nach oben

Endocrine

Erschienen in:

01.06.2013 | Review

Methylglyoxal, obesity, and diabetes

verfasst von: Paulo Matafome, Cristina Sena, Raquel Seiça

Erschienen in: Endocrine | Ausgabe 3/2013

Einloggen, um Zugang zu erhalten

Abstract

Methylglyoxal (MG) is a highly reactive compound derived mainly from glucose and fructose metabolism. This metabolite has been implicated in diabetic complications as it is a strong AGE precursor. Furthermore, recent studies suggested a role for MG in insulin resistance and beta-cell dysfunction. Although several drugs have been developed in the recent years to scavenge MG and inhibit AGE formation, we are still far from having an effective strategy to prevent MG-induced mechanisms. This review summarizes the mechanisms of MG formation, detoxification, and action. Furthermore, we review the current knowledge about its implication on the pathophysiology and complications of obesity and diabetes.

C. Neuberg, Biochem. Z. 51, 484–508 (1913)

H. Dakin, H. Dudley, An enzyme concerned with the formation of hydroxy acids from ketonic aldehydes. J. Biol. Chem. 14, 423–431 (1913)

E. Case, R. Cook, The occurrence of pyruvic acid and methylglyoxal in muscle metabolism. Biochem. J. 25(4), 1319–1335 (1931)PubMed

F. Clift, R.P. Cook, A method of determination of some biologically important aldehydes and ketones, with special reference to pyruvic acid and methylglyoxal. Biochem. J. 26(6), 1788–1799 (1932)PubMed

A. McLellan, P.J. Thornalley, Glyoxalase activity in human red blood cells fractioned by age. Mech. Ageing Dev. 48(1), 63–71 (1989)PubMedCrossRef

P.J. Thornalley, Modification of the glyoxalase system in human red blood cells by glucose in vitro. Biochem. J. 254(3), 751–755 (1988)PubMed

T. Atkins, P. Thornally, Erythrocyte glyoxalase activity in genetically obese (ob/ob) and streptozotocin diabetic mice. Diabetes Res. 11(3), 125–129 (1989)PubMed

P.J. Thornalley, N. Hooper, P. Jennings, C. Florkowski, A. Jones, J. Lunec, A. Barnett, The human red blood cell glyoxalase system in diabetes mellitus. Diabetes Res. Clin. Pract. 7(2), 115–120 (1989)PubMedCrossRef

P.J. Thornalley, The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269(1), 1–11 (1990)PubMed

10.

A. McLellan, P.J. Thornalley, J. Benn, P. Sonksen, Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. (Lond) 87(1), 21–29 (1994)

11.

H. Odani, T. Shinzato, Y. Matsumoto, J. Usami, K. Maeda, Increase in three alpha, beta-dicarbonyl compound levels in human uremic plasma: specific in vivo determination of intermediates in advanced Maillard reaction. Biochem. Biophys. Res. Commun. 256(1), 89–93 (1999)PubMedCrossRef

12.

M. Brownlee, The pathobiology of diabetic complications: a unifying mechanism. Diabetes 54(6), 1615–1625 (2005)PubMedCrossRef

13.

W. Chan, H. Wu, N. Shao, Apoptotic signaling in methylglyoxal-treated human osteoblasts involves oxidative stress, c-Jun N-terminal kinase, caspase-3 and p21-activated kanse-2. J. Cell. Biochem. 100, 1056–1069 (2007)PubMedCrossRef

14.

K. Nakayama, M. Nakayama, M. Iwabuchi, H. Terawaki, T. Sato, M. Kohno, S. Ito, Plasma alpha-oxoaldehyde levels in diabetic and nondiabetic chronic kidney disease patients. Am. J. Nephrol. 28(6), 871–878 (2008)PubMedCrossRef

15.

D. Tan, Y. Wang, C. Lo, S. Sang, C. Ho, Methylglyoxal: its presence in beverages and potential scavengers. Ann. N. Y. Acad. Sci. 1126, 72–75 (2008)PubMedCrossRef

16.

O. Lee, W. Bruce, Q. Dong, J. Bruce, R. Mehta, P. O’Brien, Fructose and carbonyl metabolites as endogenous toxins. Chem. Biol. Interact. 178(1–3), 332–339 (2009)PubMedCrossRef

17.

J. Liu, R. Wang, K. Desai, L. Wu, Upregulation of aldolase B and overproduction of methylglyoxal in vascular tissues from rats with metabolic syndrome. Cardiovasc. Res. 92(3), 494–503 (2011)PubMedCrossRef

18.

P. Yu, M. Wang, H. Fan, Y. Deng, D. Gubisne-Haberle, Involvement of SSAO-mediated deamination in adipose glucose transport and weight gain in obese diabetic KKAy mice. Am. J. Physiol. Endocrinol. Metab. 286(4), E634–E641 (2004)PubMedCrossRef

19.

M. Barrand, B. Callingham, Solubilization and some properties of a semicarbazide-sensitive amine oxidase in brown adipose tissue of the rat. Biochem. J. 222, 467–475 (1984)PubMed

20.

Y. Deng, P. Yu, Assessment of the deamination of aminoacetone, an endogenous substrate for semicarbazide-sensitive amine oxidase. Anal. Biochem. 270, 97–102 (1999)PubMedCrossRef

21.

Z. Turk, M. Cavlović-Naglić, N. Turk, Relationship of methylglyoxal-adduct biogenesis to LDL and triglyceride levels in diabetics. Life Sci. 89(13–14), 485–490 (2011)PubMedCrossRef

22.

N. Ahmed, B. Mirshekar-Syahkal, L. Kennish, N. Karachalias, R. Babaei-Jadidi, P.J. Thornalley, Assay of advanced glycation endproducts in selected beverages and food by liquid chromatography with tandem mass spectrometric detection. Mol. Nutr. Food Res. 49(7), 691–699 (2005)PubMedCrossRef

23.

A. Negre-Salvayre, R. Salvayre, N. Augé, R. Pamplona, M. Portero-Otín, Hyperglycemia and glycation in diabetic complications. Antioxid. Redox Signal. 11(12), 3071–3109 (2009)PubMedCrossRef

24.

A. Stirban, M. Negrean, C. Götting, B. Stratmann, T. Gawlowski, M. Mueller-Roesel, K. Kleesiek, T. Koschinsky, D. Tschoepe, Leptin decreases postprandially in people with type 2 diabetes, an effect reduced by the cooking method. Horm. Metab. Res. 40(12), 896–900 (2008)PubMedCrossRef

25.

E. Marceau, V.A. Yaylayan, Profiling of alpha-dicarbonyl content of commercial honeys from different botanical origins: identification of 3,4-dideoxyglucoson-3-ene (3,4-DGE) and related compounds. Agric. Food Chem. 57(22), 10837–10844 (2009)CrossRef

26.

R. Zhao, A. Lee, J.P. Abbatt, Investigation of aqueous-phase photooxidation of glyoxal and methylglyoxal by aerosol chemical ionization mass spectrometry: observation of hydroxyhydroperoxide formation. J. Phys. Chem. A. 116(24), 6253–6263 (2012)PubMedCrossRef

27.

