Retraction: PKC δ Promotes High Glucose Induced Renal Tubular Oxidative Damage via Regulating Activation and Translocation of p66Shc (Oxidative Medicine and Cellular Longevity (2014) 2014 (746531) DOI: 10.1155/2014/746531);PKC δ promotes high glucose induced renal tubular oxidative damage via regulating activation and translocation of p66Shc

Oxidative Medicine and Cellular Longevity

Volumn 2014, Issue , 2014, Pages

  Song, Panai ^a   Yang, Shikun ^a   Xiao, Li ^a   Xu, Xiaoxuan ^a   Tang, Chengyuan ^a   Yang, Yuyan ^a   Ma, Mingming ^a   Zhu, Jiefu ^a   Liu, Fuyou ^a   Sun, Lin ^a  

^a CENTRAL SOUTH UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL ACTIVATION; DISEASES; GLUCOSE; MITOCHONDRIA; PHOSPHORYLATION;

DIABETIC NEPHROPATHY; END STAGE RENAL DISEASE; KIDNEY DISEASE; MITOCHONDRIAL TRANSLOCATION; OXIDATIVE DAMAGE; POSITIVE CORRELATIONS; PRODUCTION PATHWAYS; TIME DEPENDENT;

ACTIVATION ANALYSIS;

ADAPTOR PROTEIN; GLUCOSE; HYDROGEN PEROXIDE; P66SHC PROTEIN; PROTEIN KINASE C DELTA; REACTIVE OXYGEN METABOLITE; ROTTLERIN; SMALL INTERFERING RNA; SUPEROXIDE; UNCLASSIFIED DRUG; ACETOPHENONE DERIVATIVE; BENZOPYRAN DERIVATIVE; PROTEIN SHC; SHC1 PROTEIN, HUMAN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DIABETIC NEPHROPATHY; HUMAN; HUMAN CELL; HUMAN TISSUE; HYPERGLYCEMIA; IN VITRO STUDY; KIDNEY PARENCHYMA; KIDNEY PROXIMAL TUBULE; KIDNEY TUBULE CELL; KIDNEY TUBULE DAMAGE; NONHUMAN; OXIDATIVE STRESS; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN TRANSPORT; RAT; ANTAGONISTS AND INHIBITORS; CELL LINE; DRUG EFFECTS; ENZYMOLOGY; GENE TRANSLOCATION; GENETICS; KIDNEY TUBULE; METABOLISM; MITOCHONDRION; PATHOLOGY; SIGNAL TRANSDUCTION;

ACETOPHENONES; BENZOPYRANS; CELL LINE; DIABETIC NEPHROPATHIES; GLUCOSE; HUMANS; KIDNEY TUBULES; MITOCHONDRIA; OXIDATIVE STRESS; PROTEIN KINASE C-DELTA; REACTIVE OXYGEN SPECIES; RNA, SMALL INTERFERING; SHC SIGNALING ADAPTOR PROTEINS; SIGNAL TRANSDUCTION; TRANSLOCATION, GENETIC;

EID: 84908353727     PISSN: 19420900     EISSN: 19420994     Source Type: Journal    
DOI: 10.1155/2022/9826078     Document Type: Erratum

References (43)

