D.N.2    Gabbay, K.H.3    Gallop, P.M.4
  • 13
    • 33947448299 scopus 로고
    • Dehydrated foods—Chemistry of browning reactions in model systems
    • Hodge, J.E. Dehydrated foods—Chemistry of browning reactions in model systems. J. Agric. Food Chem. 1953, 1, 928–943.
    • (1953) J. Agric. Food Chem , vol.1 , pp. 928-943
    • Hodge, J.E.1
  • 14
    • 0029923574 scopus 로고    scopus 로고
    • The advanced glycation end product, nepsilon-(Carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions
    • Fu, M.X.; Requena, J.R.; Jenkins, A.J.; Lyons, T.J.; Baynes, J.W.; Thorpe, S.R. The advanced glycation end product, nepsilon-(carboxymethyl)lysine, is a product of both lipid peroxidation and glycoxidation reactions. J. Biol. Chem. 1996, 271, 9982–9986.
    • (1996) J. Biol. Chem , vol.271 , pp. 9982-9986
    • Fu, M.X.1    Requena, J.R.2    Jenkins, A.J.3    Lyons, T.J.4    Baynes, J.W.5    Thorpe, S.R.6
  • 15
    • 0033571012 scopus 로고    scopus 로고
    • Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose
    • Thornalley, P.J.; Langborg, A.; Minhas, H.S. 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
  • 16
    • 0028951461 scopus 로고
    • Mechanism of autoxidative glycosylation: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose
    • Wells-Knecht, K.J.; Zyzak, D.V.; Litchfield, J.E.; Thorpe, S.R.; Baynes, J.W. Mechanism of autoxidative glycosylation: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose. Biochemistry 1995, 34, 3702–3709.
    • (1995) Biochemistry , vol.34 , pp. 3702-3709
    • Wells-Knecht, K.J.1    Zyzak, D.V.2    Litchfield, J.E.3    Thorpe, S.R.4    Baynes, J.W.5
  • 17
    • 84891459386 scopus 로고    scopus 로고
    • Quantification of glyoxal, methylglyoxal and 3-deoxyglucosone in blood and plasma by ultra performance liquid chromatography tandem mass spectrometry: Evaluation of blood specimen
    • Scheijen, J.L.; Schalkwijk, C.G. Quantification of glyoxal, methylglyoxal and 3-deoxyglucosone in blood and plasma by ultra performance liquid chromatography tandem mass spectrometry: Evaluation of blood specimen. Clin. Chem. Lab. Med. 2014, 52, 85–91.
    • (2014) Clin. Chem. Lab. Med. , vol.52 , pp. 85-91
    • Scheijen, J.L.1    Schalkwijk, C.G.2
  • 18
    • 0029124238 scopus 로고
    • Ne-carboxymethyllysine formation by direct addition of glyoxal to lysine during the maillard reaction
    • Al-Abed, Y.; Bucala, R. Ne-carboxymethyllysine formation by direct addition of glyoxal to lysine during the maillard reaction. Bioorg. Med. Chem. Lett. 1995, 5, 2161–2162.
    • (1995) Bioorg. Med. Chem. Lett , vol.5 , pp. 2161-2162
    • Al-Abed, Y.1    Bucala, R.2
  • 19
    • 0028867604 scopus 로고
    • Characterization of an imidazolium salt formed from glyoxal and N.Alpha.-hippuryllysine: A model for maillard reaction crosslinks in proteins
    • Wells-Knecht, K.J.; Brinkmann, E.; Baynes, J.W. Characterization of an imidazolium salt formed from glyoxal and N.alpha.-hippuryllysine: A model for maillard reaction crosslinks in proteins. J. Org. Chem. 1995, 60, 6246–6247.
    • (1995) J. Org. Chem. , vol.60 , pp. 6246-6247
    • Wells-Knecht, K.J.1    Brinkmann, E.2    Baynes, J.W.3
  • 20
    • 0034826534 scopus 로고    scopus 로고
    • Isolation and characterization of glyoxal-arginine modifications
    • Glomb, M.A.; Lang, G. Isolation and characterization of glyoxal-arginine modifications. J. Agric. Food Chem. 2001, 49, 1493–1501.
    • (2001) J. Agric. Food Chem , vol.49 , pp. 1493-1501
    • Glomb, M.A.1    Lang, G.2
  • 21
    • 0346731073 scopus 로고    scopus 로고
    • Maillard reaction products in tissue proteins: New products and new perspectives
    • Thorpe, S.R.; Baynes, J.W. Maillard reaction products in tissue proteins: New products and new perspectives. Amino Acids 2003, 25, 275–281.
    • (2003) Amino Acids , vol.25 , pp. 275-281
    • Thorpe, S.R.1    Baynes, J.W.2
  • 22
    • 0030919275 scopus 로고    scopus 로고
    • N-epsilon-(Carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with AGE in human lens proteins
    • Ahmed, M.U.; Brinkmann Frye, E.; Degenhardt, T.P.; Thorpe, S.R.; Baynes, J.W. N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with AGE in human lens proteins. Biochem. J. 1997, 324, 565–570.
    • (1997) Biochem. J , vol.324 , pp. 565-570
    • Ahmed, M.U.1    Brinkmann Frye, E.2    Degenhardt, T.P.3    Thorpe, S.R.4    Baynes, J.W.5
  • 23
    • 0029760932 scopus 로고    scopus 로고
    • Protein cross-linking by the maillard reaction: Isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal
    • 19338–19345
    • Nagaraj, R.H.; Shipanova, I.N.; Faust, F.M. Protein cross-linking by the maillard reaction: Isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal. J. Biol. Chem. 1996, 271, 19338–19345.
    • (1996) J. Biol. Chem , vol.271
    • Nagaraj, R.H.1    Shipanova, I.N.2    Faust, F.M.3
  • 24
    • 0031214523 scopus 로고    scopus 로고
    • Protein modification by methylglyoxal: Chemical nature and synthetic mechanism of a major fluorescent adduct
    • Shipanova, I.N.; Glomb, M.A.; Nagaraj, R.H. Protein modification by methylglyoxal: Chemical nature and synthetic mechanism of a major fluorescent adduct. Arch. Biochem. Biophys. 1997, 344, 29–36.
    • (1997) Arch. Biochem. Biophys , vol.344 , pp. 29-36
    • Shipanova, I.N.1    Glomb, M.A.2    Nagaraj, R.H.3
  • 25
    • 0003039181 scopus 로고
    • Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal
    • Henle, T.; Walter, A.; Haeßner, R.; Klostermeyer, H. Detection and identification of a protein-bound imidazolone resulting from the reaction of arginine residues and methylglyoxal. Z. Lebensm. Unters. Forsch. 1994, 199, 55–58.
    • (1994) Z. Lebensm. Unters. Forsch , vol.199 , pp. 55-58
    • Henle, T.1    Walter, A.2    Haeßner, R.3    Klostermeyer, H.4
  • 26
    • 0028908842 scopus 로고
    • Chromatographic evidence for pyrraline formation during protein glycation in vitro and in vivo
    • Portero-Otin, M.; Nagaraj, R.H.; Monnier, V.M. Chromatographic evidence for pyrraline formation during protein glycation in vitro and in vivo. Biochim. Biophys. Acta 1995, 1247, 74–80.
    • (1995) Biochim. Biophys. Acta , vol.1247 , pp. 74-80
    • Portero-Otin, M.1    Nagaraj, R.H.2    Monnier, V.M.3
  • 27
    • 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
    • 11654–11660
    • Dyer, D.; Blackledge, J.; Thorpe, S.; Baynes, J. 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
    • Dyer, D.1    Blackledge, J.2    Thorpe, S.3    Baynes, J.4
  • 28
    • 9144228074 scopus 로고    scopus 로고
    • Ne-(Carboxymethyl) lysine and 3-DG-imidazolone are major AGE structures in protein modification by 3-deoxyglucosone
    • Jono, T.; Nagai, R.; Lin, X.; Ahmed, N.; Thornalley, P.J.; Takeya, M.; Horiuchi, S. Ne-(carboxymethyl) lysine and 3-DG-imidazolone are major AGE structures in protein modification by 3-deoxyglucosone. J. Biochem. 2004, 136, 351–358.
    • (2004) J. Biochem , vol.136 , pp. 351-358
    • Jono, T.1    Nagai, R.2    Lin, X.3    Ahmed, N.4    Thornalley, P.J.5    Takeya, M.6    Horiuchi, S.7
  • 29
    • 0035135246 scopus 로고    scopus 로고
    • Advanced glycation end-products: A review
    • Singh, R.; Barden, A.; Mori, T.; Beilin, L. Advanced glycation end-products: A review. Diabetologia 2001, 44, 129–146.
    • (2001) Diabetologia , vol.44 , pp. 129-146
    • Singh, R.1    Barden, A.2    Mori, T.3    Beilin, L.4
  • 30
    • 0025732948 scopus 로고
    • Role of oxidative stress in development of complications in diabetes
    • Baynes, J.W. Role of oxidative stress in development of complications in diabetes. Diabetes 1991, 40, 405–412.
    • (1991) Diabetes , vol.40 , pp. 405-412
    • Baynes, J.W.1
  • 31
    • 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
  • 32
    • 0001112738 scopus 로고
    • Aging of proteins: Isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose
    • Pongor, S.; Ulrich, P.C.; Bencsath, F.A.; Cerami, A. Aging of proteins: Isolation and identification of a fluorescent chromophore from the reaction of polypeptides with glucose. Proc. Natl. Acad. Sci. USA 1984, 81, 2684–2688.
    • (1984) Proc. Natl. Acad. Sci. USA , vol.81 , pp. 2684-2688
    • Pongor, S.1    Ulrich, P.C.2    Bencsath, F.A.3    Cerami, A.4
  • 33
    • 0024852380 scopus 로고
    • Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process
    • 21597–21602
    • 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. 1989, 264, 21597–21602.