S. Gensberger, S. Mittelmaier, M. Glomb, M. Pischetsrieder, Identification and quantification of six major α-dicarbonyl process contaminants in high-fructose corn syrup. Anal. Bioanal. Chem. 403(10), 2923–2931 (2012)PubMedCrossRef

28.

R. Spanneberg, G. Salzwedel, M. Glomb, Formation of early and advanced Maillard reaction products correlates to the ripening of cheese. J. Agric. Food Chem. 60(2), 600–607 (2012)PubMedCrossRef

29.

J. Wang, T. Chang, Methylglyoxal content in drinking coffee as a cytotoxic factor. J. Food Sci. 75(6), H167–H171 (2010)PubMedCrossRef

30.

A. Goldin, J. Beckman, A. Schmidt, M. Creager, Advanced glycation end products: sparking the development of diabetic vascular injury. Circulation 114, 597–605 (2006)PubMedCrossRef

31.

M. Xue, N. Rabbani, P. Thornalley, Glyoxalase in ageing. Semin. Cell Dev. Biol. 22(3), 293–301 (2011)PubMedCrossRef

32.

P. Thornalley, N. Rabbani, Glyoxalase in tumourigenesis and multidrug resistance. Semin. Cell Dev. Biol. 22(3), 318–325 (2011)PubMedCrossRef

33.

S. Hoon, M. Gebbia, M. Costanzo, R. Davis, G. Giaever, C. Nislow, A global perspective of the genetic basis for carbonyl stress resistance. G3 (Bethesda) 1(3), 219–231 (2011)CrossRef

34.

M. Lin, H. Chen, T. Liao, T. Huang, C. Chen, J. Lee, Determination of time-dependent accumulation of d-lactate in the streptozotocin-induced diabetic rat kidney by column-switching HPLC with fluorescence detection. J. Chromatogr. B Analyt. Technol. Biomed. Life Sci. 879(29), 3214–3219 (2011)PubMedCrossRef

35.

Y. Kondoh, M. Kawase, M. Hirata, S. Ohmori, Carbon sources for d-lactate formation in rat liver. J. Biochem. 115(3), 590–595 (1994)PubMed

36.

T. Fujisawa, S. Akagi, M. Kawase, M. Yamamoto, S. Ohmori, d-lactate metabolism in starved Octopus ocellatus. J. Exp. Zool. A Comp. Exp. Biol. 303(6), 489–496 (2005)PubMed

37.

N. Rabbani, P.J. Thornalley, Glyoxalase in diabetes, obesity and related disorders. Semin. Cell Dev. Biol. 22(3), 309–317 (2011)PubMedCrossRef

38.

S. Falone, A. D’Alessandro, A. Mirabilio, G. Petruccelli, M. Cacchio, C. Di Ilio, S. Di Loreto, F. Amicarelli, Long term running biphasically improves methylglyoxal-related metabolism, redox homeostasis and neurotrophic support within adult mouse brain cortex. PLoS One 7(2), e31401 (2012)PubMedCrossRef

39.

K. Kim, Y. Kim, D. Jung, J. Lee, J. Kim, Increased glyoxalase I levels inhibit accumulation of oxidative stress and an advanced glycation end product in mouse mesangial cells cultured in high glucose. Exp. Cell Res. 318(2), 152–159 (2012)PubMedCrossRef

40.

A. Berner, O. Brouwers, R. Pringle, I. Klaassen, L. Colhoun, C. McVicar, S. Brockbank, J. Curry, T. Miyata, M. Brownlee, R. Schlingemann, C. Schalkwijk, A.W. Stitt, Protection against methylglyoxal-derived AGEs by regulation of glyoxalase 1 prevents retinal neuroglial and vasodegenerative pathology. Diabetologia 55(3), 845–854 (2012)PubMedCrossRef

41.

R. Inagi, T. Kumagai, T. Fujita, M. Nangaku, The role of glyoxalase system in renal hypoxia. Adv. Exp. Med. Biol. 662, 49–55 (2010)PubMedCrossRef

42.

M. Jack, J. Ryals, D. Wright, Protection from diabetes-induced peripheral sensory neuropathy—a role for elevated glyoxalase I? Exp. Neurol. 234(1), 62–69 (2012)PubMedCrossRef

43.

T. Fleming, J. Cuny, G. Nawroth, Z. Djuric, P. Humpert, M. Zeier, A. Bierhaus, P. Nawroth, Is diabetes an acquired disorder of reactive glucose metabolites and their intermediates? Diabetologia 55(4), 1151–1155 (2012)PubMedCrossRef

44.

A. Ceriello, M. Ihnat, J. Thorpe, The “metabolic memory”: is more than just tight glucose control necessary to prevent diabetic complications? J. Clin. Endocrinol. Metab. 94(2), 410–415 (2009)PubMedCrossRef

45.

H. Odani, J. Asami, A. Ishii, K. Oide, T. Sudo, A. Nakamura, N. Miyata, N. Otsuka, K. Maeda, J. Nakagawa, Suppression of renal alpha-dicarbonyl compounds generated following ureteral obstruction by kidney specific alpha-dicarbonyl/l-xylulose reductase. Ann. N. Y. Acad. Sci. 1126, 320–324 (2008)PubMedCrossRef

46.

N. Rabbani, P.J. Thornalley, Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome. Amino Acids 42(4), 1133–1142 (2012)PubMedCrossRef

47.

D. Li, M. Ferrari, E. Ellis, Human aldo-keto reductase AKR7A2 protects against the cytotoxicity and mutagenicity of reactive aldehydes and lowers intracellular reactive oxygen species in hamster V79-4 cells. Chem. Biol. Interact. 195(1), 25–34 (2012)PubMedCrossRef

48.

S. Baba, O. Barski, Y. Ahmed, T. O’Toole, D.J. Conklin, A. Bhatnagar, S. Srivastava, Reductive metabolism of AGE precursors: a metabolic route for preventing AGE accumulation in cardiovascular tissue. Diabetes 58(11), 2486–2497 (2009)PubMedCrossRef

49.

R. Narawongsanont, S. Kabinpong, B. Auiyawong, C. Tantitadapitak, Cloning and characterization of AKR4C14, a rice aldoketo reductase from Thai Jasmine rice. Protein J. 31(1), 35–42 (2012)PubMedCrossRef

50.

S. Baba, J. Hellmann, S. Srivastava, A. Bhatnagar, Aldose reductase (AKR1B3) regulates the accumulation of advanced glycosylation end products (AGEs) and the expression of AGE receptor (RAGE). Chem. Biol. Interact. 191(1–3), 357–363 (2011)PubMedCrossRef

51.

M. Laga, A. Cottyn, F. van Herreweghe, W. Vanden Berghe, G. Haegeman, P. Van Oostveldt, J. Vandekerckhove, K. Vancompernolle, Methylglyoxal suppresses TNF-α-induced NF-κB activation by inhibiting NF-κB DNA-binding. Biochem. Pharmacol. 74(4), 579–589 (2007)PubMedCrossRef

52.

S. Grimm, M. Horlacher, B. Catalgol, A. Hoehn, T. Reinheckel, T. Grune, Cathepsins D and L reduce the toxicity of advanced glycation end products. Free Radic. Biol. Med. 52(6), 1011–1023 (2012)PubMedCrossRef

53.