1. Kanwar Y. S., Sun L., Xie P., Liu F.-Y., Chen S., A glimpse of various pathogenetic mechanisms of diabetic nephropathy. Annual Review of Pathology: Mechanisms of Disease 2011 6 395 423 10.1146/annurev.pathol.4.110807.092150 2-s2.0-79751477368
2. Stanton R. C., Clinical challenges in diagnosis and management of diabetic kidney disease. American Journal of Kidney Diseases 2014 63 2 supplement 2 S3 S21 10.1053/j.ajkd.2013.10.050 2-s2.0-84892949060
3. Lau G. J., Godin N., Maachi H., Lo C.-S., Wu S.-J., Zhu J.-X., Brezniceanu M.-L., Chénier I., Fragasso-Marquis J., Lattouf J.-B., Ethier J., Filep J. G., Ingelfinger J. R., Nair V., Kretzler M., Cohen C. D., Zhang S.-L., Chan J. S. D., Bcl-2-modifying factor induces renal proximal tubular cell apoptosis in diabetic mice. Diabetes 2012 61 2 474 484 10.2337/db11-0141 2-s2.0-84863082340
4. Velagapudi C., Bhandari B. S., Abboud-Werner S., Simone S., Abboud H. E., Habib S. L., The tuberin/mTOR pathway promotes apoptosis of tubular epithelial cells in diabetes. Journal of the American Society of Nephrology 2011 22 2 262 273 10.1681/ASN.2010040352 2-s2.0-79551670515
5. Brezniceanu M.-L., Lau C. J., Godin N., Chénier I., Duclos A., Éthier J., Filep J. G., Ingelfinger J. R., Zhang S.-L., Chan J. S. D., Reactive oxygen species promote caspase-12 expression and tubular apoptosis in diabetic nephropathy. Journal of the American Society of Nephrology 2010 21 6 943 954 10.1681/ASN.2009030242 2-s2.0-77952967714
6. Morcos M., Sayed A. A. R., Bierhaus A., Yard B., Waldherr R., Merz W., Kloeting I., Schleicher E., Mentz S., Abd el Baki R. F., Tritschler H., Kasper M., Schwenger V., Hamann A., Dugi K. A., Schmidt A.-M., Stern D., Ziegler R., Haering H. U., Andrassy M., Van der Woude F., Nawroth P. P., Activation of tubular epithelial cells in diabetic nephropathy. Diabetes 2002 51 12 3532 3544 10.2337/diabetes.51.12.3532 2-s2.0-0036895708
7. Gilbert R. E., Cooper M. E., The tubulointerstitium in progressive diabetic kidney disease: more than an aftermath of glomerular injury? Kidney International 1999 56 5 1627 1637 10.1046/j.1523-1755.1999.00721.x 2-s2.0-0032731318
8. Shc generates reactive oxygen species that trigger mitochondrial apoptosis. Cell 2005 122 2 221 233 10.1016/j.cell.2005.05.011 2-s2.0-22744447211
9. Hall A. M., Unwin R. J., The not so "mighty chondrion": emergence of renal diseases due to mitochondrial dysfunction. Nephron Physiology 2006 105 1 1 10 10.1159/000096860 2-s2.0-33845808854
10. Migliaccio E., Giogio M., Mele S., Pelicci G., Reboldi P., Pandolfi P. P., Lanfrancone L., Pelicci P. G., The p66shc adaptor protein controls oxidative stress response and life span in mammals. Nature 1999 402 6759 309 313 10.1038/46311 2-s2.0-0033581704
11. Arany I., Faisal A., Clark J. S., Vera T., Baliga R., Nagamine Y., p66SHC-mediated mitochondrial dysfunction in renal proximal tubule cells during oxidative injury. The American Journal of Physiology-Renal Physiology 2010 298 5 F1214 F1221 10.1152/ajprenal.00639.2009 2-s2.0-77951560114
12. Sun L., Xiao L., Nie J., Liu F.-Y., Ling G.-H., Zhu X.-J., Tang W.-B., Chen W.-C., Xia Y.-C., Zhan M., Ma M.-M., Peng Y.-M., Liu H., Liu Y.-H., Kanwar Y. S., p66Shc mediates high-glucose and angiotensin II-induced oxidative stress renal tubular injury via mitochondrial-dependent apoptotic pathway. The American Journal of Physiology-Renal Physiology 2010 299 5 F1014 F1025 10.1152/ajprenal.00414.2010 2-s2.0-78349242850
13. Arany I., Faisal A., Nagamine Y., Safirstein R. L., p66shc inhibits pro-survival epidermal growth factor receptor/ERK signaling during severe oxidative stress in mouse renal proximal tubule cells. The Journal of Biological Chemistry 2008 283 10 6110 6117 10.1074/jbc.M708799200 2-s2.0-44449146636
14. Shc Science 2007 315 5812 659 663 10.1126/science.1135380 2-s2.0-33846817351