    • (1989) J. Biol. Chem , vol.264
    • Sell, D.R.1    Monnier, V.M.2
  • 35
    • 0032822303 scopus 로고    scopus 로고
    • Serum levels of advanced glycation end products are increased in patients with type 2 diabetes and coronary heart disease
    • Kilhovd, B.K.; Berg, T.J.; Birkeland, K.I.; Thorsby, P.; Hanssen, K.F. Serum levels of advanced glycation end products are increased in patients with type 2 diabetes and coronary heart disease. Diabetes Care 1999, 22, 1543–1548.
    • (1999) Diabetes Care , vol.22 , pp. 1543-1548
    • Kilhovd, B.K.1    Berg, T.J.2    Birkeland, K.I.3    Thorsby, P.4    Hanssen, K.F.5
  • 36
    • 0030763201 scopus 로고    scopus 로고
    • Increased accumulation of the glycoxidation product N(Epsilon)-(carboxymethyl) lysine in human tissues in diabetes and aging
    • Schleicher, E.D.; Wagner, E.; Nerlich, A.G. Increased accumulation of the glycoxidation product N(epsilon)-(carboxymethyl) lysine in human tissues in diabetes and aging. J. Clin. Investig. 1997, 99, 457–468.
    • (1997) J. Clin. Investig. , vol.99 , pp. 457-468
    • Schleicher, E.D.1    Wagner, E.2    Nerlich, A.G.3
  • 37
    • 2942692013 scopus 로고    scopus 로고
    • Increased accumulation of the glycoxidation product Ne-(Carboxymethyl)lysine in hearts of diabetic patients: Generation and characterisation of a monoclonal anti-CML antibody
    • Schalkwijk, C.G.; Baidoshvili, A.; Stehouwer, C.D.A.; van Hinsbergh, V.W.M.; Niessen, H.W.M. Increased accumulation of the glycoxidation product Ne-(carboxymethyl)lysine in hearts of diabetic patients: Generation and characterisation of a monoclonal anti-CML antibody. Biochim. Biophys. Acta 2004, 1636, 82–89.
    • (2004) Biochim. Biophys. Acta , vol.1636 , pp. 82-89
    • Schalkwijk, C.G.1    Baidoshvili, A.2    Stehouwer, C.3    Van Hinsbergh, V.4    Niessen, H.5
  • 39
    • 0027451507 scopus 로고
    • Differential effects of type 2 (Non-insulin dependent) diabetes mellitus on pentosidine formation in skin and glomerular basement membrane
    • Sell, D.R.; Carlson, E.C.; Monnier, V.M. Differential effects of type 2 (non-insulin dependent) diabetes mellitus on pentosidine formation in skin and glomerular basement membrane. Diabetologia 1993, 36, 936–941.
    • (1993) Diabetologia , vol.36 , pp. 936-941
    • Sell, D.R.1    Carlson, E.C.2    Monnier, V.M.3
  • 40
    • 0037067723 scopus 로고    scopus 로고
    • Identification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound
    • Biemel, K.M.; Friedl, D.A.; Lederer, M.O. Identification and quantification of major maillard cross-links in human serum albumin and lens protein. Evidence for glucosepane as the dominant compound. J. Biol. Chem. 2002, 277, 24907–24915.
    • (2002) J. Biol. Chem , vol.277 , pp. 24907-24915
    • Biemel, K.M.1    Friedl, D.A.2    Lederer, M.O.3
  • 41
    • 16844380283 scopus 로고    scopus 로고
    • Glucosepane is a major protein cross-link of the senescent human extracellular matrix. Relationship with diabetes
    • Sell, D.R.; Biemel, K.M.; Reihl, O.; Lederer, M.O.; Strauch, C.M.; Monnier, V.M. Glucosepane is a major protein cross-link of the senescent human extracellular matrix. Relationship with diabetes. J. Biol. Chem. 2005, 280, 12310–12315.
    • (2005) J. Biol. Chem , vol.280 , pp. 12310-12315
    • Sell, D.R.1    Biemel, K.M.2    Reihl, O.3    Lederer, M.O.4    Strauch, C.M.5    Monnier, V.M.6
  • 42
    • 23744467295 scopus 로고    scopus 로고
    • Glycation products as markers and predictors of the progression of diabetic complications
    • Monnier, V.M.; Sell, D.R.; Genuth, S. Glycation products as markers and predictors of the progression of diabetic complications. Ann. NY Acad. Sci. 2005, 1043, 567–581.
    • (2005) Ann. NY Acad. Sci , vol.1043 , pp. 567-581
    • Monnier, V.M.1    Sell, D.R.2    Genuth, S.3
  • 44
    • 59449086530 scopus 로고    scopus 로고
    • Determination of Ne-(Carboxymethyl)lysine in food systems by ultra performance liquid chromatography-mass spectrometry
    • Assar, S.; Moloney, C.; Lima, M.; Magee, R.; Ames, J. Determination of Ne-(carboxymethyl)lysine in food systems by ultra performance liquid chromatography-mass spectrometry. Amino Acids 2009, 36, 317–326.
    • (2009) Amino Acids , vol.36 , pp. 317-326
    • Assar, S.1    Moloney, C.2    Lima, M.3    Magee, R.4    Ames, J.5
  • 45
    • 0037406409 scopus 로고    scopus 로고
    • AGEs in foods: Do they play a role in uremia?
    • Henle, T. AGEs in foods: Do they play a role in uremia? Kidney Int. Suppl. 2003, S145–S147.
    • (2003) Kidney Int. Suppl , pp. S145-S147
    • Henle, T.1
  • 47
    • 84864748556 scopus 로고    scopus 로고
    • Study of the urinary and faecal excretion of nepsilon-carboxymethyllysine in young human volunteers
    • Delgado-Andrade, C.; Tessier, F.J.; Niquet-Leridon, C.; Seiquer, I.; Pilar Navarro, M. Study of the urinary and faecal excretion of nepsilon-carboxymethyllysine in young human volunteers. Amino Acids 2012, 43, 595–602.
    • (2012) Amino Acids , vol.43 , pp. 595-602
    • Delgado-Andrade, C.1    Tessier, F.J.2    Niquet-Leridon, C.3    Seiquer, I.4    Pilar Navarro, M.5
  • 49
    • 0037369890 scopus 로고    scopus 로고
    • Restriction of dietary glycotoxins reduces excessive advanced glycation end products in renal failure patients
    • Uribarri, J.; Peppa, M.; Cai, W.; Goldberg, T.; Lu, M.; He, C.; Vlassara, H. Restriction of dietary glycotoxins reduces excessive advanced glycation end products in renal failure patients. J. Am. Soc. Nephrol. 2003, 14, 728–731.
    • (2003) J. Am. Soc. Nephrol , vol.14 , pp. 728-731
    • Uribarri, J.1    Peppa, M.2    Cai, W.3    Goldberg, T.4    Lu, M.5    He, C.6    Vlassara, H.7
  • 50
    • 80052142793 scopus 로고    scopus 로고
    • Restriction of advanced glycation end products improves insulin resistance in human type 2 diabetes: Potential role of AGER1 and SIRT1
    • Uribarri, J.; Cai, W.; Ramdas, M.; Goodman, S.; Pyzik, R.; Chen, X.; Zhu, L.; Striker, G.E.; Vlassara, H. Restriction of advanced glycation end products improves insulin resistance in human type 2 diabetes: Potential role of AGER1 and SIRT1. Diabetes Care 2011, 34, 1610–1616.
    • (2011) Diabetes Care , vol.34 , pp. 1610-1616
    • Uribarri, J.1    Cai, W.2    Ramdas, M.3    Goodman, S.4    Pyzik, R.5    Chen, X.6    Zhu, L.7    Striker, G.E.8    Vlassara, H.9
  • 51
    • 34250327529 scopus 로고    scopus 로고
    • Circulating glycotoxins and dietary advanced glycation endproducts: Two links to inflammatory response, oxidative stress, and aging
    • Uribarri, J.; Cai, W.; Peppa, M.; Goodman, S.; Ferrucci, L.; Striker, G.; Vlassara, H. Circulating glycotoxins and dietary advanced glycation endproducts: Two links to inflammatory response, oxidative stress, and aging. J. Gerontol. Ser. A Biol. Sci. Med. Sci. 2007, 62, 427–433.
    • (2007) J. Gerontol. Ser. A Biol. Sci. Med. Sci , vol.62 , pp. 427-433
    • Uribarri, J.1    Cai, W.2    Peppa, M.3    Goodman, S.4    Ferrucci, L.5    Striker, G.6    Vlassara, H.7
  • 52
    • 84866839740 scopus 로고    scopus 로고
    • Oral advanced glycation endproducts (AGEs) promote insulin resistance and diabetes by depleting the antioxidant defenses AGE receptor-1 and Sirtuin 1
    • 15888–15893
    • Cai, W.; Ramdas, M.; Zhu, L.; Chen, X.; Striker, G.E.; Vlassara, H. Oral advanced glycation endproducts (AGEs) promote insulin resistance and diabetes by depleting the antioxidant defenses AGE receptor-1 and Sirtuin 1. Proc. Natl. Acad. Sci. USA 2012, 109, 15888–15893.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109
    • Cai, W.1    Ramdas, M.2    Zhu, L.3    Chen, X.4    Striker, G.E.5    Vlassara, H.6
  • 54
    • 0033603241 scopus 로고    scopus 로고
    • RAGE mediates a novel proinflammatory axis: A central cell surface receptor for S100/calgranulin polypeptides
    • Hofmann, M.A.; Drury, S.; Fu, C.; Qu, W.; Taguchi, A.; Lu, Y.; Avila, C.; Kambham, N.; Bierhaus, A.; Nawroth, P.; et al. RAGE mediates a novel proinflammatory axis: A central cell surface receptor for S100/calgranulin polypeptides. Cell 1999, 97, 889–901.