C. Bento, F. Marques, R. Fernandes, P. Pereira, Methylglyoxal alters the function and stability of critical components of the protein quality control. PLoS One 5(9), e13007 (2010)PubMedCrossRef

54.

K. Nakajou, S. Horiuchi, M. Sakai, N. Haraguchi, M. Tanaka, M. Takeya, M. Otagiri, Renal clearance of glycolaldehyde- and methylglyoxal-modified proteins in mice is mediated by mesangial cells through a class A scavenger receptor (SR-A). Diabetologia 48(2), 317–327 (2005)PubMedCrossRef

55.

S. Chetyrkin, W. Zhang, B. Hudson, A. Serianni, P. Voziyan, Pyridoxamine protects proteins from functional damage by 3-deoxyglucosone: mechanism of action of pyridoxamine. Biochemistry 47(3), 997–1006 (2008)PubMedCrossRef

56.

J. Kim, O. Kim, C. Kim, E. Sohn, K. Jo, J. Kim, Accumulation of argpyrimidine, a methylglyoxal-derived advanced glycation end product, increases apoptosis of lens epithelial cells both in vitro and in vivo. Exp. Mol. Med. 44(2), 167–175 (2012)PubMedCrossRef

57.

X. Fan, L. Xiaoqin, B. Potts, C. Strauch, I. Nemet, V. Monnier, Topical application of l-arginine blocks advanced glycation by ascorbic acid in the lens of hSVCT2 transgenic mice. Mol. Vis. 17, 2221–2227 (2011)PubMed

58.

L. Lv, X. Shao, H. Chen, C. Ho, S. Sang, Genistein inhibits advanced glycation end product formation by trapping methylglyoxal. Chem. Res. Toxicol. 24(4), 579–586 (2011)PubMedCrossRef

59.

A. Dhar, K. Desai, L. Wu, Alagebrium attenuates acute methylglyoxal-induced glucose intolerance in Sprague-Dawley rats. Br. J. Pharmacol. 159(1), 166–175 (2010)PubMedCrossRef

60.

H. Liu, H. Liu, W. Wang, C. Khoo, J. Taylor, L. Gu, Cranberry phytochemicals inhibit glycation of human hemoglobin and serum albumin by scavenging reactive carbonyls. Food Funct. 2(8), 475–482 (2011)PubMedCrossRef

61.

H. Liu, L. Gu, Phlorotannins from brown algae (Fucus vesiculosus) inhibited the formation of advanced glycation endproducts by scavenging reactive carbonyls. J. Agric. Food Chem. 60(5), 1326–1334 (2012)PubMedCrossRef

62.

M. Lu, R. Wang, X. Song, R. Chibbar, X. Wang, L. Wu, Q. Meng, Dietary soy isoflavones increase insulin secretion and prevent the development of diabetic cataracts in streptozotocin-induced diabetic rats. Nutr. Res. 28(7), 464–471 (2008)PubMedCrossRef

63.

P. Maher, R. Dargusch, J. Ehren, S. Okada, K. Sharma, D. Schubert, Fisetin lowers methylglyoxal dependent protein glycation and limits the complications of diabetes. PLoS One 6(6), e21226 (2011)PubMedCrossRef

64.

Z. Wang, C. Hsu, C. Huang, M. Yin, Anti-glycative effects of oleanolic acid and ursolic acid in kidney of diabetic mice. Eur. J. Pharmacol. 628(1–3), 255–260 (2010)PubMedCrossRef

65.

P. Muthenna, C. Akileshwari, G. Reddy, Ellagic acid, a new antiglycating agent: its inhibition of Nϵ-(carboxymethyl)lysine. Biochem. J. 442(1), 221–230 (2012)PubMedCrossRef

66.

S. Taneda, K. Honda, K. Tomidokoro, K. Uto, K. Nitta, H. Oda, Eicosapentaenoic acid restores diabetic tubular injury through regulating oxidative stress and mitochondrial apoptosis. Am. J. Physiol. Renal Physiol. 299(6), F1451–F1461 (2010)PubMedCrossRef

67.

X. Jia, D.J. Olson, A.R. Ross, L. Wu, Structural and functional changes in human insulin induced by methylglyoxal. FASEB J. 20, 1555–1557 (2006)PubMedCrossRef

68.

Y. Gao, Y. Wang, Site-selective modifications of arginine residues in human hemoglobin induced by methylglyoxal. Biochemistry 45, 15654–15660 (2006)PubMedCrossRef

69.

A. Cantero, M. Portero-Otin, V. Ayala, N. Auge, M. Sanson, M. Elbaz, J. Thiers, R. Pamplona, R. Salvayre, A. Negre-Salvayre, Methylglyoxal induces advanced glycation end product (AGEs) formation and dysfunction of PDGF receptor-beta: implications for diabetic atherosclerosis. FASEB J. 21, 3096–3106 (2007)PubMedCrossRef

70.

A. Biswas, B. Wang, M. Miyagi, R.H. Nagaraj, Effect of methylglyoxal modification on stress-induced aggregation of client proteins and their chaperoning by human alphaA crystallin. Biochem. J. 409, 771–777 (2008)PubMedCrossRef

71.

M.U. Ahmed, F. Brinkmann, T.P. Degenhardt, S. Thorpe, J. Baynes, N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem. J. 324, 565–570 (1997)PubMed

72.

N. Rabbani, P. Thornalley, The dicarbonyl proteome: proteins susceptible to dicarbonyl glycation at functional sites in health, aging, and disease. Ann. N. Y. Acad. Sci. 1126, 124–127 (2008)PubMedCrossRef

73.

R. Nagaraj, A. Panda, S. Shanthakumar, P. Santhoshkumar, N. Pasupuleti, B. Wang, A. Biswas, Hydroimidazolone modification of the conserved Arg12 in small heat shock proteins: studies on the structure and chaperone function using mutant mimics. PLoS One 7(1), e30257 (2012)PubMedCrossRef

74.

T. Kumagai, M. Nangaku, I. Kojima, R. Nagai, J. Ingelfinger, T. Miyata, T. Fujita, R. Inagi, Glyoxalase I overexpression ameliorates renal ischemic-reperfusion injury in rats. Am. J. Physiol. Renal Physiol. 296, F912–F921 (2009)PubMedCrossRef

75.

P. Matafome, D. Santos-Silva, J. Crisóstomo, T. Rodrigues, L. Rodrigues, C. Sena, P. Pereira, R. Seiça, Methylglyoxal causes structural and functional alterations in adipose tissue independently of obesity. Arch. Physiol. Biochem. 118(2), 58–68 (2012)PubMedCrossRef

76.

J.W. Baynes, The Maillard hypothesis on aging: time to focus on DNA. Ann. N. Y. Acad. Sci. 959, 360–367 (2002)PubMedCrossRef

77.

M.J. Roberts, G.T. Wondrak, D.C. Laurean, M.K. Jacobson, E. Jacobson, DNA damage by carbonyl stress in human skin cells. Mutat. Res. 522(1–2), 45–56 (2003)PubMed

78.

P.J. Thornalley, Protecting the genome: defence against nucleotide glycation and emerging role of glyoxalase I overexpression in multidrug resistance in cancer chemotherapy. Biochem. Soc. Trans. 31(Pt 6), 1372–1377 (2003)PubMedCrossRef

79.