15. Kikkawa U., Matsuzaki H., Yamamoto T., Protein kinase C δ (PKC δ): activation mechanisms and functions. Journal of Biochemistry 2002 132 6 831 839 10.1093/oxfordjournals.jbchem.a003294 2-s2.0-0036947279
16. Persaud S. D., Hoang V., Huang J., Basu A., Involvement of proteolytic activation of PKC δ in cisplatin-induced apoptosis in human small cell lung cancer H69 cells. International Journal of Oncology 2005 27 1 149 154 2-s2.0-24644517020
17. Qi X., Disatnik M. H., Shen N., Sobel R. A., Mochly-Rosen D., Aberrant mitochondrial fission in neurons induced by protein kinase C δ under oxidative stress conditions in vivo. Molecular Biology of the Cell 2011 22 2 256 265 10.1091/mbc.E10-06-0551 2-s2.0-78751470559
18. Wang H., Xiao L., Kazanietz M. G., p23/Tmp21 associates with protein kinase C δ (PKC δ) and modulates its apoptotic function. The Journal of Biological Chemistry 2011 286 18 15821 15831 10.1074/jbc.M111.227991 2-s2.0-79955534014
19. 2-stimulated cells. The Journal of Biochemistry 2008 143 1 31 38 10.1093/jb/mvm190 2-s2.0-38849134147
20. Haruna Y., Kashihara N., Satoh M., Tomita N., Namikoshi T., Sasaki T., Fujimori T., Xie P., Kanwar Y. S., Amelioration of progressive renal injury by genetic manipulation of Klotho gene. Proceedings of the National Academy of Sciences of the United States of America 2007 104 7 2331 2336 10.1073/pnas.0611079104 2-s2.0-33847781131
21. Sun L., Zhang D., Liu F., Xiang X., Ling G., Xiao L., Liu Y., Zhu X., Zhan M., Yang Y., Kondeti V. K., Kanwar Y. S., Low-dose paclitaxel ameliorates fibrosis in the remnant kidney model by down-regulating miR-192. Journal of Pathology 2011 225 3 364 377 10.1002/path.2961 2-s2.0-80054771082
22. Sun L., Shukair S., Naik T. J., Moazed F., Ardehali H., Glucose phosphorylation and mitochondrial binding are required for the protective effects of hexokinases I and II. Molecular and Cellular Biology 2008 28 3 1007 1017 10.1128/MCB.00224-07 2-s2.0-38549163731
23. Li X., Pabla N., Wei Q., Dong G., Messing R. O., Wang C.-Y., Dong Z., PKC- δ promotes renal tubular cell apoptosis associated with proteinuria. Journal of the American Society of Nephrology 2010 21 7 1115 1124 10.1681/ASN.2009070760 2-s2.0-77954587516
24. Verzola D., Gandolfo M. T., Ferrario F., Rastaldi M. P., Villaggio B., Gianiorio F., Giannoni M., Rimoldi L., Lauria F., Miji M., Deferrari G., Garibotto G., Apoptosis in the kidneys of patients with type II diabetic nephropathy. Kidney International 2007 72 10 1262 1272 10.1038/sj.ki.5002531 2-s2.0-35848951893
25. Camici G. G., Schiavoni M., Francia P., Bachschmid M., Martin-Padura I., Hersberger M., Tanner F. C., Pelicci P., Volpe M., Anversa P., Lüscher T. F., Cosentino F., Genetic deletion of p66Shc adaptor protein prevents hyperglycemia-induced endothelial dysfunction and oxidative stress. Proceedings of the National Academy of Sciences of the United States of America 2007 104 12 5217 5222 10.1073/pnas.0609656104 2-s2.0-34247596394
26. Tomilov A. A., Bicocca V., Schoenfeld R. A., Giorgio M., Migliaccio E., Ramsey J. J., Hagopian K., Pelicci P. G., Cortopassi G. A., Decreased superoxide production in macrophages of long-lived p66Shc knock-out mice. Journal of Biological Chemistry 2010 285 2 1153 1165 10.1074/jbc.M109.017491 2-s2.0-74049115059
27. Vashistha H., Meggs L., Diabetic nephropathy: lessons from the mouse. Ochsner Journal 2013 13 1 140 146 2-s2.0-84875165676
28. shcA mediates obesity-induced insulin resistance. Proceedings of the National Academy of Sciences of the United States of America 2010 107 30 13420 13425 10.1073/pnas.1008647107 2-s2.0-77955798757
29. Paneni F., Mocharla P., Akhmedov A., Costantino S., Osto E., Volpe M., Lüscher T. F., Cosentino F., Gene silencing of the mitochondrial adaptor p66Shc suppresses vascular hyperglycemic memory in diabetes. Circulation Research 2012 111 3 278 289 10.1161/CIRCRESAHA.112.266593 2-s2.0-84864210978