    • (1999) Cell , vol.97 , pp. 889-901
    • Hofmann, M.A.1    Drury, S.2    Fu, C.3    Qu, W.4    Taguchi, A.5    Lu, Y.6    Avila, C.7    Kambham, N.8    Bierhaus, A.9    Nawroth, P.10
  • 55
    • 0028851635 scopus 로고
    • The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of RAGE and amphoterin in the developing nervous system
    • 25752–25761
    • Hori, O.; Brett, J.; Slattery, T.; Cao, R.; Zhang, J.; Chen, J.X.; Nagashima, M.; Lundh, E.R.; Vijay, S.; Nitecki, D.; et al. The receptor for advanced glycation end products (RAGE) is a cellular binding site for amphoterin. Mediation of neurite outgrowth and co-expression of RAGE and amphoterin in the developing nervous system. J. Biol. Chem. 1995, 270, 25752–25761.
    • (1995) J. Biol. Chem. , vol.270
    • Hori, O.1    Brett, J.2    Slattery, T.3    Cao, R.4    Zhang, J.5    Chen, J.X.6    Nagashima, M.7    Lundh, E.R.8    Vijay, S.9    Nitecki, D.10
  • 56
  • 57
    • 84867757240 scopus 로고    scopus 로고
    • Advanced-glycation-endproduct- induced formation of immunoproteasomes: Involvement of RAGE and Jak2/Stat1
    • Grimm, S.; Ott, C.; Horlacher, M.; Weber, D.; Hohn, A.; Grune, T. Advanced-glycation-endproduct- induced formation of immunoproteasomes: Involvement of RAGE and Jak2/Stat1. Biochem. J. 2012, 448, 127–139.
    • (2012) Biochem. J. , vol.448 , pp. 127-139
    • Grimm, S.1    Ott, C.2    Horlacher, M.3    Weber, D.4    Hohn, A.5    Grune, T.6
  • 58
    • 71549141594 scopus 로고    scopus 로고
    • Advanced glycation end products increase endothelial permeability through the RAGE/Rho signaling pathway
    • Hirose, A.; Tanikawa, T.; Mori, H.; Okada, Y.; Tanaka, Y. Advanced glycation end products increase endothelial permeability through the RAGE/Rho signaling pathway. FEBS Lett. 2010, 584, 61–66.
    • (2010) FEBS Lett , vol.584 , pp. 61-66
    • Hirose, A.1    Tanikawa, T.2    Mori, H.3    Okada, Y.4    Tanaka, Y.5
  • 59
    • 67649447069 scopus 로고    scopus 로고
    • Advanced glycation end products induce calcification of vascular smooth muscle cells through RAGE/p38 mapk
    • Tanikawa, T.; Okada, Y.; Tanikawa, R.; Tanaka, Y. Advanced glycation end products induce calcification of vascular smooth muscle cells through RAGE/p38 mapk. J. Vasc. Res. 2009, 46, 572–580.
    • (2009) J. Vasc. Res , vol.46 , pp. 572-580
    • Tanikawa, T.1    Okada, Y.2    Tanikawa, R.3    Tanaka, Y.4
  • 60
    • 1642336325 scopus 로고    scopus 로고
    • Advanced glycation end products induce tubular epithelial-myofibroblast transition through the RAGE-ERK1/2 MAP kinase signaling pathway
    • Li, J.H.; Wang, W.; Huang, X.R.; Oldfield, M.; Schmidt, A.M.; Cooper, M.E.; Lan, H.Y. Advanced glycation end products induce tubular epithelial-myofibroblast transition through the RAGE-ERK1/2 MAP kinase signaling pathway. Am. J. Pathol. 2004, 164, 1389–1397.
    • (2004) Am. J. Pathol , vol.164 , pp. 1389-1397
    • Li, J.H.1    Wang, W.2    Huang, X.R.3    Oldfield, M.4    Schmidt, A.M.5    Cooper, M.E.6    Lan, H.Y.7
  • 61
    • 77249116145 scopus 로고    scopus 로고
    • Advanced glycation end products induce production of reactive oxygen species via the activation of NADPH oxidase in murine hepatic stellate cells
    • Guimaraes, E.L.; Empsen, C.; Geerts, A.; van Grunsven, L.A. Advanced glycation end products induce production of reactive oxygen species via the activation of NADPH oxidase in murine hepatic stellate cells. J. Hepatol. 2010, 52, 389–397.
    • (2010) J. Hepatol , vol.52 , pp. 389-397
    • Guimaraes, E.L.1    Empsen, C.2    Geerts, A.3    Van Grunsven, L.A.4
  • 62
    • 33645524328 scopus 로고    scopus 로고
    • Glycated proteins stimulate reactive oxygen species production in cardiac myocytes: Involvement of Nox2 (gp91phox)-containing NADPH oxidase
    • Zhang, M.; Kho, A.L.; Anilkumar, N.; Chibber, R.; Pagano, P.J.; Shah, A.M.; Cave, A.C. Glycated proteins stimulate reactive oxygen species production in cardiac myocytes: Involvement of Nox2 (gp91phox)-containing NADPH oxidase. Circulation 2006, 113, 1235–1243.
    • (2006) Circulation , vol.113 , pp. 1235-1243
    • Zhang, M.1    Kho, A.L.2    Anilkumar, N.3    Chibber, R.4    Pagano, P.J.5    Shah, A.M.6    Cave, A.C.7
  • 64
    • 0025343895 scopus 로고
    • Activation of interleukin-6 gene expression through the NF-κB transcription factor
    • Libermann, T.A.; Baltimore, D. Activation of interleukin-6 gene expression through the NF-κB transcription factor. Mol. Cell. Biol. 1990, 10, 2327–2334.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 2327-2334
    • Libermann, T.A.1    Baltimore, D.2
  • 65
    • 0030707615 scopus 로고    scopus 로고
    • Transcriptional regulation of the human monocyte chemoattractant protein-1 gene: Cooperation of two NF-κB sites and NF-κB/Rel subunit specificity
    • 31092–31099
    • Ueda, A.; Ishigatsubo, Y.; Okubo, T.; Yoshimura, T. Transcriptional regulation of the human monocyte chemoattractant protein-1 gene: Cooperation of two NF-κB sites and NF-κB/Rel subunit specificity. J. Biol. Chem. 1997, 272, 31092–31099.
    • (1997) J. Biol. Chem , vol.272
    • Ueda, A.1    Ishigatsubo, Y.2    Okubo, T.3    Yoshimura, T.4
  • 66
    • 0030910830 scopus 로고    scopus 로고
    • Characterization and functional analysis of the promoter of RAGE, the receptor for advanced glycation end products
    • 16498–16506
    • Li, J.; Schmidt, A.M. Characterization and functional analysis of the promoter of RAGE, the receptor for advanced glycation end products. J. Biol. Chem. 1997, 272, 16498–16506.
    • (1997) J. Biol. Chem , vol.272
    • Li, J.1    Schmidt, A.M.2
  • 69
    • 84857233918 scopus 로고    scopus 로고
    • Cathepsins D and L reduce the toxicity of advanced glycation end products. Free Radic
    • Grimm, S.; Horlacher, M.; Catalgol, B.; Hoehn, A.; Reinheckel, T.; Grune, T. Cathepsins D and L reduce the toxicity of advanced glycation end products. Free Radic. Biol. Med. 2012, 52, 1011–1023.
    • (2012) Biol. Med , vol.52 , pp. 1011-1023
    • Grimm, S.1    Horlacher, M.2    Catalgol, B.3    Hoehn, A.4    Reinheckel, T.5    Grune, T.6
  • 70
    • 77749264564 scopus 로고    scopus 로고
    • AGER1 regulates endothelial cell NADPH oxidase-dependent oxidant stress via PKC-delta: Implications for vascular disease
    • Cai, W.; Torreggiani, M.; Zhu, L.; Chen, X.; He, J.C.; Striker, G.E.; Vlassara, H. AGER1 regulates endothelial cell NADPH oxidase-dependent oxidant stress via PKC-delta: Implications for vascular disease. Am. J. Physiol. Cell Physiol. 2010, 298, C624–C634.
    • (2010) Am. J. Physiol. Cell Physiol , vol.298 , pp. C624-C634
    • Cai, W.1    Torreggiani, M.2    Zhu, L.3    Chen, X.4    He, J.C.5    Striker, G.E.6    Vlassara, H.7
  • 71
    • 4143087382 scopus 로고    scopus 로고
    • Advanced glycation endproduct (AGE) receptor 1 is a negative regulator of the inflammatory response to AGE in mesangial cells
    • Lu, C.; He, J.C.; Cai, W.; Liu, H.; Zhu, L.; Vlassara, H. Advanced glycation endproduct (AGE) receptor 1 is a negative regulator of the inflammatory response to AGE in mesangial cells. Proc. Natl. Acad. Sci. USA 2004, 101, 11767–11772.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 11767-11772
    • Lu, C.1    He, J.C.2    Cai, W.3    Liu, H.4    Zhu, L.5    Vlassara, H.6
  • 72
    • 70449131003 scopus 로고    scopus 로고
    • Protection against loss of innate defenses in adulthood by low advanced glycation end products (AGE) intake: Role of the antiinflammatory AGE receptor-1
    • Vlassara, H.; Cai, W.; Goodman, S.; Pyzik, R.; Yong, A.; Chen, X.; Zhu, L.; Neade, T.; Beeri, M.; Silverman, J.M.; et al. Protection against loss of innate defenses in adulthood by low advanced glycation end products (AGE) intake: Role of the antiinflammatory AGE receptor-1. J. Clin. Endocrinol. Metab. 2009, 94, 4483–4491.