A. Guerin-Dubourg, A. Catan, E. Bourdon, P. Rondeau, Structural modifications of human albumin in diabetes. Diabetes Metab. 38(2), 171–178 (2012)PubMedCrossRef

80.

S. Yamagishi, Y. Inagaki, T. Okamoto, S. Amano, K. Koga, M. Takeuchi, Advanced glycation end products inhibit de novo protein synthesis and induce TGF-beta overexpression in proximal tubular cells. Kidney Int. 63(2), 464–473 (2003)PubMedCrossRef

81.

T. Lund, A. Svindland, M. Pepaj, A. Jensen, J. Berg, B. Kilhovd, K. Hanssen, Fibrin(ogen) may be an important target for methylglyoxal-derived AGE modification in elastic arteries of humans. Diab. Vasc. Dis. Res. 8(4), 284–294 (2011)PubMedCrossRef

82.

M. Mukohda, M. Okada, Y. Hara, H. Yamawaki, Exploring mechanisms of diabetes-related macrovascular complications: role of methylglyoxal, a metabolite of glucose on regulation of vascular contractility. J. Pharmacol. Sci. 118(3), 303–310 (2012)PubMedCrossRef

83.

M. Mukohda, T. Morita, M. Okada, Y. Hara, H. Yamawaki, Long-term methylglyoxal treatment impairs smooth muscle contractility in organ-cultured rat mesenteric artery. Pharmacol. Res. 65(1), 91–99 (2012)PubMedCrossRef

84.

A. Pozzi, R. Zent, S. Chetyrkin, C. Borza, N. Bulus, P. Chuang, D. Chen, B. Hudson, P. Voziyan, Modification of collagen IV by glucose or methylglyoxal alters distinct mesangial cell functions. J. Am. Soc. Nephrol. 20(10), 2119–2125 (2009)PubMedCrossRef

85.

V. Pedchenko, S. Chetyrkin, P. Chuang, A. Ham, M. Sallem, P. Mathieson, B. Hudson, P. Voziyan, Mechanisms of perturbation of integrin-mediated cell-matrix interactions by reactive carbonyl compounds and its implication for pathogenesis of diabetic nephropathy. Diabetes 54, 2952–2960 (2005)PubMedCrossRef

86.

D. Yao, T. Taguchi, T. Matsumura, R. Pestell, D. Edelstein, I. Giardino, G. Suske, N. Rabbani, P. Thornalley, V. Sarthy, H. Hammes, M. Brownlee, High glucose increases angiopoietin-2 transcription in microvascular endothelial cells through methylglyoxal modification of mSin3A. J. Biol. Chem. 282, 31038–31045 (2007)PubMedCrossRef

87.

H. Thangarajah, D. Yao, E. Chang, Y. Shi, L. Jazayeri, I. Vial, R. Galiano, X. Du, R. Grogan, M. Galvez, M. Januszyk, M. Brownlee, G. Gurtner, The molecular basis for impaired hypoxia-induced VEGF expression in diabetic tissues. Proc. Natl. Acad. Sci. USA 106(32), 13505–13510 (2009)PubMedCrossRef

88.

C. Bento, R. Fernandes, J. Ramalho, C. Marques, F. Shang, A. Taylor, P. Pereira, The chaperone-dependent ubiquitin ligase chip targets HIF-1α for degradation in the presence of methylglyoxal. PLoS One 5(11), e15062 (2010)PubMedCrossRef

89.

C. Bento, R. Fernandes, P. Matafome, C. Sena, R. Seiça, P. Pereira, Methylglyoxal-induced imbalance in the ratio of vascular endothelial growth factor to angiopoietin 2 secreted by retinal pigment epithelial cells leads to endothelial dysfunction. Exp. Physiol. 95(9), 955–970 (2010)PubMed

90.

D. Vander Jagt, R. Hassebrook, L. Hunsaker, W. Brown, R. Royer, Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications. Chem. Biol. Interact. 130–132, 549–562 (2001)PubMedCrossRef

91.

G. Tang, Y. Minemoto, B. Dibling, N. Purcell, Z. Li, M. Karin, A. Lin, Inhibition of JNK activation through NF-κB target genes. Nature 414(6861), 6313–6317 (2001)CrossRef

92.

M. Queisser, D. Yao, S. Geisler, H. Hammes, G. Lochnit, E. Schleicher, M. Brownlee, K. Preissner, Hyperglycemia impairs proteasome function by methylglyoxal. Diabetes 59(3), 670–678 (2010)PubMedCrossRef

93.

A.K. Padival, J. Crabb, R. Nagaraj, Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells. FEBS Lett. 551(1–3), 113–118 (2003)PubMedCrossRef

94.

K. Desai, L. Wu, Free radical generation by methylglyoxal in tissues. Drug Metabol. Drug Interact. 23, 151–173 (2008)PubMedCrossRef

95.

L. Wu, B. Juurlink, Increased methylglyoxal and oxidative stress in hypertensive rat vascular smooth muscle cells. Hypertension 39, 809–814 (2002)PubMedCrossRef

96.

T. Chang, R. Wang, L. Wu, Methylglyoxal-induced nitric oxide and peroxynitrite production in vascular smooth muscle cells. Free Radic. Biol. Med. 38, 286–293 (2005)PubMedCrossRef

97.

A. Dhar, K. Desai, M. Kazachmov, P. Yu, L. Wu, Methylglyoxal production in vascular smooth muscle cells from different metabolic precursors. Metabolism 57, 1211–1220 (2008)PubMedCrossRef

98.

C. Sena, P. Matafome, J. Crisóstomo, L. Rodrigues, R. Fernandes, P. Pereira, R. Seiça, Methylglyoxal promotes oxidative stress and endothelial dysfunction. Pharmacol. Res. 65(5), 497–506 (2012)PubMedCrossRef

99.

R. Ward, K. McLeish, Methylglyoxal: a stimulus to neutrophil oxygen radical production in chronic renal failure? Nephrol. Dial. Transplant. 19, 1702–1707 (2004)PubMedCrossRef

100.

G. Leoncini, M. Poggi, Effects of methylglyoxal on platelet hydrogen peroxide accumulation, aggregation and release reaction. Cell Biochem. Funct. 14, 89–95 (1996)PubMed

101.

M.P. Kalapos, A. Littauer, H. de Groot, Has reactive oxygen a role in methylglyoxal toxicity? A study on cultured rat hepatocytes. Arch. Toxicol. 67, 369–372 (1993)PubMedCrossRef

102.

S. Di Loreto, V. Caracciolo, S. Colafarina, P. Sebastiani, A. Gasbarri, F. Amicarelli, Methylglyoxal induces oxidative stress-dependent cell injury and up-regulation of interleukin-1beta and nerve growth factor in cultured hippocampal neuronal cells. Brain Res. 1006, 157–167 (2004)PubMedCrossRef

103.

A. Akhand, K. Hossain, H. Mitsui, M. Kato, T. Miyata, R. Inagi, J. Du, K. Takeda, Y. Kawamoto, H. Suzuki, K. Kurokawa, I. Nakashima, Glyoxal and methylglyoxal trigger distinct signals for map family kinases and caspase activation in human endothelial cells. Free Radic. Biol. Med. 31, 20–30 (2001)PubMedCrossRef

104.

