#PAGE_PARAMS# #ADS_HEAD_SCRIPTS# #MICRODATA#

Receptor pro konečné produkty pokročilé glykace (RAGE) – klíčový hráč diabetické angiopatie?


Authors: Jan Škrha Jr 1,2;  Marta Kalousová 2;  Tomáš Zima 2
Authors‘ workplace: III. interní klinika 1. LF UK a VFN Praha, přednosta prof. MUDr. Štěpán Svačina, DrSc., MBA 1;  Ústav lékařské biochemie a laboratorní diagnostiky 1. LF UK a VFN Praha, přednosta prof. MUDr. Tomáš Zima, DrSc., MBA 2
Published in: Vnitř Lék 2014; 60(9): 782-786
Category:

Overview

Receptor for advanced glycation end-products plays a crucial role in chronic diabetes complications. It is supposed to be involved in the development of all kinds of diabetic angiopathy. Advanced glycation end-products (AGEs) excessively accumulated in diabetes belong to the most important ligands of RAGE, however there are more potent activators of this receptor – especially alarmins, often involved in inflammatory reactions. Activated RAGE triggers pathways leading to excessive accumulation of AGEs, reactive oxygen species and sustained inflammatory reactions via NF-κB. Central role of RAGE in the pathogenesis of vascular changes in diabetes represents suitable target for new therapeutic or preventive approach.

Key words:
advanced glycation end-products – diabetes mellitus – hyperglycaemia – macroangiopathy – methylglyoxal – microangiopathy – receptor for advanced glycation end-products


Sources

1. IDF Diabetes Atlas 2012. 5th ed. Update 2012. Dostupné z WWW: <http://www.idf.org/sites/default/files/5E_IDFAtlasPoster_2012_EN.pdf>.

2. Zvolský M. Činnost oboru diabetologie, péče o diabetiky v roce 2012. ÚZIS 2013. Aktuální informace 2013; 24. Dostupné z WWW: <http://www.uzis.cz>.

3. Brownlee M. The pathobiology of diabetic complications – A unifying mechanism. Diabetes 2005; 54(6): 1615–1625.

4. Giacco F, Brownlee M. Oxidative stress and diabetic complications. Circ Res 2010; 107(9): 1058–1070.

5. Thornalley PJ. Glyoxalase I -structure, function and a critical role in the enzymatic defence against glycation. Biochem Soc Trans 2003; 31(Pt 6): 1343–1348.

6. Thornalley PJ. Dicarbonyl intermediates in the maillard reaction. Ann NY Acad Sci 2005; 1043: 111–117.

7. Makita Z, Radoff S, Rayfield EJ et al. Advanced glycosylation end products in patients with diabetic nephropathy. N Engl J Med 1991; 325(12): 836–842.

8. Schmidt AM, Vianna M, Gerlach M et al. Isolation and characterization of 2 binding-proteins for advanced glycosylation end-products from bovine lung which are present on the endothelial-cell surface. J Biol Chem 1992; 267(21): 14987–14997.

9. Ohgami N, Nagai R, Ikemoto M et al. Cd36, a member of the class b scavenger receptor family, as a receptor for advanced glycation end products. J Biol Chem 2001; 276(5): 3195–3202.

10. Rudijanto A. The expression and down stream effect of lectin like-oxidized low density lipoprotein 1 (LOX-1) in hyperglycemic state. Acta Med Indones 2007; 39(1): 36–43.

11. Katakami N, Matsuhisa M, Kaneto H et al. Endogenous secretory RAGE but not soluble RAGE is associated with carotid atherosclerosis in type 1 diabetes patients. Diab Vasc Dis Re 2008; 5(3): 190–197.

12. Vazzana N, Santilli F, Cuccurullo C et al. Soluble forms of RAGE in internal medicine. Intern Emerg Med 2009; 4(5): 389–401.