    • (2009) J. Clin. Endocrinol. Metab. , vol.94 , pp. 4483-4491
    • Vlassara, H.1    Cai, W.2    Goodman, S.3    Pyzik, R.4    Yong, A.5    Chen, X.6    Zhu, L.7    Neade, T.8    Beeri, M.9    Silverman, J.M.10
  • 73
    • 73549096880 scopus 로고    scopus 로고
    • Advanced glycation end product receptor-1 transgenic mice are resistant to inflammation, oxidative stress, and post-injury intimal hyperplasia
    • Torreggiani, M.; Liu, H.; Wu, J.; Zheng, F.; Cai, W.; Striker, G.; Vlassara, H. Advanced glycation end product receptor-1 transgenic mice are resistant to inflammation, oxidative stress, and post-injury intimal hyperplasia. Am. J. Pathol. 2009, 175, 1722–1732.
    • (2009) Am. J. Pathol , vol.175 , pp. 1722-1732
    • Torreggiani, M.1    Liu, H.2    Wu, J.3    Zheng, F.4    Cai, W.5    Striker, G.6    Vlassara, H.7
  • 74
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • Zimmet, P.; Alberti, K.G.M.M.; Shaw, J. Global and societal implications of the diabetes epidemic. Nature 2001, 414, 782–787.
    • (2001) Nature , vol.414 , pp. 782-787
    • Zimmet, P.1    Alberti, K.2    Shaw, J.3
  • 75
    • 79960159996 scopus 로고    scopus 로고
    • Serum advanced glycation end products (AGEs) are associated with insulin resistance
    • Tan, K.C.; Shiu, S.W.; Wong, Y.; Tam, X. Serum advanced glycation end products (AGEs) are associated with insulin resistance. Diabetes Metab. Res. Rev. 2011, 27, 488–492.
    • (2011) Diabetes Metab. Res. Rev , vol.27 , pp. 488-492
    • Tan, K.C.1    Shiu, S.W.2    Wong, Y.3    Tam, X.4
  • 76
    • 0021813187 scopus 로고
    • Homeostasis model assessment: Insulin resistance and b-cell function from fasting plasma glucose and insulin concentrations in man
    • Matthews, D.; Hosker, J.; Rudenski, A.; Naylor, B.; Treacher, D.; Turner, R. Homeostasis model assessment: Insulin resistance and b-cell function from fasting plasma glucose and insulin concentrations in man. Diabetologia 1985, 28, 412–419.
    • (1985) Diabetologia , vol.28 , pp. 412-419
    • Matthews, D.1    Hosker, J.2    Rudenski, A.3    Naylor, B.4    Treacher, D.5    Turner, R.6
  • 77
    • 84856252632 scopus 로고    scopus 로고
    • Serum levels of advanced glycation end products (AGEs) are independent correlates of insulin resistance in nondiabetic subjects
    • Tahara, N.; Yamagishi, S.; Matsui, T.; Takeuchi, M.; Nitta, Y.; Kodama, N.; Mizoguchi, M.; Imaizumi, T. Serum levels of advanced glycation end products (AGEs) are independent correlates of insulin resistance in nondiabetic subjects. Cardiovasc. Ther. 2012, 30, 42–48.
    • (2012) Cardiovasc. Ther , vol.30 , pp. 42-48
    • Tahara, N.1    Yamagishi, S.2    Matsui, T.3    Takeuchi, M.4    Nitta, Y.5    Kodama, N.6    Mizoguchi, M.7    Imaizumi, T.8
  • 78
    • 0035025782 scopus 로고    scopus 로고
    • Tumor necrosis factor-alpha is induced through phorbol ester—And glycated human albumin-dependent pathway in Thp-1 cells
    • Naitoh, T.; Kitahara, M.; Tsuruzoe, N. Tumor necrosis factor-alpha is induced through phorbol ester—And glycated human albumin-dependent pathway in Thp-1 cells. Cell Signal. 2001, 13, 331–334.
    • (2001) Cell Signal , vol.13 , pp. 331-334
    • Naitoh, T.1    Kitahara, M.2    Tsuruzoe, N.3
  • 79
    • 0346850870 scopus 로고    scopus 로고
    • Human glycated albumin affects glucose metabolism in l6 skeletal muscle cells by impairing insulin-induced insulin receptor substrate (IRS) signaling through a protein kinase C alpha-mediated mechanism
    • Miele, C.; Riboulet, A.; Maitan, M.A.; Oriente, F.; Romano, C.; Formisano, P.; Giudicelli, J.; Beguinot, F.; van Obberghen, E. Human glycated albumin affects glucose metabolism in l6 skeletal muscle cells by impairing insulin-induced insulin receptor substrate (IRS) signaling through a protein kinase C alpha-mediated mechanism. J. Biol. Chem. 2003, 278, 47376–47387.
    • (2003) J. Biol. Chem , vol.278 , pp. 47376-47387
    • Miele, C.1    Riboulet, A.2    Maitan, M.A.3    Oriente, F.4    Romano, C.5    Formisano, P.6    Giudicelli, J.7    Beguinot, F.8    Van Obberghen, E.9
  • 80
    • 61349095437 scopus 로고    scopus 로고
    • In skeletal muscle advanced glycation end products (AGEs) inhibit insulin action and induce the formation of multimolecular complexes including the receptor for AGEs
    • 36088–36099
    • Cassese, A.; Esposito, I.; Fiory, F.; Barbagallo, A.P.; Paturzo, F.; Mirra, P.; Ulianich, L.; Giacco, F.; Iadicicco, C.; Lombardi, A.; et al. In skeletal muscle advanced glycation end products (AGEs) inhibit insulin action and induce the formation of multimolecular complexes including the receptor for AGEs. J. Biol. Chem. 2008, 283, 36088–36099.
    • (2008) J. Biol. Chem. , vol.283
    • Cassese, A.1    Esposito, I.2    Fiory, F.3    Barbagallo, A.P.4    Paturzo, F.5    Mirra, P.6    Ulianich, L.7    Giacco, F.8    Iadicicco, C.9    Lombardi, A.10
  • 81
    • 4243150843 scopus 로고    scopus 로고
    • The role of TNF-a in insulin resistance
    • Borst, S. The role of TNF-a in insulin resistance. Endocrine 2004, 23, 177–182.
    • (2004) Endocrine , vol.23 , pp. 177-182
    • Borst, S.1
  • 82
    • 0034617286 scopus 로고    scopus 로고
    • Selective attenuation of metabolic branch of insulin receptor down-signaling by high glucose in a hepatoma cell line, Hepg2 cells
    • 20880–20886
    • Nakajima, K.; Yamauchi, K.; Shigematsu, S.; Ikeo, S.; Komatsu, M.; Aizawa, T.; Hashizume, K. Selective attenuation of metabolic branch of insulin receptor down-signaling by high glucose in a hepatoma cell line, Hepg2 cells. J. Biol. Chem. 2000, 275, 20880–20886.
    • (2000) J. Biol. Chem , vol.275
    • Nakajima, K.1    Yamauchi, K.2    Shigematsu, S.3    Ikeo, S.4    Komatsu, M.5    Aizawa, T.6    Hashizume, K.7
  • 83
    • 0035793592 scopus 로고    scopus 로고
    • Protein kinase c-z phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin
    • Ravichandran, L.V.; Esposito, D.L.; Chen, J.; Quon, M.J. Protein kinase c-z phosphorylates insulin receptor substrate-1 and impairs its ability to activate phosphatidylinositol 3-kinase in response to insulin. J. Biol. Chem. 2001, 276, 3543–3549.
    • (2001) J. Biol. Chem , vol.276 , pp. 3543-3549
    • Ravichandran, L.V.1    Esposito, D.L.2    Chen, J.3    Quon, M.J.4
  • 84
    • 0034283354 scopus 로고    scopus 로고
    • Impaired ability of glycated insulin to regulate plasma glucose and stimulate glucose transport and metabolism in mouse abdominal muscle
    • Boyd, A.C.; Abdel-Wahab, Y.H.; McKillop, A.M.; McNulty, H.; Barnett, C.R.; O’Harte, F.P.; Flatt, P.R. Impaired ability of glycated insulin to regulate plasma glucose and stimulate glucose transport and metabolism in mouse abdominal muscle. Biochim. Biophys. Acta 2000, 1523, 128–134.
    • (2000) Biochim. Biophys. Acta , vol.1523 , pp. 128-134
    • Boyd, A.C.1    Abdel-Wahab, Y.H.2    McKillop, A.M.3    McNulty, H.4    Barnett, C.R.5    O’Harte, F.P.6    Flatt, P.R.7
  • 85
    • 0037312856 scopus 로고    scopus 로고
    • Demonstration of glycated insulin in human diabetic plasma and decreased biological activity assessed by euglycemic-hyperinsulinemic clamp technique in humans
    • Hunter, S.J.; Boyd, A.C.; O’Harte, F.P.; McKillop, A.M.; Wiggam, M.I.; Mooney, M.H.; McCluskey, J.T.; Lindsay, J.R.; Ennis, C.N.; Gamble, R.; et al. Demonstration of glycated insulin in human diabetic plasma and decreased biological activity assessed by euglycemic-hyperinsulinemic clamp technique in humans. Diabetes 2003, 52, 492–498.
    • (2003) Diabetes , vol.52 , pp. 492-498
    • Hunter, S.J.1    Boyd, A.C.2    O’Harte, F.P.3    McKillop, A.M.4    Wiggam, M.I.5    Mooney, M.H.6    McCluskey, J.T.7    Lindsay, J.R.8    Ennis, C.N.9    Gamble, R.10
  • 86
    • 33845677195 scopus 로고    scopus 로고
    • Structural and functional changes in human insulin induced by methylglyoxal
    • Jia, X.; Olson, D.J.; Ross, A.R.; Wu, L. Structural and functional changes in human insulin induced by methylglyoxal. FASEB J. 2006, 20, 1555–1557.
    • (2006) FASEB J , vol.20 , pp. 1555-1557
    • Jia, X.1    Olson, D.J.2    Ross, A.R.3    Wu, L.4
  • 88
    • 0031030963 scopus 로고    scopus 로고
    • Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture
    • Abdel-Wahab, Y.H.A.; O’Harte, F.P.M.; Barnett, C.R.; Flatt, P.R. Characterization of insulin glycation in insulin-secreting cells maintained in tissue culture. J. Endocrinol. 1997, 152, 59–67.