A. Uriuhara, S. Miyata, B. Liu, H. Miyazaki, H. Kusunoki, H. Kojima, Y. Yamashita, K. Suzuki, K. Inaba, M. Kasuga, Methylglyoxal induces prostaglandin E2 production in rat mesangial cells. Kobe J. Med. Sci. 53(6), 305–315 (2008)PubMed

105.

S. Kikuchi, K. Shinpo, F. Moriwaka, Z. Makita, T. Miyata, K. Tashiro, Neurotoxicity of methylglyoxal and 3-deoxyglucosone on cultured cortical neurons: synergism between glycation and oxidative stress, possibly involved in neurodegenerative diseases. J. Neurosci. Res. 57, 280–289 (1999)PubMedCrossRef

106.

F. Amicarelli, S. Colafarina, F. Cattani, A. Cimini, C. Di Ilio, M. Ceru, M. Miranda, Scavenging system efficiency is crucial for cell resistance to ROS-mediated methylglyoxal injury. Free Radic. Biol. Med. 35, 856–871 (2003)PubMedCrossRef

107.

C. Paget, M. Lecomte, D. Ruggiero, N. Wiernsperger, M. Lagarde, Modification of enzymatic antioxidants in retinal microvascular cells by glucose or advanced glycation end products. Free. Radic. Biol. Med. 25, 121–129 (1998)PubMedCrossRef

108.

H. Wang, J. Liu, L. Wu, Methylglyoxal-induced mitochondrial dysfunction in vascular smooth muscle cells. Biochem. Pharmacol. 77, 1709–1716 (2009)PubMedCrossRef

109.

K. Desai, T. Chang, H. Wang, A. Banigesh, A. Dhar, J. Liu, A. Untereiner, L. Wu, Oxidative stress and aging: is methylglyoxal the hidden enemy? Can. J. Physiol. Pharmacol. 88, 273–284 (2010)PubMedCrossRef

110.

D. Yao, M. Brownlee, Hyperglycemia-induced reactive oxygen species increase expression of the receptor for advanced glycation end products (RAGE) and RAGE ligands. Diabetes 59, 249–255 (2010)PubMedCrossRef

111.

S. Yan, R. Ramasamy, Y. Naka, A. Schmidt, Glycation, inflammation, and RAGE: a scaffold for the macrovascular complications of diabetes and beyond. Circ. Res. 93(12), 1159–1169 (2003)PubMedCrossRef

112.

R. Ramasamy, S. Yan, A. Schmidt, Advanced glycation endproducts: from precursors to RAGE: round and round we go. Amino Acids 42(4), 1151–1161 (2012)PubMedCrossRef

113.

H. Ueno, H. Koyama, T. Shoji, M. Monden, S. Fukumoto, S. Tanaka, Y. Otsuka, Y. Mima, T. Morioka, K. Mori, A. Shioi, H. Yamamoto, M. Inaba, Y. Nishizawa, Receptor for advanced glycation end products (RAGE) regulation of adiposity and adiponectin is associated with atherogenesis in apoE deficient mouse. Atherosclerosis 211(2), 431–436 (2010)PubMedCrossRef

114.

B. Leuner, M. Max, K. Thamm, C. Kausler, Y. Yakobus, A. Bierhaus, S. Sel, B. Hofmann, R. Silber, A. Simm, N. Nass, RAGE influences obesity in mice. Effects of the presence of RAGE on weight gain, AGE accumulation, and insulin levels in mice on a high fat diet. Z. Gerontol. Geriatr. 45(2), 102–108 (2012)PubMedCrossRef

115.

Y. Hattori, H. Kakishita, K. Akimoto, M. Matsumura, K. Kasai, Glycated serum albumin-induced vascular smooth muscle cell proliferation through activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by protein kinase C. Biochem. Biophys. Res. Commun. 281(4), 891–896 (2001)PubMedCrossRef

116.

C. Lu, J. He, W. Cai, H. Liu, L. Zhu, H. Vlassara, Advanced glycation endproduct (AGE) receptor 1 is a negative regulator of the inflammatory response to AGE in mesangial cells. Proc. Natl. Acad. Sci. USA 101(32), 11767–11772 (2004)PubMedCrossRef

117.

W. Cai, J.C. He, L. Zhu, X. Chen, G. Striker, H. Vlassara, AGE-receptor-1 counteracts cellular oxidant stress induced by AGEs via negative regulation of p66shc-dependent FKHRL1 phosphorylation. Am. J. Physiol. Cell Physiol. 294(1), C145–C152 (2008)PubMedCrossRef

118.

W. Cai, M. Torreggiani, L. Zhu, X. Chen, J. He, G. Striker, H. Vlassara, AGER1 regulates endothelial cell NADPH oxidase-dependent oxidant stress via PKC-delta: implications for vascular disease. Am. J. Physiol. Cell Physiol. 298(3), C624–C634 (2010)PubMedCrossRef

119.

J. Skrha Jr, J. Gáll, R. Buchal, E. Sedláčková, J. Pláteník, Glucose and its metabolites have distinct effects on the calcium-induced mitochondrial permeability transition. Folia Biol. (Praha) 57(3), 96–103 (2011)

120.

A. Remor, F. de Matos, K. Ghisoni, T. da Silva, G. Eidt, M. Búrigo, A. de Bem, P. Silveira, A. de León, M. Sanchez, A. Hohl, V. Glaser, C. Gonçalves, A. Quincozes-Santos, R. Borba Rosa, A. Latini, Differential effects of insulin on peripheral diabetes-related changes in mitochondrial bioenergetics: involvement of advanced glycosylated end products. Biochim. Biophys. Acta. 1812(11), 1460–1471 (2011)PubMedCrossRef

121.

B. Liu, S. Miyata, Y. Hirota, S. Higo, H. Miyazaki, M. Fukunaga, Y. Hamada, S. Ueyama, O. Muramoto, A. Uriuhara, M. Kasuga, Methylglyoxal induces apoptosis through activation of p38 mitogen-activated protein kinase in rat mesangial cells. Kidney Int. 63(3), 947–957 (2003)PubMedCrossRef

122.

C. Ho, P. Lee, W. Huang, Y. Hsu, C. Lin, J. Wang, Methylglyoxal-induced fibronectin gene expression through Ras-mediated NADPH oxidase activation in renal mesangial cells. Nephrology (Carlton) 12(4), 348–356 (2007)CrossRef

123.

J. Kim, O. Kim, C. Kim, N. Kim, J. Kim, Cytotoxic role of methylglyoxal in rat retinal pericytes: involvement of a nuclear factor-kappaB and inducible nitric oxide synthase pathway. Chem. Biol. Interact. 188(1), 86–93 (2010)PubMedCrossRef

124.

M. Kalapos, The tandem of free radicals and methylglyoxal. Chem. Biol. Interact. 171(3), 251–271 (2008)PubMedCrossRef

125.

J. Du, S. Cai, H. Suzuki, A. Akhand, X. Ma, Y. Takagi, T. Miyata, I. Nakashima, F. Nagase, Involvement of MEKK1/ERK/P21Waf1/Cip1 signal transduction pathway in inhibition of IGF-I-mediated cell growth response by methylglyoxal. J. Cell. Biochem. 88(6), 1235–1246 (2003)PubMedCrossRef

126.

