AGEs-rage system down-regulates sirt1 through the ubiquitin-proteasome pathway to promote fn and tgf-ß1 expression in male rat glomerular mesangial cells

Endocrinology

Volumn 156, Issue 1, 2015, Pages 268-279

  Huang, Kai Peng ^a   Chen, Cheng ^a   Hao, Jie ^a   Huang, Jun Ying ^a   Liu, Pei Qing ^a   Huang, He Qing ^a  

^a SUN YAT SEN UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

ADVANCED GLYCATION END PRODUCT; DEUBIQUITINASE; FIBRONECTIN; PROTEASOME; SIRTUIN 1; TRANSFORMING GROWTH FACTOR BETA1; UBIQUITIN; ADVANCED GLYCOSYLATION END-PRODUCT RECEPTOR; IMMUNOGLOBULIN RECEPTOR; THIOL ESTER HYDROLASE;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIABETIC NEPHROPATHY; DOWN REGULATION; HUMAN; HUMAN CELL; MALE; MESANGIUM CELL; NONHUMAN; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; RAT; UBIQUITINATION; UPREGULATION; ANIMAL; GENE EXPRESSION REGULATION; GENETICS; METABOLISM; PHYSIOLOGY; SPRAGUE DAWLEY RAT;

ANIMALS; FIBRONECTINS; GENE EXPRESSION REGULATION; GLYCOSYLATION END PRODUCTS, ADVANCED; MALE; RATS; RATS, SPRAGUE-DAWLEY; RECEPTORS, IMMUNOLOGIC; SIRTUIN 1; THIOLESTER HYDROLASES; TRANSFORMING GROWTH FACTOR BETA1;

EID: 84919725504     PISSN: 00137227     EISSN: 19457170     Source Type: Journal    
DOI: 10.1210/en.2014-1381     Document Type: Article

References (49)