    • (1997) J. Endocrinol , vol.152 , pp. 59-67
    • Abdel-Wahab, Y.1    O’Harte, F.2    Barnett, C.R.3    Flatt, P.R.4
  • 89
    • 0030473543 scopus 로고    scopus 로고
    • Identification of the site of glycation of human insulin
    • O’Harte, F.P.; Hojrup, P.; Barnett, C.R.; Flatt, P.R. Identification of the site of glycation of human insulin. Peptides 1996, 17, 1323–1330.
    • (1996) Peptides , vol.17 , pp. 1323-1330
    • O’Harte, F.P.1    Hojrup, P.2    Barnett, C.R.3    Flatt, P.R.4
  • 90
    • 4444281151 scopus 로고    scopus 로고
    • N-terminal pyrazinones: A new class of peptide-bound advanced glycation end-products
    • Krause, R.; Kühn, J.; Penndorf, I.; Knoll, K.; Henle, T. N-terminal pyrazinones: A new class of peptide-bound advanced glycation end-products. Amino Acids 2004, 27, 9–18.
    • (2004) Amino Acids , vol.27 , pp. 9-18
    • Krause, R.1    Kühn, J.2    Penndorf, I.3    Knoll, K.4    Henle, T.5
  • 91
    • 78650161056 scopus 로고    scopus 로고
    • Pyridoxamine, an inhibitor of advanced glycation end product (AGE) formation ameliorates insulin resistance in obese, type 2 diabetic mice
    • Unoki-Kubota, H.; Yamagishi, S.; Takeuchi, M.; Bujo, H.; Saito, Y. Pyridoxamine, an inhibitor of advanced glycation end product (AGE) formation ameliorates insulin resistance in obese, type 2 diabetic mice. Protein Pept. Lett. 2010, 17, 1177–1181.
    • (2010) Protein Pept. Lett , vol.17 , pp. 1177-1181
    • Unoki-Kubota, H.1    Yamagishi, S.2    Takeuchi, M.3    Bujo, H.4    Saito, Y.5
  • 92
    • 68449092608 scopus 로고    scopus 로고
    • Methylglyoxal contributes to the development of insulin resistance and salt sensitivity in sprague-dawley rats
    • Guo, Q.; Mori, T.; Jiang, Y.; Hu, C.; Osaki, Y.; Yoneki, Y.; Sun, Y.; Hosoya, T.; Kawamata, A.; Ogawa, S.; et al. Methylglyoxal contributes to the development of insulin resistance and salt sensitivity in sprague-dawley rats. J. Hypertens. 2009, 27, 1664–1671.
    • (2009) J. Hypertens , vol.27 , pp. 1664-1671
    • Guo, Q.1    Mori, T.2    Jiang, Y.3    Hu, C.4    Osaki, Y.5    Yoneki, Y.6    Sun, Y.7    Hosoya, T.8    Kawamata, A.9    Ogawa, S.10
  • 94
    • 57749184079 scopus 로고    scopus 로고
    • Induction of apoptosis of beta cells of the pancreas by advanced glycation end-products, important mediators of chronic complications of diabetes mellitus
    • Lim, M.; Park, L.; Shin, G.; Hong, H.; Kang, I.; Park, Y. Induction of apoptosis of beta cells of the pancreas by advanced glycation end-products, important mediators of chronic complications of diabetes mellitus. Ann. NY Acad. Sci. 2008, 1150, 311–315.
    • (2008) Ann. NY Acad. Sci , vol.1150 , pp. 311-315
    • Lim, M.1    Park, L.2    Shin, G.3    Hong, H.4    Kang, I.5    Park, Y.6
  • 96
    • 78650890745 scopus 로고    scopus 로고
    • Inhibition of the receptor for advanced glycation endproducts (RAGE) protects pancreatic beta-cells
    • Zhu, Y.; Shu, T.; Lin, Y.; Wang, H.; Yang, J.; Shi, Y.; Han, X. Inhibition of the receptor for advanced glycation endproducts (RAGE) protects pancreatic beta-cells. Biochem. Biophys. Res. Commun. 2011, 404, 159–165.
    • (2011) Biochem. Biophys. Res. Commun. , vol.404 , pp. 159-165
    • Zhu, Y.1    Shu, T.2    Lin, Y.3    Wang, H.4    Yang, J.5    Shi, Y.6    Han, X.7
  • 97
    • 84863513527 scopus 로고    scopus 로고
    • Advanced glycation end-products induce injury to pancreatic beta cells through oxidative stress
    • Lin, N.; Zhang, H.; Su, Q. Advanced glycation end-products induce injury to pancreatic beta cells through oxidative stress. Diabetes Metab. 2012, 38, 250–257.
    • (2012) Diabetes Metab , vol.38 , pp. 250-257
    • Lin, N.1    Zhang, H.2    Su, Q.3
  • 98
    • 66649125230 scopus 로고    scopus 로고
    • Advanced glycation end products inhibit glucose-stimulated insulin secretion through nitric oxide-dependent inhibition of cytochrome C oxidase and adenosine triphosphate synthesis
    • Zhao, Z.; Zhao, C.; Zhang, X.H.; Zheng, F.; Cai, W.; Vlassara, H.; Ma, Z.A. Advanced glycation end products inhibit glucose-stimulated insulin secretion through nitric oxide-dependent inhibition of cytochrome C oxidase and adenosine triphosphate synthesis. Endocrinology 2009, 150, 2569–2576.
    • (2009) Endocrinology , vol.150 , pp. 2569-2576
    • Zhao, Z.1    Zhao, C.2    Zhang, X.H.3    Zheng, F.4    Cai, W.5    Vlassara, H.6    Ma, Z.A.7
  • 100
    • 84897042207 scopus 로고    scopus 로고
    • Advanced glycation end products impair glucose-induced insulin secretion from rat pancreatic beta-cells
    • Hachiya, H.; Miura, Y.; Inoue, K.; Park, K.H.; Takeuchi, M.; Kubota, K. Advanced glycation end products impair glucose-induced insulin secretion from rat pancreatic beta-cells. J. Hepatobiliary Pancreat. Sci. 2014, 21, 134–141.
    • (2014) J. Hepatobiliary Pancreat. Sci , vol.21 , pp. 134-141
    • Hachiya, H.1    Miura, Y.2    Inoue, K.3    Park, K.H.4    Takeuchi, M.5    Kubota, K.6
  • 102
    • 79955134104 scopus 로고    scopus 로고
    • AGEs decrease insulin synthesis in pancreatic beta-cell by repressing Pdx-1 protein expression at the post-translational level
    • Shu, T.; Zhu, Y.; Wang, H.; Lin, Y.; Ma, Z.; Han, X. AGEs decrease insulin synthesis in pancreatic beta-cell by repressing Pdx-1 protein expression at the post-translational level. PLOS ONE 2011, 6, e18782.
    • (2011) PLOS ONE , vol.6
    • Shu, T.1    Zhu, Y.2    Wang, H.3    Lin, Y.4    Ma, Z.5    Han, X.6
  • 103
    • 77951905952 scopus 로고    scopus 로고
    • Advanced glycation end-products affect transcription factors regulating insulin gene expression
    • Puddu, A.; Storace, D.; Odetti, P.; Viviani, G.L. Advanced glycation end-products affect transcription factors regulating insulin gene expression. Biochem. Biophys. Res. Commun. 2010, 395, 122–125.
    • (2010) Biochem. Biophys. Res. Commun , vol.395 , pp. 122-125
    • Puddu, A.1    Storace, D.2    Odetti, P.3    Viviani, G.L.4
  • 105
    • 4544341580 scopus 로고    scopus 로고
    • Elevated serum levels of Ne-carboxymethyl-lysine, an advanced glycation end product, are associated with proliferative diabetic retinopathy and macular oedema
    • Boehm, B.; Schilling, S.; Rosinger, S.; Lang, G.; Lang, G.; Kientsch-Engel, R.; Stahl, P. Elevated serum levels of Ne-carboxymethyl-lysine, an advanced glycation end product, are associated with proliferative diabetic retinopathy and macular oedema. Diabetologia 2004, 47, 1376–1379.
    • (2004) Diabetologia , vol.47 , pp. 1376-1379
    • Boehm, B.1    Schilling, S.2    Rosinger, S.3    Lang, G.4    Lang, G.5    Kientsch-Engel, R.6    Stahl, P.7
  • 106
    • 30744468605 scopus 로고    scopus 로고
    • Increased serum levels of the specific advanced glycation end product methylglyoxal-derived hydroimidazolone are associated with retinopathy in patients with type 2 diabetes mellitus
    • Fosmark, D.S.; Torjesen, P.A.; Kilhovd, B.K.; Berg, T.J.; Sandvik, L.; Hanssen, K.F.; Agardh, C.-D.; Agardh, E. Increased serum levels of the specific advanced glycation end product methylglyoxal-derived hydroimidazolone are associated with retinopathy in patients with type 2 diabetes mellitus. Metabolism 2006, 55, 232–236.
    • (2006) Metabolism , vol.55 , pp. 232-236
    • Fosmark, D.S.1    Torjesen, P.A.2    Kilhovd, B.K.3    Berg, T.J.4    Sandvik, L.5    Hanssen, K.F.6    Agardh, C.-D.7    Agardh, E.8
  • 107
    • 0034529945 scopus 로고    scopus 로고
    • Serum concentrations of advanced glycation endproducts are associated with the development of atherosclerosis as well as diabetic microangiopathy in patients with type 2 diabetes
    • Aso, Y.; Inukai, T.; Tayama, K.; Takemura, Y. Serum concentrations of advanced glycation endproducts are associated with the development of atherosclerosis as well as diabetic microangiopathy in patients with type 2 diabetes. Acta Diabetol. 2000, 37, 87–92.