C. Schalkwijk, O. Brouwers, C. Stehouwer, Modulation of insulin action by advanced glycation endproducts: a new player in the field. Horm. Metab. Res. 40(9), 614–619 (2008)PubMedCrossRef

127.

A. Riboulet-Chavey, A. Pierron, I. Durand, J. Murdaca, J. Giudicelli, E. Van Obberghen, Methylglyoxal impairs the insulin signaling pathways independently of the formation of intracellular reactive oxygen species. Diabetes 55(5), 1289–1299 (2006)PubMedCrossRef

128.

X. Jia, L. Wu, Accumulation of endogenous methylglyoxal impaired insulin signaling in adipose tissue of fructose-fed rats. Mol. Cell. Biochem. 306, 133–139 (2007)PubMedCrossRef

129.

A. Dhar, I. Dhar, B. Jiang, K. Desai, L. Wu, Chronic methylglyoxal infusion by minipump causes pancreatic beta-cell dysfunction and induces type 2 diabetes in Sprague-Dawley rats. Diabetes 60(3), 899–908 (2011)PubMedCrossRef

130.

Q. Guo, T. Mori, Y. Jiang, C. Hu, Y. Osaki, Y. Yoneki, Y. Sun, T. Hosoya, A. Kawamata, S. Ogawa, M. Nakayama, T. Miyata, S. Ito, Methylglyoxal contributes to the development of insulin resistance and salt sensitivity in Sprague-Dawley rats. J. Hypertens. 27(8), 1664–1671 (2009)PubMedCrossRef

131.

S. Hofmann, H. Dong, Z. Li, W. Cai, J. Altomonte, S. Thung, F. Zeng, E. Fisher, H. Vlassara, Improved insulin sensitivity is associated with restricted intake of dietary glycoxidation products in the db/db mouse. Diabetes 51(7), 2082–2089 (2002)PubMedCrossRef

132.

F. Fiory, A. Lombardi, C. Miele, J. Giudicelli, F. Beguinot, E. Van Obberghen, Methylglyoxal impairs insulin signalling and insulin action on glucose-induced insulin secretion in the pancreatic beta cell line INS-1E. Diabetologia 54(11), 2941–2952 (2011)PubMedCrossRef

133.

L. Cook, J. Davies, A. Yates, A. Elliott, J. Lovell, J. Joule, P. Pemberton, P.J. Thornalley, L. Best, Effects of methylglyoxal on rat pancreatic beta-cells. Biochem. Pharmacol. 55(9), 1361–1367 (1998)PubMedCrossRef

134.

J.W. Baynes, S. Thorpe, Glycoxidation and lipoxidation in atherogenesis. Free Radic. Biol. Med. 28, 1708–1716 (2000)PubMedCrossRef

135.

T. Chang, L. Wu, Methylglyoxal, oxidative stress, and hypertension. Can. J. Physiol. Pharmacol. 84, 1229–1238 (2006)PubMedCrossRef

136.

D. Vander Jagt, L. Hunsaker, T. Vander Jagt, M. Gomez, D. Gonzales, L. Deck, R. Royer, Inactivation of glutathione reductase by 4-hydroxynonenal and other endogenous aldehydes. Biochem. Pharmacol. 53, 1133–1140 (1997)PubMedCrossRef

137.

S. Hou, P. Nori, J. Fang, C. Vaca, Methylglyoxal induces hprt mutation and DNA adducts in human T lymphocytes in vitro. Environ. Mol. Mutagen. 26, 286–291 (1995)PubMedCrossRef

138.

Y. Kang, L. Edwards, P.J. Thornalley, Effect of methylglyoxal on human leukaemia 60 cell growth: modification of DNA G1 growth arrest and induction of apoptosis. Leuk. Res. 20, 397–405 (1996)PubMedCrossRef

139.

J. Du, H. Suzuki, F. Nagase, A. Akhand, X. Ma, T. Yokoyama, T. Miyata, I. Nakashima, Superoxide-mediated early oxidation and activation of ASK1 are important for initiating methylglyoxal-induced apoptosis process. Free Radic. Biol. Med. 31, 469–478 (2001)PubMedCrossRef

140.

A. Okado, Y. Kawasaki, Y. Hasuike, M. Takahashi, T. Teshima, J. Fujii, N. Taniguchi, Induction of apoptotic cell death by methylglyoxal and 3-deoxyglucosone in macrophage-derived cell lines. Biochem. Biophys. Res. Commun. 225, 219–224 (1996)PubMedCrossRef

141.

A. De Vriese, J. Van De Voorde, H. Blom, P. Vanhoutte, M. Verbeke, N. Lameire, The impaired renal vasodilator response attributed to endothelium-derived hyperpolarizing factor in streptozotocin-induced diabetic rats is restored by 5-methyltetrahydrofolate. Diabetologia 43, 1116–1125 (2000)PubMedCrossRef

142.

H. Ding, M. Hashem, W. Wiehler, W. Lau, J. Martin, J. Reid, C. Triggle, Endothelial dysfunction in the streptozotocin-induced diabetic apoE deficient mouse. Br. J. Pharmacol. 146, 1110–1118 (2005)PubMedCrossRef

143.

M. Pannirselvam, W. Wiehler, T. Anderson, C. Triggle, Enhanced vascular reactivity of small mesenteric arteries from diabetic mice is associated with enhanced oxidative stress and cyclooxygenase products. Br. J. Pharmacol. 144, 953–960 (2005)PubMedCrossRef

144.

C. Sena, E. Nunes, T. Louro, T. Proença, R. Fernandes, M. Boarder, R. Seiça, Effects of alpha-lipoic acid on endothelial function in aged diabetic and high-fat fed rats. Br. J. Pharmacol. 153, 894–906 (2008)PubMedCrossRef

145.

N. Rabbani, L. Godfrey, M. Xue, F. Shaheen, M. Geoffrion, R. Milne, P.J. Thornalley, Glycation of LDL by methylglyoxal increases arterial atherogenicity: a possible contributor to increased risk of cardiovascular disease in diabetes. Diabetes 60(7), 1973–1980 (2011)PubMedCrossRef

146.

P. Thornalley, Dicarbonyl intermediates in the Maillard reaction. Ann. N. Y. Acad. Sci. 1043, 111–117 (2005)PubMedCrossRef

147.

N. Rabbani, M. Chittari, C. Bodmer, D. Zehnder, A. Ceriello, P.J. Thornalley, Increased glycation and oxidative damage to apolipoprotein B100 of LDL cholesterol in patients with type 2 diabetes and effect of metformin. Diabetes 59, 1038–1045 (2010)PubMedCrossRef

148.

P. Beisswenger, S.K. Howell, A. Touchette, S. Lal, B. Szwergold, Metformin reduces systemic methylglyoxal levels in type 2 diabetes. Diabetes 48, 198–202 (1999)PubMedCrossRef

149.

X. Wang, K. Desai, T. Chang, L. Wu, Vascular methylglyoxal metabolism and the development of hypertension. J. Hypertens. 23, 1565–1573 (2005)PubMedCrossRef

150.