13. Wautier JL, Grossin N. sRAGE and esRAGE. Diabetes Metab 2008; 34(6 Pt 1): 631–631.

14. Yan SF, Ramasamy R, Schmidt AM. Soluble RAGE: therapy and biomarker in unraveling the RAGE axis in chronic disease and aging. Biochem Pharmacol 2010; 79(10): 1379–1386.

15. Yao D, Brownlee M Hyperglycemia-induced reactive oxygen species increase expression of the receptor for advanced glycation end products (RAGE) and RAGE ligands. Diabetes 2010; 59(1): 249–255.

16. Ma W, Rai V, Hudson BI et al. RAGE binds C1q and enhances C1q-mediated phagocytosis. Cell Immunol 2012; 274(1–2): 72–82.

17. Yamamoto Y, Harashima A, Saito H et al. Septic shock is associated with receptor for advanced glycation end products ligation of LPS. J Immunol 2011; 186(5): 3248–3257.

18. Rai V, Toure F, Chitayat S et al. Lysophosphatidic acid targets vascular and oncogenic pathways via RAGE signaling. J Exp Med 2012; 209(13): 2339–2350.

19. Yan SF, Ramasamy R, Schmidt AM. Receptor for AGE (RAGE) and its ligands-cast into leading roles in diabetes and the inflammatory response. J Mol Med (Berl) 2009; 87(3): 235–247.

20. Bierhaus A, Nawroth PP. Multiple levels of regulation determine the role of the receptor for AGE (RAGE) as common soil in inflammation, immune responses and diabetes mellitus and its complications. Diabetologia 2009; 52(11): 2251–2263.

21. Kosaki A, Hasegawa T, Kimura T et al. Increased plasma S100A12 (EN-RAGE) levels in patients with type 2 diabetes. J Clin Endocrinol Metab 2004; 89(11): 5423–5428.

22. Rai V, Maldonado AY, Burz DS et al. Signal transduction in receptor for advanced glycation end products (RAGE): solution structure of C-terminal rage (ctRAGE) and its binding to mDia1. J Biol Chem 2012; 287(7): 5133–5144.

23. Hudson BI, Kalea AZ, Del Mar Arriero M et al. Interaction of the RAGE cytoplasmic domain with diaphanous-1 is required for ligand-stimulated cellular migration through activation of Rac1 and Cdc42. J Biol Chem 2008; 283(49): 34457–34468.

24. Xie J, Mendez JD, Mendez-Valenzuela V et al. Cellular signalling of the receptor for advanced glycation end products (RAGE). Cell Signal 2013; 25(11): 2185–2197.

25. Wautier MP, Chappey O, Corda S et al. Activation of NADPH oxidase by AGE links oxidant stress to altered gene expression via RAGE. Am J Physiol Endocrinol Metab 2001; 280(5): E685-E694.

26. Reiniger N, Lau K, McCalla D et al. Deletion of the receptor for advanced glycation end products reduces glomerulosclerosis and preserves renal function in the diabetic OVE26 mouse. Diabetes 2010; 59(8): 2043–2054.

27. Niu W, Qi Y, Wu Z et al. A meta-analysis of receptor for advanced glycation end products gene: four well-evaluated polymorphisms with diabetes mellitus. Mol Cell Endocrinol 2012; 358(1): 9–17.

28. Tanji N, Markowitz GS, Fu C et al. Expression of advanced glycation end products and their cellular receptor RAGE in diabetic nephropathy and nondiabetic renal disease. J Am Soc Nephrol 2000; 11(9): 1656–1666.

29. Inagi R, Yamamoto Y, Nangaku M et al. A severe diabetic nephropathy model with early development of nodule-like lesions induced by megsin overexpression in RAGE/iNOS transgenic mice. Diabetes 2006; 55(2): 356–366.

30. Myint KM, Yamamoto Y, Doi T et al. RAGE control of diabetic nephropathy in a mouse model: effects of RAGE gene disruption and administration of low-molecular weight heparin. Diabetes 2006; 55(9): 2510–2522.