    • (2000) Acta Diabetol , vol.37 , pp. 87-92
    • Aso, Y.1    Inukai, T.2    Tayama, K.3    Takemura, Y.4
  • 108
    • 0032143589 scopus 로고    scopus 로고
    • Increased serum levels of advanced glycation end-products and diabetic complications
    • Ono, Y.; Aoki, S.; Ohnishi, K.; Yasuda, T.; Kawano, K.; Tsukada, Y. Increased serum levels of advanced glycation end-products and diabetic complications. Diabetes Res. Clin. Pract. 1998, 41, 131–137.
    • (1998) Diabetes Res. Clin. Pract. , vol.41 , pp. 131-137
    • Ono, Y.1    Aoki, S.2    Ohnishi, K.3    Yasuda, T.4    Kawano, K.5    Tsukada, Y.6
  • 109
    • 0034757228 scopus 로고    scopus 로고
    • Increased serum concentrations of advanced glycation end products: A marker of coronary artery disease activity in type 2 diabetic patients
    • Kiuchi, K.; Nejima, J.; Takano, T.; Ohta, M.; Hashimoto, H. Increased serum concentrations of advanced glycation end products: A marker of coronary artery disease activity in type 2 diabetic patients. Heart 2001, 85, 87–91.
    • (2001) Heart , vol.85 , pp. 87-91
    • Kiuchi, K.1    Nejima, J.2    Takano, T.3    Ohta, M.4    Hashimoto, H.5
  • 110
    • 33748897506 scopus 로고    scopus 로고
    • The advanced glycation end product Ne-carboxymethyllysine is not a predictor of cardiovascular events and renal outcomes in patients with type 2 diabetic kidney disease and hypertension
    • Busch, M.; Franke, S.; Wolf, G.; Brandstädt, A.; Ott, U.; Gerth, J.; Hunsicker, L.G.; Stein, G. The advanced glycation end product Ne-carboxymethyllysine is not a predictor of cardiovascular events and renal outcomes in patients with type 2 diabetic kidney disease and hypertension. Am. J. Kidney Dis. 2006, 48, 571–579.
    • (2006) Am. J. Kidney Dis , vol.48 , pp. 571-579
    • Busch, M.1    Franke, S.2    Wolf, G.3    Brandstädt, A.4    Ott, U.5    Gerth, J.6    Hunsicker, L.G.7    Stein, G.8
  • 111
    • 84881496313 scopus 로고    scopus 로고
    • Plasma levels of advanced glycation endproducts Ne-(Carboxymethyl) lysine, Ne-(carboxyethyl) lysine, and pentosidine are not independently associated with cardiovascular disease in individuals with or without type 2 diabetes: The hoorn and codam studies
    • Hanssen, N.M.; Engelen, L.; Ferreira, I.; Scheijen, J.L.; Huijberts, M.S.; van Greevenbroek, M.M.; van der Kallen, C.J.; Dekker, J.M.; Nijpels, G.; Stehouwer, C.D. Plasma levels of advanced glycation endproducts Ne-(carboxymethyl) lysine, Ne-(carboxyethyl) lysine, and pentosidine are not independently associated with cardiovascular disease in individuals with or without type 2 diabetes: The hoorn and codam studies. J. Clin. Endocrinol. Metab. 2013, 98, E1369–E1373.
    • (2013) J. Clin. Endocrinol. Metab. , vol.98 , pp. E1369-E1373
    • Hanssen, N.M.1    Engelen, L.2    Ferreira, I.3    Scheijen, J.L.4    Huijberts, M.S.5    Van Greevenbroek, M.M.6    Van Der Kallen, C.J.7    Dekker, J.M.8    Nijpels, G.9    Stehouwer, C.D.10
  • 112
    • 84919969049 scopus 로고    scopus 로고
    • Plasma advanced glycation endproducts are associated with incident cardiovascular events in individuals with type 2 diabetes: A case-cohort study with a median follow-up of 10 years (EPIC-NL)
    • Hanssen, N.M.; Beulens, J.W.; van Dieren, S.; Scheijen, J.L.; Spijkerman, A.M.; van der Schouw, Y.T.; Stehouwer, C.D.; Schalkwijk, C.G. Plasma advanced glycation endproducts are associated with incident cardiovascular events in individuals with type 2 diabetes: A case-cohort study with a median follow-up of 10 years (EPIC-NL). Diabetes 2014, 64, 257–265.
    • (2014) Diabetes , vol.64 , pp. 257-265
    • Hanssen, N.M.1    Beulens, J.W.2    Van Dieren, S.3    Scheijen, J.L.4    Spijkerman, A.M.5    Van Der Schouw, Y.T.6    Stehouwer, C.D.7    Schalkwijk, C.G.8
  • 113
    • 33747080843 scopus 로고    scopus 로고
    • Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification
    • Dobler, D.; Ahmed, N.; Song, L.; Eboigbodin, K.E.; Thornalley, P.J. Increased dicarbonyl metabolism in endothelial cells in hyperglycemia induces anoikis and impairs angiogenesis by RGD and GFOGER motif modification. Diabetes 2006, 55, 1961–1969.
    • (2006) Diabetes , vol.55 , pp. 1961-1969
    • Dobler, D.1    Ahmed, N.2    Song, L.3    Eboigbodin, K.E.4    Thornalley, P.J.5
  • 115
    • 84891818459 scopus 로고    scopus 로고
    • Degradation of oxidized and glycoxidized collagen: Role of collagen cross-linking
    • Nowotny, K.; Grune, T. Degradation of oxidized and glycoxidized collagen: Role of collagen cross-linking. Arch. Biochem. Biophys. 2014, 542, 56–64.
    • (2014) Arch. Biochem. Biophys. , vol.542 , pp. 56-64
    • Nowotny, K.1    Grune, T.2
  • 120
    • 76549095723 scopus 로고    scopus 로고
    • Two dicarbonyl compounds, 3-deoxyglucosone and methylglyoxal, differentially modulate dermal fibroblasts
    • Sassi-Gaha, S.; Loughlin, D.T.; Kappler, F.; Schwartz, M.L.; Su, B.; Tobia, A.M.; Artlett, C.M. Two dicarbonyl compounds, 3-deoxyglucosone and methylglyoxal, differentially modulate dermal fibroblasts. Matrix Biol. 2010, 29, 127–134.
    • (2010) Matrix Biol , vol.29 , pp. 127-134
    • Sassi-Gaha, S.1    Loughlin, D.T.2    Kappler, F.3    Schwartz, M.L.4    Su, B.5    Tobia, A.M.6    Artlett, C.M.7
  • 121
    • 0022979094 scopus 로고
    • Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm
    • Charonis, A.S.; Tsilibary, E.C.; Saku, T.; Furthmayr, H. Inhibition of laminin self-assembly and interaction with type IV collagen by antibodies to the terminal domain of the long arm. J. Cell Biol. 1986, 103, 1689–1697.
    • (1986) J. Cell Biol , vol.103 , pp. 1689-1697
    • Charonis, A.S.1    Tsilibary, E.C.2    Saku, T.3    Furthmayr, H.4
  • 122
    • 0026696647 scopus 로고
    • Altered cellular interactions between endothelial cells and nonenzymatically glucosylated laminin/type IV collagen
    • 12404–12407
    • Haitoglou, C.S.; Tsilibary, E.C.; Brownlee, M.; Charonis, A.S. Altered cellular interactions between endothelial cells and nonenzymatically glucosylated laminin/type IV collagen. J. Biol. Chem. 1992, 267, 12404–12407.
    • (1992) J. Biol. Chem , vol.267
    • Haitoglou, C.S.1    Tsilibary, E.C.2    Brownlee, M.3    Charonis, A.S.4
  • 123
    • 0021225742 scopus 로고
    • Inhibition of fibronectin binding to matrix components by nonenzymatic glycosylation
    • Cohen, M.P.; Ku, L. Inhibition of fibronectin binding to matrix components by nonenzymatic glycosylation. Diabetes 1984, 33, 970–974.
    • (1984) Diabetes , vol.33 , pp. 970-974
    • Cohen, M.P.1    Ku, L.2
  • 125
    • 73249151401 scopus 로고    scopus 로고
    • Advanced glycation end products in extracellular matrix proteins contribute to the failure of sensory nerve regeneration in diabetes
    • Duran-Jimenez, B.; Dobler, D.; Moffatt, S.; Rabbani, N.; Streuli, C.H.; Thornalley, P.J.; Tomlinson, D.R.; Gardiner, N.J. Advanced glycation end products in extracellular matrix proteins contribute to the failure of sensory nerve regeneration in diabetes. Diabetes 2009, 58, 2893–2903.
    • (2009) Diabetes , vol.58 , pp. 2893-2903
    • Duran-Jimenez, B.1    Dobler, D.2    Moffatt, S.3    Rabbani, N.4    Streuli, C.H.5    Thornalley, P.J.6    Tomlinson, D.R.7    Gardiner, N.J.8
  • 126
    • 77953821528 scopus 로고    scopus 로고
    • Collaboration, E.R.F. Diabetes mellitus, fasting blood glucose concentration, and risk of vascular disease: A collaborative meta-analysis of 102 prospective studies
    • Collaboration, E.R.F. Diabetes mellitus, fasting blood glucose concentration, and risk of vascular disease: A collaborative meta-analysis of 102 prospective studies. Lancet 2010, 375, 2215–2222.
    • (2010) Lancet , vol.375 , pp. 2215-2222
  • 127
    • 34249931268 scopus 로고    scopus 로고
    • Increased serum levels of advanced glycation endproducts predict total, cardiovascular and coronary mortality in women with type 2 diabetes: A population-based 18 year follow-up study
    • Kilhovd, B.K.; Juutilainen, A.; Lehto, S.; Rönnemaa, T.; Torjesen, P.A.; Hanssen, K.F.; Laakso, M. Increased serum levels of advanced glycation endproducts predict total, cardiovascular and coronary mortality in women with type 2 diabetes: A population-based 18 year follow-up study. Diabetologia 2007, 50, 1409–1417.