X. Wang, K. Desai, J. Clausen, L. Wu, Increased methylglyoxal and advanced glycation end products in kidney from spontaneously hypertensive rats. Kidney Int. 66, 2315–2321 (2004)PubMedCrossRef

151.

X. Wang, X. Jia, T. Chang, K. Desai, L. Wu, Attenuation of hypertension development by scavenging methylglyoxal in fructose-treated rats. J. Hypertens. 26, 765–772 (2008)PubMedCrossRef

152.

S. Ogawa, K. Nakayama, M. Nakayama, T. Mori, M. Matsushima, M. Okamura, M. Senda, K. Nako, T. Miyata, S. Ito, Methylglyoxal is a predictor in type 2 diabetic patients of intima-media thickening and elevation of blood pressure. Hypertension 56, 471–476 (2010)PubMedCrossRef

153.

M. Beeri, E. Moshier, J. Schmeidler, J. Godbold, J. Uribarri, S. Reddy, M. Sano, H. Grossman, W. Cai, H. Vlassara, J. Silverman, Serum concentration of an inflammatory glycotoxin, methylglyoxal, is associated with increased cognitive decline in elderly individuals. Mech. Ageing Dev. 132(11–12), 583–587 (2011)PubMedCrossRef

154.

M. Fukunaga, S. Miyata, S. Higo, Y. Hamada, S. Ueyama, M. Kasuga, Methylglyoxal induces apoptosis through oxidative stress-mediated activation of p38 mitogen-activated protein kinase in rat Schwann cells. Ann. N. Y. Acad. Sci. 1043, 151–157 (2005)PubMedCrossRef

155.

J. Berlanga, D. Cibrian, I. Guillén, F. Freyre, J. Alba, P. Lopez-Saura, N. Merino, A. Aldama, A. Quintela, M. Triana, J. Montequin, H. Ajamieh, D. Urquiza, N. Ahmed, P.J. Thornalley, Methylglyoxal administration induces diabetes-like microvascular changes and perturbs the healing process of cutaneous wounds. Clin. Sci. (Lond) 109(1), 83–95 (2005)CrossRef

156.

X. Wang, W. Lau, Y. Yuan, Y. Wang, W. Yi, T. Christopher, B. Lopez, H. Liu, X. Ma, Methylglyoxal increases cardiomyocyte ischemia-reperfusion injury via glycative inhibition of thioredoxin activity. Am. J. Physiol. Endocrinol. Metab. 299(2), E207–E214 (2010)PubMed

157.

L. Vona-Davis, D. Rose, Angiogenesis, adipokines and breast cancer. Cytokine Growth Factor Rev. 20, 193–201 (2009)PubMedCrossRef

158.

A. Ozdemir, U. Hopfer, M. Rosca, X. Fan, V. Monnier, M. Weiss, Effects of advanced glycation end product modification on proximal tubule epithelial cell processing of albumin. Am. J. Nephrol. 28(1), 14–24 (2008)PubMedCrossRef

159.

M. Coughlan, S. Patel, G. Jerums, S. Penfold, T. Nguyen, K. Sourris, S. Panagiotopoulos, P. Srivastava, M. Cooper, L. Burrell, R. Macisaac, J. Forbes, Advanced glycation urinary protein-bound biomarkers and severity of diabetic nephropathy in man. Am. J. Nephrol. 34(4), 347–355 (2011)PubMedCrossRef

160.

S. Mauer, M. Steffes, E. Ellis, D. Sutherland, D. Brown, F. Goetz, Structural-functional relationships in diabetic nephropathy. J. Clin. Invest. 74, 1143–1155 (1984)PubMedCrossRef

161.

A. Mostafa, E. Randell, S. Vasdev, V. Gill, Y. Han, V. Gadag, A. Raouf, H. El Said, Plasma protein advanced glycation end products, carboxymethyl cysteine, and carboxyethyl cysteine, are elevated and related to nephropathy in patients with diabetes. Mol. Cell. Biochem. 302(1–2), 35–42 (2007)PubMedCrossRef

162.

B. Harcourt, K. Sourris, M. Coughlan, K. Walker, S. Dougherty, S. Andrikopoulos, A. Morley, V. Thallas-Bonke, V. Chand, S. Penfold, M. de Courten, M.C. Thomas, B.A. Kingwell, A. Bierhaus, M.E. Cooper, B. Courten, J.M. Forbes, Targeted reduction of advanced glycation improves renal function in obesity. Kidney Int. 80(2), 190–198 (2011)PubMedCrossRef

163.

S. Tang, L. Chan, J. Leung, A. Cheng, M. Lin, H. Lan, K. Lai, Differential effects of advanced glycation end-products on renal tubular cell inflammation. Nephrology (Carlton). 16(4), 417–425 (2011)CrossRef

164.

M. Rosca, T. Mustata, M. Kinter, A. Ozdemir, T. Kern, L. Szweda, M. Brownlee, V. Monnier, M. Weiss, Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation. Am. J. Physiol. Renal. Physiol. 289, F420–F430 (2005)PubMedCrossRef

165.

Y. Zhao, S. Banerjee, W. LeJeune, S. Choudhary, R. Tilton, NF-κB-inducing kinase increases renal tubule epithelial inflammation associated with diabetes. Exp. Diabetes Res. 2011, 192564 (2011)PubMedCrossRef

166.

S. Nakatani, A. Kakehashi, E. Ishimura, S. Yamano, K. Mori, M. Wei, M. Inaba, H. Wanibuchi, Targeted proteomics of isolated glomeruli from the kidneys of diabetic rats: sorbin and SH3 domain containing 2 is a novel protein associated with diabetic nephropathy. Exp. Diabetes Res. 2011, 979354 (2011)PubMedCrossRef

167.

A. Diez-Sampedro, O. Lenz, A. Fornoni, Podocytopathy in diabetes: a metabolic and endocrine disorder. Am. J. Kidney Dis. 58(4), 637–646 (2011)PubMedCrossRef

168.

D. Fosmark, J. Berg, A. Jensen, L. Sandvik, E. Agardh, C. Agardh, K. Hanssen. Increased retinopathy occurrence in type 1 diabetes patients with increased serum levels of the advanced glycation endproduct hydroimidazolone. Acta Ophthalmol. 87(5), 498–500 (2009)PubMedCrossRef

169.

Z. Wagner, P. Degrell, B. Lukáts, T. Niwa, G. Molnár, L. Markó, Z. Karádi, I. Wittmann, Accumulation of renin and imidazolone in peritubular capillary endothelial cells in insulin-resistant hypertensive rats. J. Nephrol. 24(5), 656–664 (2011)PubMedCrossRef

170.

X. Wang, K. Desai, B. Juurlink, J. de Champlain, L. Wu, Gender-related differences in advanced glycation endproducts, oxidative stress markers and nitric oxide synthases in rats. Kidney Int. 69(2), 281–287 (2006)PubMedCrossRef

171.

N. Reiniger, K. Lau, D. McCalla, B. Eby, B. Cheng, Y. Lu, W. Qu, N. Quadri, R. Ananthakrishnan, M. Furmansky, R. Rosario, F. Song, V. Rai, A. Weinberg, R. Friedman, R. Ramasamy, V. D’Agati, A. Schmidt, Deletion of the receptor for advanced Glycation end products reduces glomerulosclerosis and preserves renal function in the diabetic OVE26 mouse. Diabetes 59, 2043–2054 (2010)PubMedCrossRef

172.