30. shc via lectin-like oxidized low-density lipoprotein receptor-1, protein kinase c- β and c-jun n-terminal kinase kinase in human endothelial cells. Arteriosclerosis, Thrombosis, and Vascular Biology 2011 31 9 2090 2097 10.1161/ATVBAHA.111.229260 2-s2.0-80052175705
31. Chen Z., Wang G., Zhai X., Hu Y., Gao D., Ma L., Yao J., Tian X., Selective inhibition of protein kinase C β 2 attenuates the adaptor P66Shc-mediated intestinal ischemia-reperfusion injury. Cell Death and Disease 2014 5 4 e1164 10.1038/cddis.2014.131 2-s2.0-84901028902
32. Liu S., Yuan Q., Zhao S., Wang J., Guo Y., Wang F., Zhang Y., Liu Q., Zhang S., Ling E.-A., Hao A., High glucose induces apoptosis in embryonic neural progenitor cells by a pathway involving protein PKC δ Cellular Signalling 2011 23 8 1366 1374 10.1016/j.cellsig.2011.03.019 2-s2.0-79955862104
33. Acin-Perez R., Hoyos B., Gong J., Vinogradov V., Fischman D. A., Leitges M., Borhan B., Starkov A., Manfredi G., Hammerling U., Regulation of intermediary metabolism by the PKC δ signalosome in mitochondria. The FASEB Journal 2010 24 12 5033 5042 10.1096/fj.10-166934 2-s2.0-78649734511
34. Davies S. P., Reddy H., Caivano M., Cohen P., Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochemical Journal 2000 351 1 95 105 10.1042/0264-6021:3510095 2-s2.0-0034306450
35. Lin C. S., Lin F. Y., Ho L. J., PKC δ signalling regulates SR-A and CD36 expression and foam cell formation. Cardiovascular Research 2012 95 3 346 355 10.1093/cvr/cvs189
36. Talior I., Tennenbaum T., Kuroki T., Eldar-Finkelman H., PKC- δ -dependent activation of oxidative stress in adipocytes of obese and insulin-resistant mice: role for NADPH oxidase. The American Journal of Physiology-Endocrinology and Metabolism 2005 288 2 E405 E411 10.1152/ajpendo.00378.2004 2-s2.0-12144273607
37. Leitges M., Mayr M., Braun U., Mayr U., Li C., Pfister G., Ghaffari-Tabrizi N., Baier G., Hu Y., Xu Q., Exacerbated vein graft arteriosclerosis in protein kinase C δ -null mice. The Journal of Clinical Investigation 2001 108 10 1505 1512 10.1172/JCI200112902 2-s2.0-0035179086
38. Murriel C. L., Churchill E., Inagaki K., Szweda L. I., Mochly-Rosen D., Protein kinase C δ activation induces apoptosis in response to cardiac ischemia and reperfusion damage: a mechanism involving bad and the mitochondria. The Journal of Biological Chemistry 2004 279 46 47985 47991 10.1074/jbc.M405071200 2-s2.0-9144256765
39. Churchill E. N., Szweda L. I., Translocation of δ PKC to mitochondria during cardiac reperfusion enhances superoxide anion production and induces loss in mitochondrial function. Archives of Biochemistry and Biophysics 2005 439 2 194 199 10.1016/j.abb.2005.05.007 2-s2.0-21544446752
40. Leitges M., Gimborn K., Elis W., Kalesnikoff J., Hughes M. R., Krystal G., Huber M., Protein kinase C- δ is a negative regulator of antigen-induced mast cell degranulation. Molecular and Cellular Biology 2002 22 12 3970 3980 10.1128/MCB.22.12.3970-3980.2002 2-s2.0-0036258094
41. Mochly-Rosen D., Das K., Grimes K. V., Protein kinase C, an elusive therapeutic target? Nature Reviews Drug Discovery 2012 11 12 937 957 10.1038/nrd3871 2-s2.0-84870772239
42. Aiello L. P., Vignati L., Sheetz M. J., Zhi X., Girach A., Davis M. D., Wolka A. M., Shahri N., Milton R. C., Oral protein kinase c β inhibition using ruboxistaurin: efficacy, safety, and causes of vision loss among 813 patients (1,392 eyes) with diabetic retinopathy in the protein kinase c β inhibitor-diabetic retinopathy study and the protein kinase c β inhibitor-diabetic retinopathy study 2. Retina 2011 31 10 2084 2094 10.1097/IAE.0b013e3182111669 2-s2.0-80055100383
43. Tuttle K. R., McGill J. B., Haney D. J., Lin T. E., Anderson P. W., Kidney outcomes in long-term studies of ruboxistaurin for diabetic eye disease. Clinical Journal of the American Society of Nephrology 2007 2 4 631 636 10.2215/CJN.00840207 2-s2.0-34548836596