    • (2007) Diabetologia , vol.50 , pp. 1409-1417
    • Kilhovd, B.K.1    Juutilainen, A.2    Lehto, S.3    Rönnemaa, T.4    Torjesen, P.A.5    Hanssen, K.F.6    Laakso, M.7
  • 130
    • 84865132307 scopus 로고    scopus 로고
    • An update on advanced glycation endproducts and atherosclerosis
    • Del Turco, S.; Basta, G. An update on advanced glycation endproducts and atherosclerosis. BioFactors 2012, 38, 266–274.
    • (2012) Biofactors , vol.38 , pp. 266-274
    • Del Turco, S.1    Basta, G.2
  • 131
    • 0029121260 scopus 로고
    • Immunohistochemical and ultrastructural detection of advanced glycation end products in atherosclerotic lesions of human aorta with a novel specific monoclonal antibody
    • Kume, S.; Takeya, M.; Mori, T.; Araki, N.; Suzuki, H.; Horiuchi, S.; Kodama, T.; Miyauchi, Y.; Takahashi, K. Immunohistochemical and ultrastructural detection of advanced glycation end products in atherosclerotic lesions of human aorta with a novel specific monoclonal antibody. Am. J. Pathol. 1995, 147, 654–667.
    • (1995) Am. J. Pathol , vol.147 , pp. 654-667
    • Kume, S.1    Takeya, M.2    Mori, T.3    Araki, N.4    Suzuki, H.5    Horiuchi, S.6    Kodama, T.7    Miyauchi, Y.8    Takahashi, K.9
  • 132
    • 0032588929 scopus 로고    scopus 로고
    • Ne-(Carboxymethyl)lysine in atherosclerotic vascular lesions as a marker for local oxidative stress
    • Nerlich, A.G.; Schleicher, E.D. Ne-(carboxymethyl)lysine in atherosclerotic vascular lesions as a marker for local oxidative stress. Atherosclerosis 1999, 144, 41–47.
    • (1999) Atherosclerosis , vol.144 , pp. 41-47
    • Nerlich, A.G.1    Schleicher, E.D.2
  • 133
    • 33646081531 scopus 로고    scopus 로고
    • Hepatocyte growth factor protects human endothelial cells against advanced glycation end products-induced apoposis
    • Zhou, Y.J.; Wang, J.H.; Zhang, J. Hepatocyte growth factor protects human endothelial cells against advanced glycation end products-induced apoposis. Biochem. Biophys. Res. Communi. 2006, 344, 658–666.
    • (2006) Biochem. Biophys. Res. Communi , vol.344 , pp. 658-666
    • Zhou, Y.J.1    Wang, J.H.2    Zhang, J.3
  • 134
    • 84876333512 scopus 로고    scopus 로고
    • Inhibitory effect of atorvastatin on AGE-induced HCAEC apoptosis by upregulating HSF-1 protein
    • Li, Y.; Li, J.; Cui, L.; Lai, Y.; Yao, Y.; Zhang, Y.; Pang, X.; Wang, J.; Liu, X. Inhibitory effect of atorvastatin on AGE-induced HCAEC apoptosis by upregulating HSF-1 protein. Int. J. Biol. Macromol. 2013, 57, 259–264.
    • (2013) Int. J. Biol. Macromol , vol.57 , pp. 259-264
    • Li, Y.1    Li, J.2    Cui, L.3    Lai, Y.4    Yao, Y.5    Zhang, Y.6    Pang, X.7    Wang, J.8    Liu, X.9
  • 135
    • 75949121425 scopus 로고    scopus 로고
    • Advanced glycation endproducts alter functions and promote apoptosis in endothelial progenitor cells through receptor for advanced glycation endproducts mediate overpression of cell oxidant stress
    • Chen, J.; Song, M.; Yu, S.; Gao, P.; Yu, Y.; Wang, H.; Huang, L. Advanced glycation endproducts alter functions and promote apoptosis in endothelial progenitor cells through receptor for advanced glycation endproducts mediate overpression of cell oxidant stress. Mol. Cell. Biochem. 2010, 335, 137–146.
    • (2010) Mol. Cell. Biochem , vol.335 , pp. 137-146
    • Chen, J.1    Song, M.2    Yu, S.3    Gao, P.4    Yu, Y.5    Wang, H.6    Huang, L.7
  • 136
    • 0037301050 scopus 로고    scopus 로고
    • Pigment epithelium-derived factor prevents advanced glycation end products-induced monocyte chemoattractant protein-1 production in microvascular endothelial cells by suppressing intracellular reactive oxygen species generation
    • Inagaki, Y.; Yamagishi, S.; Okamoto, T.; Takeuchi, M.; Amano, S. Pigment epithelium-derived factor prevents advanced glycation end products-induced monocyte chemoattractant protein-1 production in microvascular endothelial cells by suppressing intracellular reactive oxygen species generation. Diabetologia 2003, 46, 284–287.
    • (2003) Diabetologia , vol.46 , pp. 284-287
    • Inagaki, Y.1    Yamagishi, S.2    Okamoto, T.3    Takeuchi, M.4    Amano, S.5
  • 137
    • 0029295736 scopus 로고
    • Advanced glycation endproducts promote adhesion molecule (VCAM-1, ICAM-1) expression and atheroma formation in normal rabbits
    • Vlassara, H.; Fuh, H.; Donnelly, T.; Cybulsky, M. Advanced glycation endproducts promote adhesion molecule (VCAM-1, ICAM-1) expression and atheroma formation in normal rabbits. Mol. Med. 1995, 1, 447–456.
    • (1995) Mol. Med , vol.1 , pp. 447-456
    • Vlassara, H.1    Fuh, H.2    Donnelly, T.3    Cybulsky, M.4
  • 138
    • 0029088742 scopus 로고
    • Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes
    • Schmidt, A.M.; Hori, O.; Chen, J.X.; Li, J.F.; Crandall, J.; Zhang, J.; Cao, R.; Yan, S.D.; Brett, J.; Stern, D. Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes. J. Clin. Investig. 1995, 96, 1395–1403.
    • (1995) J. Clin. Investig. , vol.96 , pp. 1395-1403
    • Schmidt, A.M.1    Hori, O.2    Chen, J.X.3    Li, J.F.4    Crandall, J.5    Zhang, J.6    Cao, R.7    Yan, S.D.8    Brett, J.9    Stern, D.10
  • 139
    • 73949118948 scopus 로고    scopus 로고
    • Glucagon-like peptide-1 (GLP-1) inhibits advanced glycation end product (AGE)-induced up-regulation of VCAM-1 mRNA levels in endothelial cells by suppressing AGE receptor (RAGE) expression
    • Ishibashi, Y.; Matsui, T.; Takeuchi, M.; Yamagishi, S.-I. Glucagon-like peptide-1 (GLP-1) inhibits advanced glycation end product (AGE)-induced up-regulation of VCAM-1 mRNA levels in endothelial cells by suppressing AGE receptor (RAGE) expression. Biochem. Biophys. Res. Commun. 2010, 391, 1405–1408.
    • (2010) Biochem. Biophys. Res. Commun , vol.391 , pp. 1405-1408
    • Ishibashi, Y.1    Matsui, T.2    Takeuchi, M.3    Yamagishi, S.-I.4
  • 140
    • 84883084459 scopus 로고    scopus 로고
    • Advanced glycation end products evoke endothelial cell damage by stimulating soluble dipeptidyl peptidase-4 production and its interaction with mannose 6-phosphate/insulin-like growth factor II receptor
    • Ishibashi, Y.; Matsui, T.; Maeda, S.; Higashimoto, Y.; Yamagishi, S.-I. Advanced glycation end products evoke endothelial cell damage by stimulating soluble dipeptidyl peptidase-4 production and its interaction with mannose 6-phosphate/insulin-like growth factor II receptor. Cardiovasc. Diabetol. 2013, 12, 125–125.
    • (2013) Cardiovasc. Diabetol , vol.12
    • Ishibashi, Y.1    Matsui, T.2    Maeda, S.3    Higashimoto, Y.4    Yamagishi, S.-I.5
  • 141
    • 0031773362 scopus 로고    scopus 로고
    • Advanced glycation endproducts inhibit prostacyclin production and induce plasminogen activator inhibitor-1 in human microvascular endothelial cells
    • Yamagishi, S.; Fujimori, H.; Yonekura, H.; Yamamoto, Y.; Yamamoto, H. Advanced glycation endproducts inhibit prostacyclin production and induce plasminogen activator inhibitor-1 in human microvascular endothelial cells. Diabetologia 1998, 41, 1435–1441.
    • (1998) Diabetologia , vol.41 , pp. 1435-1441
    • Yamagishi, S.1    Fujimori, H.2    Yonekura, H.3    Yamamoto, Y.4    Yamamoto, H.5
  • 144
    • 0026062122 scopus 로고
    • Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilatation in experimental diabetes
    • Bucala, R.; Tracey, K.J.; Cerami, A. Advanced glycosylation products quench nitric oxide and mediate defective endothelium-dependent vasodilatation in experimental diabetes. J. Clin. Investig. 1991, 87, 432–438.
    • (1991) J. Clin. Investig , vol.87 , pp. 432-438
    • Bucala, R.1    Tracey, K.J.2    Cerami, A.3
  • 145
    • 0038265440 scopus 로고    scopus 로고
    • Impairment of vascular endothelial nitric oxide synthase activity by advanced glycation end products
    • Xu, B.; Chibber, R.; Ruggiero, D.; Kohner, E.; Ritter, J.; Ferro, A. Impairment of vascular endothelial nitric oxide synthase activity by advanced glycation end products. FASEB J. 2003, 17, 1289–1291.