D. Fosmark, J. Berg, A. Jensen, L. Sandvik, E. Agardh, C. Agardh, K. Hanssen, Increased retinopathy occurrence in type 1 diabetes patients with increased serum levels of the advanced glycation endproduct hydroimidazolone. Acta Ophthalmol. 87(5), 498–500 (2009)PubMedCrossRef

173.

O. Kim, J. Kim, C. Kim, N. Kim, J. Kim, KIOM-79 prevents methyglyoxal-induced retinal pericyte apoptosis in vitro and in vivo. J. Ethnopharmacol. 129(3), 285–292 (2010)PubMedCrossRef

174.

J. Kim, J. Son, J. Lee, Y. Oh, S. Shinn, Methylglyoxal induces apoptosis mediated by reactive oxygen species in bovine retinal pericytes. J. Korean Med. Sci. 19(1), 95–100 (2004)PubMedCrossRef

175.

R. Milne, S. Brownstein. Advanced glycation end products and diabetic retinopathy. Amino Acids (2011) [Epub Ahead of Print]

176.

J. Kim, C. Kim, Y. Lee, K. Jo, S. Shin, J. Kim, Methylglyoxal induces hyperpermeability of the bloodretinal barrier via the loss of tight junction proteins and the activation of matrix metalloproteinases. Graefes Arch. Clin. Exp. Ophthalmol. 250(5), 691–697 (2012)PubMedCrossRef

177.

O. Brouwers, P. Niessen, I. Ferreira, T. Miyata, P. Scheffer, T. Teerlink, P. Schrauwen, M. Brownlee, C. Stehouwer, C. Schalkwijk, Overexpression of glyoxalase-I reduces hyperglycemia-induced levels of advanced glycation endproducts and oxidative stress in diabetic rats. J. Biol. Chem. 286(2), 1374–1380 (2011)PubMedCrossRef

178.

A. Sartori, H. Garay-Malpartida, M. Forni, R. Schumacher, F. Dutra, M. Sogayar, E. Bechara, Aminoacetone, a putative endogenous source of methylglyoxal, causes oxidative stress and death in insulin-producing RINm5f cells. Chem. Res. Toxicol. 21(9), 1841–1850 (2008)PubMedCrossRef

179.

I. Nemet, L. Varga-Defterdarović, Z. Turk, Methylglyoxal in food and living organisms. Mol. Nutr. Food Res. 50(12), 1105–1117 (2006)PubMedCrossRef

180.

J. Adolphe, M. Drew, Q. Huang, T. Silver, L. Weber, Postprandial impairment of flow-mediated dilation and elevated methylglyoxal after simple but not complex carbohydrate consumption in dogs. Nutr. Res. 32(4), 278–284 (2012)PubMedCrossRef

181.

P.J. Beisswenger, S.K. Howell, R.M. O’Dell, M.E. Wood, A.D. Touchette, B.S. Szwergold, alpha-Dicarbonyls increase in the postprandial period and reflect the degree of hyperglycemia. Diabetes Care 24(4), 726–732 (2001)PubMedCrossRef

182.

A.G. Miller, G. Tan, K.J. Binger, R.J. Pickering, M.C. Thomas, R.H. Nagaraj, M.E. Cooper, J.L. Wilkinson-Berka, Candesartan attenuates diabetic retinal vascular pathology by restoring glyoxalase-I function. Diabetes 59(12), 3208–3215 (2010)PubMedCrossRef

183.

J. Xue, V. Rai, D. Singer, S. Chabierski, J. Xie, S. Reverdatto, D.S. Burz, A.M. Schmidt, R. Hoffmann, A. Shekhtman, Advanced glycation end product recognition by the receptor for AGEs. Structure 19(5), 722–732 (2011)PubMedCrossRef

184.

R. Ramasamy, S. Yan, A. Schmidt, Receptor for AGE (RAGE): signaling mechanisms in the pathogenesis of diabetes and its complications. Ann. N. Y. Acad. Sci. 1243, 88–102 (2011)PubMedCrossRef

Titel: Methylglyoxal, obesity, and diabetes
verfasst von: Paulo Matafome
Cristina Sena
Raquel Seiça
Publikationsdatum: 01.06.2013
Verlag: Springer US
Erschienen in: Endocrine / Ausgabe 3/2013
Print ISSN: 1355-008X
Elektronische ISSN: 1559-0100
DOI: https://doi.org/10.1007/s12020-012-9795-8

Leitlinien kompakt für die Innere Medizin

Mit medbee Pocketcards sicher entscheiden.

^{Seit 2022 gehört die medbee GmbH zum Springer Medizin Verlag}

Kostenlos registrieren

Neu im Fachgebiet Innere Medizin

Notfall-TEP der Hüfte ist auch bei 90-Jährigen machbar

26.04.2024 Hüft-TEP Nachrichten

Ob bei einer Notfalloperation nach Schenkelhalsfraktur eine Hemiarthroplastik oder eine totale Endoprothese (TEP) eingebaut wird, sollte nicht allein vom Alter der Patientinnen und Patienten abhängen. Auch über 90-Jährige können von der TEP profitieren.

Niedriger diastolischer Blutdruck erhöht Risiko für schwere kardiovaskuläre Komplikationen

25.04.2024 Hypotonie Nachrichten

Wenn unter einer medikamentösen Hochdrucktherapie der diastolische Blutdruck in den Keller geht, steigt das Risiko für schwere kardiovaskuläre Ereignisse: Darauf deutet eine Sekundäranalyse der SPRINT-Studie hin.

Bei schweren Reaktionen auf Insektenstiche empfiehlt sich eine spezifische Immuntherapie

25.04.2024 Allergien und Intoleranzreaktionen Nachrichten

Insektenstiche sind bei Erwachsenen die häufigsten Auslöser einer Anaphylaxie. Einen wirksamen Schutz vor schweren anaphylaktischen Reaktionen bietet die allergenspezifische Immuntherapie. Jedoch kommt sie noch viel zu selten zum Einsatz.

Therapiestart mit Blutdrucksenkern erhöht Frakturrisiko

25.04.2024 Hypertonie Nachrichten

Beginnen ältere Männer im Pflegeheim eine Antihypertensiva-Therapie, dann ist die Frakturrate in den folgenden 30 Tagen mehr als verdoppelt. Besonders häufig stürzen Demenzkranke und Männer, die erstmals Blutdrucksenker nehmen. Dafür spricht eine Analyse unter US-Veteranen.

Update Innere Medizin

Bestellen Sie unseren Fach-Newsletter und bleiben Sie gut informiert.

Newsletter bestellen

Springer Medizin

Abstract

Bitte loggen Sie sich ein, um Zugang zu diesem Inhalt zu erhalten

Weitere Artikel der Ausgabe 3/2013

Insulin therapy for type 2 diabetes

Swim training of monosodium l-glutamate-obese mice improves the impaired insulin receptor tyrosine phosphorylation in pancreatic islets

Thin core biopsy should help to discriminate thyroid nodules cytologically classified as indeterminate. A new sampling technique

Relationship between goiter and gender: a systematic review and meta-analysis

Lack of standardized description of TRAb assays