31. Yamaguchi Y, Iwano M, Suzuki D et al. Epithelial-mesenchymal transition as a potential explanation for podocyte depletion in diabetic nephropathy. Am J Kidney Dis 2009; 54(4): 653–664.

32. Skrha J Jr, Kalousova M, Svarcova J et al. Relationship of soluble RAGE and RAGE ligands HMGB1 and EN-RAGE to endothelial dysfunction in type 1 and type 2 diabetes mellitus. Exp Clin Endocrinol Diabetes 2012; 120(5): 277–281.

33. Kalousova M, Hodkova M, Kazderova M et al. Soluble receptor for advanced glycation end products in patients with decreased renal function. Am J Kidney Dis 2006; 47(3): 406–411.

34. Kalousova M, Bartosova K, Zima T et al. Pregnancy-associated plasma protein A and soluble receptor for advanced glycation end products after kidney transplantation. Kidney Blood Press Res 2007; 30(1): 31–37.

35. Skrha J, Soupal J, Ekali GL et al. Skin autofluorescence relates to soluble receptor for advanced glycation end-products and albuminuria in diabetes mellitus. J Diabetes Res 2013; 2013: 650694. Dostupné z DOI: <http://doi: 10.1155/2013/650694>.

36. Gaens KHJ, Ferreira I, van der Kallen CJH et al. Association of polymorphism in the receptor for advanced glycation end products (RAGE) gene with circulating RAGE levels. J Clin Endocrinol Metab 2009; 94(12): 5174–5180.

37. Krechler T, Jachymova M, Mestek O et al. Soluble receptor for advanced glycation end-products (sRAGE) and polymorphisms of RAGE and glyoxalase I genes in patients with pancreas cancer. Clin Biochem 2010; 43(10–11): 882–886.

38. Jang Y, Kim JY, Kang SM et al. Association of the Gly82Ser polymorphism in the receptor for advanced glycation end products (RAGE) gene with circulating levels of soluble RAGE and inflammatory markers in nondiabetic and nonobese Koreans. Metabolism 2007; 56(2): 199–205.

39. Kankova K, Stejskalova A, Hertlova M et al. Haplotype analysis of the RAGE gene: identification of a haplotype marker for diabetic nephropathy in type 2 diabetes mellitus. Nephrol Dial Transplant 2005; 20(6): 1093–1102.

40. Wendt TM, Tanji N, Guo J et al. RAGE drives the development of glomerulosclerosis and implicates podocyte activation in the pathogenesis of diabetic nephropathy. Am J Pathol 2003; 162(4): 1123–1137.

41. Manigrasso MB, Juranek J, Ramasamy R et al. Unlocking the biology of RAGE in diabetic microvascular complications. Trends Endocrinol Metab 2014; 25(1): 15–22.

42. Zong H, Ward M, Stitt AW. AGEs, RAGE, and diabetic retinopathy. Curr Diab Rep 2011; 11(4): 244–252.

43. Kerkeni M, Saidi A, Bouzidi H et al. Elevated serum levels of AGEs, sRAGE, and pentosidine in Tunisian patients with severity of diabetic retinopathy. Microvasc Res 2012; 84(3): 378–383.

44. Barile GR, Pachydaki SI, Tari SR et al. The RAGE axis in early diabetic retinopathy. Invest Ophthalmol Vis Sci 2005; 46(8): 2916–2924.

45. Mohammad G, Siddiquei MM, Othman A et al. High-mobility group box-1 protein activates inflammatory signaling pathway components and disrupts retinal vascular-barrier in the diabetic retina. Exp Eye Res 2013; 107: 101–109.

46. Thornalley PJ. Glycation in diabetic neuropathy: characteristics, consequences, causes, and therapeutic options. Int Rev Neurobiol 2002; 50: 37–57.