    • (2003) FASEB J , vol.17 , pp. 1289-1291
    • Xu, B.1    Chibber, R.2    Ruggiero, D.3    Kohner, E.4    Ritter, J.5    Ferro, A.6
  • 146
    • 0031831261 scopus 로고    scopus 로고
    • Constitutive nitric oxide synthase expression in retinal vascular endothelial cells is suppressed by high glucose and advanced glycation end products
    • Chakravarthy, U.; Hayes, R.G.; Stitt, A.W.; McAuley, E.; Archer, D.B. Constitutive nitric oxide synthase expression in retinal vascular endothelial cells is suppressed by high glucose and advanced glycation end products. Diabetes 1998, 47, 945–952.
    • (1998) Diabetes , vol.47 , pp. 945-952
    • Chakravarthy, U.1    Hayes, R.G.2    Stitt, A.W.3    McAuley, E.4    Archer, D.B.5
  • 147
    • 3042521592 scopus 로고    scopus 로고
    • Nitric oxide and arterial disease
    • Barbato, J.E.; Tzeng, E. Nitric oxide and arterial disease. J. Vasc. Surg. 2004, 40, 187–193.
    • (2004) J. Vasc. Surg , vol.40 , pp. 187-193
    • Barbato, J.E.1    Tzeng, E.2
  • 149
    • 19944367877 scopus 로고    scopus 로고
    • Substrates modified by advanced glycation end-products cause dysfunction and death in retinal pericytes by reducing survival signals mediated by platelet-derived growth factor
    • Stitt, A.W.; Hughes, S.J.; Canning, P.; Lynch, O.; Cox, O.; Frizzell, N.; Thorpe, S.R.; Cotter, T.G.; Curtis, T.M.; Gardiner, T.A. Substrates modified by advanced glycation end-products cause dysfunction and death in retinal pericytes by reducing survival signals mediated by platelet-derived growth factor. Diabetologia 2004, 47, 1735–1746.
    • (2004) Diabetologia , vol.47 , pp. 1735-1746
    • Stitt, A.W.1    Hughes, S.J.2    Canning, P.3    Lynch, O.4    Cox, O.5    Frizzell, N.6    Thorpe, S.R.7    Cotter, T.G.8    Curtis, T.M.9    Gardiner, T.A.10
  • 150
    • 70449113602 scopus 로고    scopus 로고
    • Eye vessels saved by rescuing their pericyte partners
    • Antonetti, D. Eye vessels saved by rescuing their pericyte partners. Nat. Med. 2009, 15, 1248–1249.
    • (2009) Nat. Med , vol.15 , pp. 1248-1249
    • Antonetti, D.1
  • 152
    • 0032520871 scopus 로고    scopus 로고
    • Advanced glycation end products increase retinal vascular endothelial growth factor expression
    • Lu, M.; Kuroki, M.; Amano, S.; Tolentino, M.; Keough, K.; Kim, I.; Bucala, R.; Adamis, A.P. Advanced glycation end products increase retinal vascular endothelial growth factor expression. J. Clin. Investig. 1998, 101, 1219–1224.
    • (1998) J. Clin. Investig , vol.101 , pp. 1219-1224
    • Lu, M.1    Kuroki, M.2    Amano, S.3    Tolentino, M.4    Keough, K.5    Kim, I.6    Bucala, R.7    Adamis, A.P.8
  • 153
  • 154
    • 0035992573 scopus 로고    scopus 로고
    • Advanced glycation end products increase, through a protein kinase C-dependent pathway, vascular endothelial growth factor expression in retinal endothelial cells. Inhibitory effect of gliclazide
    • Mamputu, J.C.; Renier, G. Advanced glycation end products increase, through a protein kinase C-dependent pathway, vascular endothelial growth factor expression in retinal endothelial cells. Inhibitory effect of gliclazide. J. Diabetes Complicat. 2002, 16, 284–293.
    • (2002) J. Diabetes Complicat , vol.16 , pp. 284-293
    • Mamputu, J.C.1    Renier, G.2
  • 155
    • 0037036345 scopus 로고    scopus 로고
    • Advanced glycation end product-induced apoptosis and overexpression of vascular endothelial growth factor and monocyte chemoattractant protein-1 in human-cultured mesangial cells
    • Yamagishi, S.; Inagaki, Y.; Okamoto, T.; Amano, S.; Koga, K.; Takeuchi, M.; Makita, Z. Advanced glycation end product-induced apoptosis and overexpression of vascular endothelial growth factor and monocyte chemoattractant protein-1 in human-cultured mesangial cells. J. Biol. Chem. 2002, 277, 20309–20315.
    • (2002) J. Biol. Chem , vol.277 , pp. 20309-20315
    • Yamagishi, S.1    Inagaki, Y.2    Okamoto, T.3    Amano, S.4    Koga, K.5    Takeuchi, M.6    Makita, Z.7
  • 156
    • 84859868983 scopus 로고    scopus 로고
    • Contractility of the renal glomerulus and mesangial cells: Lingering doubts and strategies for the future
    • Ghayur, M.N.; Krepinsky, J.C.; Janssen, L.J. Contractility of the renal glomerulus and mesangial cells: Lingering doubts and strategies for the future. Med. Hypotheses Res. 2008, 4, 1–9.
    • (2008) Med. Hypotheses Res. , vol.4 , pp. 1-9
    • Ghayur, M.N.1    Krepinsky, J.C.2    Janssen, L.J.3
  • 157
    • 0037246065 scopus 로고    scopus 로고
    • Advanced glycation end products inhibit de novo protein synthesis and induce TGF-beta overexpression in proximal tubular cells
    • Yamagishi, S.; Inagaki, Y.; Okamoto, T.; Amano, S.; Koga, K.; Takeuchi, M. Advanced glycation end products inhibit de novo protein synthesis and induce TGF-beta overexpression in proximal tubular cells. Kidney Int. 2003, 63, 464–473.
    • (2003) Kidney Int , vol.63 , pp. 464-473
    • Yamagishi, S.1    Inagaki, Y.2    Okamoto, T.3    Amano, S.4    Koga, K.5    Takeuchi, M.6
  • 158
    • 0028980435 scopus 로고
    • PDGF and TGF-bold beta mediate collagen production by mesangial cells exposed to advanced glycosylation end products
    • Throckmorton, D.C.; Brogden, A.P.; Min, B.; Rasmussen, H.; Kashgarian, M. PDGF and TGF-bold beta mediate collagen production by mesangial cells exposed to advanced glycosylation end products. Kidney Int. 1995, 48, 111–117.
    • (1995) Kidney Int , vol.48 , pp. 111-117
    • Throckmorton, D.C.1    Brogden, A.P.2    Min, B.3    Rasmussen, H.4    Kashgarian, M.5
  • 159
  • 162
    • 33748031093 scopus 로고    scopus 로고
    • Connective tissue growth factor plays an important role in advanced glycation end product-induced tubular epithelial-to-mesenchymal transition: Implications for diabetic renal disease
    • Burns, W.C.; Twigg, S.M.; Forbes, J.M.; Pete, J.; Tikellis, C.; Thallas-Bonke, V.; Thomas, M.C.; Cooper, M.E.; Kantharidis, P. Connective tissue growth factor plays an important role in advanced glycation end product-induced tubular epithelial-to-mesenchymal transition: Implications for diabetic renal disease. J. Am. Soc. Nephrol. 2006, 17, 2484–2494.
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 2484-2494
    • Burns, W.C.1    Twigg, S.M.2    Forbes, J.M.3    Pete, J.4    Tikellis, C.5    Thallas-Bonke, V.6    Thomas, M.C.7    Cooper, M.E.8    Kantharidis, P.9
  • 164
    • 77949395650 scopus 로고    scopus 로고
    • Advanced glycation end-products induce tubular CTGF via TGF-β-independent Smad3 signaling
    • Chung, A.C.K.; Zhang, H.; Kong, Y.-Z.; Tan, J.-J.; Huang, X.R.; Kopp, J.B.; Lan, H.Y. Advanced glycation end-products induce tubular CTGF via TGF-β-independent Smad3 signaling. J. Am. Soc. Nephrol. 2010, 21, 249–260.
    • (2010) J. Am. Soc. Nephrol , vol.21 , pp. 249-260
    • Chung, A.1    Zhang, H.2    Kong, Y.-Z.3    Tan, J.-J.4    Huang, X.R.5    Kopp, J.B.6    Lan, H.Y.7
  • 165
    • 34948869847 scopus 로고    scopus 로고
    • Dietary AGEs and ALEs and risk to human health by their interaction with the receptor for advanced glycation endproducts (RAGE)—An introduction
    • Thornalley, P.J. Dietary AGEs and ALEs and risk to human health by their interaction with the receptor for advanced glycation endproducts (RAGE)—An introduction. Mol. Nutr. Food Res. 2007, 51, 1107–1110.
    • (2007) Mol. Nutr. Food Res , vol.51 , pp. 1107-1110
    • Thornalley, P.J.1
  • 166
    • 34948829109 scopus 로고    scopus 로고
    • Arguing for the motion: Yes, rage is a receptor for advanced glycation endproducts
    • Ramasamy, R.; Yan, S.F.; Schmidt, A.M. Arguing for the motion: Yes, rage is a receptor for advanced glycation endproducts. Mol. Nutr. Food Res. 2007, 51, 1111–1115.
    • (2007) Mol. Nutr. Food Res , vol.51 , pp. 1111-1115
    • Ramasamy, R.1    Yan, S.F.2    Schmidt, A.M.3
  • 167
    • 34948881793 scopus 로고    scopus 로고
    • The mechanism by which dietary AGEs are a risk to human health is via their interaction with RAGE: Arguing against the motion
    • Heizmann, C.W. The mechanism by which dietary AGEs are a risk to human health is via their interaction with RAGE: Arguing against the motion. Mol. Nutr. Food Res. 2007, 51, 1116–1119.
    • (2007) Mol. Nutr. Food Res , vol.51 , pp. 1116-1119
    • Heizmann, C.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.