1. Kanwar YS, Sun L, Xie P, Liu FY, Chen S. A glimpse of various pathogenetic mechanisms of diabetic nephropathy. Annu Rev Pathol Mech Dis. 2011;6:395-423
2. KanwarYS,WadaJ, Sun L, et al. Diabetic nephropathy: mechanisms of renal disease progression. Exp Biol Med. 2008;233(1):4-11
3. Schlöndorff D, Banas B. The mesangial cell revisited: no cell is an island. J Am Soc Nephrol. 2009;20(6):1179-1187
4. Wendt T, Tanji N, Guo J, et al. Glucose, glycation, and RAGE: Implications for amplification of cellular dysfunction in diabetic nephropathy. J Am Soc Nephrol. 2003;14(5):1383-1395
5. Fukami K, Yamagishi S, Ueda S, Okuda S. Role of AGEs in diabetic nephropathy. Curr Pharm Des. 2008;14(10):946-952
6. Yamagishi SI, Matsui T. Advanced glycation end products, oxidative stress and diabetic nephropathy. Oxid Med Cell Longev. 2010; 3(2):101-108
7. Houtkooper RH, Pirinen E, Auwerx J. Sirtuins as regulators of metabolism and healthspan. Nat Rev Mol Cell Biol. 2012;13(4):225-238
8. Rahman S, Islam R. Mammalian Sirt1: Insights on its biological functions. Cell Commun Signal. 2011;9:1-8
9. Hasegawa K, Wakino S, Simic P, et al. Renal tubular Sirt1 attenuates diabetic albuminuria by epigenetically suppressing Claudin-1 overexpression in podocytes. Nat Med. 2013;19(11):1496-1504
10. Kitada M, Kume S, Takeda-Watanabe A, Kanasaki K, Koya D. Sirtuins and renal diseases: Relationship with aging and diabetic nephropathy. Clin Sci (Lond). 2013;124(3):153-164
11. Huang K, Huang J, Xie X, et al. Sirt1 resists advanced glycation end products-induced expressions of fibronectin and TGF-ß1 by activating the Nrf2/ARE pathway in glomerular mesangial cells. Free Radic Biol Med. 2013;65:528-540
12. Goldberg AL. Nobel committee tags ubiquitin for distinction. Neuron. 2005;45(3):339-344
13. Sun SC. Deubiquitylation and regulation of the immune response. Nat Rev Immunol. 2008;8(7):501-511
14. Love KR, Catic A, Schlieker C, Ploegh HL. Mechanisms, biology and inhibitors of deubiquitinating enzymes. Nat Chem Biol. 2007; 3(11):697-705
15. Edelmann MJ, Kessler BM. Ubiquitin and ubiquitin-like specific proteases targeted by infectious pathogens: Emerging patterns and molecular principles. Biochim Biophys Acta. 2008;1782(12):809-816
16. Sacco JJ, Coulson JM, Clague MJ, Urbé S. Emerging roles of deubiquitinases in cancer-Associated pathways. IUBMB Life. 2010; 62(2):140-157
17. Revollo JR, Li X. The ways and means that fine tune Sirt1 activity. Trends Biochem Sci. 2013;38(3):160-167
18. Milner J. Cellular regulation of SIRT1. Curr Pharm Des. 2009; 15(1):39-44
19. Villalba JM, Alcaín FJ. Sirtuin activators and inhibitors. Biofactors. 2012;38(5):349-359
20. Flick F, Lüscher B. Regulation of sirtuin function by posttranslational modifications. Front Pharmacol. 2012;3:29
21. Sasaki T, Kim HJ, Kobayashi M, et al. Induction of hypothalamic Sirt1 leads to cessation of feeding via agouti-related peptide. Endocrinology. 2010;151(6):2556-2566
22. Hong EH, Lee SJ, Kim JS, et al. Ionizing radiation induces cellular senescence of articular chondrocytes via negative regulation of SIRT1 by p38 kinase. J Biol Chem. 2010;285(2):1283-1295
23. Gao Z, Zhang J, Kheterpal I, Kennedy N, Davis RJ, Ye JP. Sirtuin 1 (SIRT1) protein degradation in response to persistent c-Jun Nterminal kinase 1 (JNK1) activation contributes to hepatic steatosis in obesity. J Biol Chem. 2011;286(25):22227-22234
24. Geoffroy K, Wiernsperger N, Lagarde M, El Bawab S. Bimodal effect of advanced glycation end products on mesangial cell proliferation is mediated by neutral ceramidase regulation and endogenous sphingolipids. J Biol Chem. 2004;279(33):34343-34352
25. Perrone L, Peluso G, Melone MA. RAGE recycles at the plasma membrane in S100B secretory vesicles and promotes Schwann cells morphological changes. J Cell Physiol. 2008;217(1):60-71
26. Xie YB, Park JH, Kim DK, et al. Transcriptional corepressor SMILE recruits SIRT1 to inhibit nuclear receptor estrogen receptor-related receptor γ transactivation. J Biol Chem. 2009;284(42):28762-28774