47. Dauch JR, Bender DE, Luna-Wong LA et al. Neurogenic factor-induced Langerhans cell activation in diabetic mice with mechanical allodynia. J Neuroinflammation 2013; 10: 64. Dostupné z DOI: <http://doi: 10.1186/1742–2094–10–64>.

48. Juranek JK, Geddis MS, Song F et al. RAGE deficiency improves postinjury sciatic nerve regeneration in type 1 diabetic mice. Diabetes 2013; 62(3): 931–943.

49. Toth C, Rong LL, Yang C et al. Receptor for advanced glycation end products (RAGEs) and experimental diabetic neuropathy. Diabetes 2008; 57(4): 1002–1017.

50. Burke AP, Kolodgie FD, Zieske A et al. Morphologic findings of coronary atherosclerotic plaques in diabetics: a postmortem study. Arterioscler Thromb Vasc Biol 2004; 24(7): 1266–1271.

51. Chen J, Song M, Yu S et al. 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(1–2): 137–146.

52. Soro-Paavonen A, Watson AM, Li J et al. Receptor for advanced glycation end products (RAGE) deficiency attenuates the development of atherosclerosis in diabetes. Diabetes 2008; 57(9): 2461–2469.

53. Bu DX, Rai V, Shen X et al. Activation of the ROCK1 branch of the transforming growth factor-beta pathway contributes to RAGE-dependent acceleration of atherosclerosis in diabetic ApoE-null mice. Circ Res 2010; 106(6): 1040–1051.

54. Morris-Rosenfeld S, Blessing E, Preusch MR et al. Deletion of bone marrow-derived receptor for advanced glycation end products inhibits atherosclerotic plaque progression. Eur J Clin Invest 2011; 41(11): 1164–1171.

55. Bucciarelli LG, Ananthakrishnan R, Hwang YC et al. RAGE and modulation of ischemic injury in the diabetic myocardium. Diabetes 2008; 57(7): 1941–1951.

56. Nielsen JM, Kristiansen SB, Norregaard R et al. Blockage of receptor for advanced glycation end products prevents development of cardiac dysfunction in db/db type 2 diabetic mice. Eur J Heart Fail 2009; 11(7): 638–647.

57. Distler MG, Plant LD, Sokoloff G et al. Glyoxalase 1 increases anxiety by reducing GABAA receptor agonist methylglyoxal. J Clin Invest 2012; 122(6): 2306–2315.

58. Ramasamy R, Yan SF, Schmidt AM. The diverse ligand repertoire of the receptor for advanced glycation endproducts and pathways to the complications of diabetes. Vascul Pharmacol 2012; 57(5–6): 160–167.

59. Kaida Y, Fukami K, Matsui T et al. DNA aptamer raised against AGEs blocks the progression of experimental diabetic nephropathy. Diabetes 2013; 62(9): 3241–3250.

60. Ishibashi Y, Matsui T, Takeuchi M et al. Metformin inhibits advanced glycation end products (AGEs)-induced renal tubular cell injury by suppressing reactive oxygen species generation via reducing receptor for AGEs (RAGE) expression. Horm Metab Res 2012; 44(12): 891–895.

61. Ishibashi Y, Yamagishi S, Matsui T et al. Pravastatin inhibits advanced glycation end products (AGEs)-induced proximal tubular cell apoptosis and injury by reducing receptor for AGEs (RAGE) level. Metabolism 2012; 61(8): 1067–1072.

62. Song F, Hurtado Del Pozo C, Rosario R et al. rage regulates the metabolic and inflammatory response to high-fat feeding in mice. Diabetes 2014; 63(6): 1948–1965.

Labels
Diabetology Endocrinology Internal medicine

Article was published in

Internal Medicine

Issue 9

2014 Issue 9

Most read in this issue
Topics Journals
Login
Forgotten password

Enter the email address that you registered with. We will send you instructions on how to set a new password.

Login

Don‘t have an account?  Create new account

#ADS_BOTTOM_SCRIPTS#