27. Wilkinson KD, Ventii KH, Friedrich KL, Mullally JE. The ubiquitin signal: Assembly, recognition and termination. Symposium on ubiquitin and signaling. EMBO Rep. 2005;6(9):815-820
28. Ciechanover A, Stanhill A. The complexity of recognition of ubiquitinated substrates by the 26S proteasome. Biochim Biophys Acta. 2014;1843(1):86-96
29. Xie J, Méndez JD, Méndez-Valenzuela V, Aguilar-Hernández MM. Cellular signalling of the receptor for advanced glycation end products (RAGE). Cell Signal. 2013;25(11):2185-2197
30. Law IK, Liu L, Xu A, et al. Identification and characterization of proteins interacting with SIRT1 and SIRT3: Implications in the antiaging and metabolic effects of sirtuins. Proteomics. 2009;9(9): 2444-2456
31. Lin ZH, Yang HY, Kong QF, et al. USP22 antagonizes p53 transcriptional activation by deubiquitinating Sirt1 to suppress cell apoptosis and is required for mouse embryonic development. Mol Cell. 2012;46(4):1-11
32. Fukami K, Ueda S, Yamagishi S, et al. AGEs activate mesangial TGF-ß-Smad signaling via an angiotensin II type I receptor interaction. Kidney Int. 2004;66(6):2137-2147
33. 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
34. 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
35. Sourris KC, Morley AL, Koitka A, et al. Receptor for AGEs (RAGE) blockade may exert its renoprotective effects in patients with diabetic nephropathy via induction of the angiotensin II type 2 (AT2) receptor. Diabetologia. 2010;53(11):2442-2451
36. Grimm S, Ott C, Hörlacher M, Weber D, Höhn A, Grune T. Advanced-glycation-end-product-induced formation of immunoproteasomes: Involvement of RAGE and Jak2/STAT1. Biochem J. 2012;448(1):127-139
37. Shu T, Zhu Y, Wang H, Lin Y,MaZ, Han X. AGEs decrease insulin synthesis in pancreaticß-cell by repressing Pdx-1 protein expression at the post-translational level. PLoS One. 2011;6(4):e18782
38. Brune M, Müller M, Melino G, Bierhaus A, Schilling T, Nawroth PP. Depletion of the receptor for advanced glycation end products (RAGE) sensitizes towards apoptosis via p53 and p73 posttranslational regulation. Oncogene. 2013;32(11):1460-1468
39. Zhang XY, Varthi M, Sykes SM, et al. The putative cancer stem cell marker USP22 is a subunit of thehumanSAGAcomplex required for activated transcription and cell-cycle progression. Mol Cell. 2008; 29(1):102-111
40. Zhang XY, Pfeiffer HK, Thorne AW, McMahon SB. USP22, an hSAGA subunit and potential cancer stem cell marker, reverses the polycomb-catalyzed ubiquitylation of histone H2A. Cell Cycle. 2008;7(11):1522-1524
41. Atanassov BS, Dent SY. USP22 regulates cell proliferation by deubiquitinating the transcriptional regulator FBP1.EMBORep. 2011; 12(9):924-930
42. Armour SM, Bennett EJ, Braun CR, et al. A high-confidence interaction map identifies SIRT1 as a mediator of acetylation of USP22 and the SAGA coactivator complex. Mol Cell Biol. 2013;33(8): 1487-1502
43. Sussman RT, Stanek TJ, Esteso P, Gearhart JD, Knudsen KE, Mc-Mahon SB. The epigenetic modifier ubiquitin specific protease 22 (USP22) regulates embryonic stem cell differentiation via transcriptional repression of Sex determining region Y-box 2 (SOX2). J Biol Chem. 2013;288(33):24234-24246
44. Voorhees PM, Dees EC, O'Neil B, Orlowski RZ. The proteasome as a target for cancer therapy. Clin Cancer Res. 2003;9(17):6316-6325
45. Adams J, Kauffillan M. Development of the proteasome inhibitor Veleade (Bortezomib). Cancer Invesr. 2004;22(2):304-311
46. Song R, Peng W, Zhang Y, et al. Central role of E3 ubiquitin ligase MG53 in insulin resistance and metabolic disorders. Nature. 2013; 494(7437):375-379
47. Marfella R, D'Amico M, Esposito K, et al. The ubiquitin-proteasome system and inflammatory activity in diabetic atherosclerotic plaques: Effects of rosiglitazone treatment. Diabetes. 2006;55(3): 622-632
48. Kurihara T, Ozawa Y, Nagai N, et al. Angiotensin II type 1 receptor signaling contributes to synaptophysin degradation and neuronal dysfunction in the diabetic retina. Diabetes. 2008;57(8):2191-2198
49. Gao CL, Aqie K, Zhu JH, et al. MG132 ameliorates kidney lesions by inhibiting the degradation of Smad7 in streptozotocin-induced diabetic nephropathy. J Diabetes Res. 2014;2014:918396.