Proteomic analysis of human proximal tubular cells exposed to high glucose concentrations

Proteomics - Clinical Applications

Volumn 2, Issue 7-8, 2008, Pages 1118-1126

  So, Eun Jeong ^a   Kim, Hyun Jung ^a   Kim, Chan Wha ^a  

^a Korea University   (South Korea)

Author keywords

2 DE; Diabetic nephropathy; HK 2 cells

Indexed keywords

CELL PROTEIN; GLUCOSE; LACTATE DEHYDROGENASE;

ARTICLE; CELL CULTURE; CONCENTRATION RESPONSE; CONTROLLED STUDY; DIABETIC NEPHROPATHY; DOWN REGULATION; GLUCOSE BLOOD LEVEL; GLUCOSE METABOLISM; HUMAN; HUMAN CELL; HYPERGLYCEMIA; INTERSTITIAL NEPHRITIS; KIDNEY FUNCTION; KIDNEY TUBULE CELL; MASS SPECTROMETRY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEOMICS; TWO DIMENSIONAL ELECTROPHORESIS; UPREGULATION; WESTERN BLOTTING;

EID: 50849103366     PISSN: 18628346     EISSN: None     Source Type: Journal    
DOI: 10.1002/prca.200780151     Document Type: Article

References (48)

1. Yung, S., Lee, C. Y., Zhang, Q., Lau, S. K. et al., Elevated glucose induction of thrombospondin-1 up-regulates fibronectin synthesis in proximal renal tubular epithelial cells through TGF-beta1 dependent and TGF-beta1 independent pathways. Nephrol. Dial. Transplant. 2006, 21, 1504-1513.
2. Nath, K. A., Tubulointerstitial changes as a major determinant in the progression of renal damage. Am. J. Kidney Dis. 1992, 20, 1-17.
3. Panchapakesan, U., Pollock, C. A., Chen, X. M., The effect of high glucose and PPAR-gamma agonists on PPAR-gamma expression and function in HK-2 cells. Am. J. Physiol. Renal Physiol. 2004, 287, F528-F534.
4. Chow, F. Y., Nikolic-Paterson, D. J., Ozols, E., Atkins, R. C. et al., Monocyte chemoattractant protein-1 promotes the development of diabetic renal injury in streptozotocin-treated mice. Kidney Int. 2006, 69, 73-80.
5. Ha, H., Yu, M. R., Choi, Y. J., Kitamura, M., Lee, H. B., Role of high glucose-induced nuclear factor-kappaB activation in monocyte chemoattractant protein-1 expression by mesangial cells. J. Am. Soc. Nephrol. 2002, 13, 894-902.
6. Baynes, J. W., Role of axidative stress in development of complications in diabetes. Diabetes 1991, 40, 405-412.
7. Kang, B. P. S., Frencher, S., Reddy, V., Kessler, A. et al., High glucose promotes mesangial cell apoptosis by oxidant-dependent mechanism. Am. J. Physiol. Renal Physiol. 2003, 284, F455-F466.
8. Verzola, D., Bertolotto, M. B., Villaggio, B., Ottonello, L. et al., Taurine prevents apoptosis induced by high ambient glucose in human tubule renal cells. J. Invest. Med. 2002, 50, 443-451.
9. Allen, A. D., Harwood, S. M., Varagunam, M., Raftery, M. J., Vaqoob, M. M., High glucose-induced oxidative stress in proximal tubular epithelial cells and is mediated by multiple caspases. FASEB J. 2003, 17, 908-910.
10. Gilbert, R. E., Cooper, M. E., The tubulointerstitium in progressive diabetic kidney disease: More than an aftermath of glomerular injury? Kidney Int. 1999, 56, 1627-1637.
11. Phillips, A. O., Steadman, R., Diabetic nephropathy: The central role of renal proximal tubular cells in tubulointerstitial injury. Histol. Histopathol. 2002, 17, 247-252.
12. Qi, W., Chen, X., Gilbert, R. E., Zhang, Y. et al., High glucose-induced thioredoxin-interacting protein in renal proximal tubule cells is independent of transforming growth factor-beta1. Am. J. Pathol. 2007, 171, 744-754.
13. Kim, H. J., Cho, E. H., Yoo, J. H., Kim, P. K. et al., Proteome analysis of serum from type 2 diabetics with nephropathy. J. Proteome Res. 2007, 6, 735-743.
14. Cho, E. H., Kim, M. R., Kim, H. J., Lee, D. Y. et al., of Discovery of biomarkers for type 2 diabetic nephropathy by serum proteome analysis. Proteomics Clin. Appl. 2007, 1, 352-361.
15. Thongboonkerd, V., Barati, M. T., McLeish, K. R., Benarafa, C. et al., Alterations in the renal elastin-elastase system in type 1 diabetic nephropathy identified by proteomic analysis, J. Am. Soc. Nephrol. 2004, 15, 650-662.
16. Rao, P. V., Lu, X., Standley, M., Pattee, P. et al., Proteomic identification of urinary biomarkers of diabetic nephropathy. Diabetes Care 2007, 30, 629-637.
17. Bradford, M. M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254.
18. Kim, H. J., Kim, M. R., So, E. J., Kim, C. W., Comparison of proteomes in various human plasma preparations by two-dimensional gel electrophoresis. J. Biochem. Biophys. Methods 2007, 70, 619-625.
19. Yoo, B. S., Yoo, M. A., Song, Y. K., Byun, S. Y., Regulation of proteins related to melanogenesis by heartwood extract of Morus bombycis using proteome analysis. Biotechnol. Bioprocess Eng. 2007, 12, 662-667.
20. Kim, C. Y., Park, H. J., Kim, E. S., Proteomics-driven identification of putative AfsR2-target proteins stimulating antibiotic biosynthesis in Streptomyces lividans, Biotechnol. Bioprocess Eng. 2005, 10, 248-253.
21. Han, H. J., Choi, H. J., Park, S. H., High glucose inhibits glucose uptake in renal proximal tubule cells by oxidative stress and protein kinase C. Kidney Int. 2000, 57, 918-926.
22. Zhang, F., Hong, S., Stone, V., Smith, P. J. Expression of cannabinoid CB1 receptors in models of diabetic neuropathy. J. Pharmacol. Exp. Ther. 2007, 323, 508-515.
23. Sechi, L. A., Ceriello, A., Griffin, C. A., Catena, C. et al., Renal antioxidant enzyme mRNA levels are increased in rats with experimental diabetes mellitus. Diabetologia 1997, 40, 23-29.
24. Ha, H., Yoon, S. J., Kim, K. H., High glucose can induce lipid peroxidation in the isolated rat glomeruli. Kidney Int. 1994, 46, 1620-1626.
25. 2 toxicity between intact renal tubules and cultured proximal tubular cells. Biochem. Pharmacol. 1998, 56, 489-495.
26. Nahman, N. S., Jr., Leonhart, K. L., Cosio, F. G., Hebert, C. L., Effects of high glucose on cellular proliferation and fibronectin production by cultured human mesangial cells. Kidney Int. 1992, 41, 396-402.
27. Lorenzi, M., Cagliero, E., Toledo, S., Glucose toxicity for human endothelial cells in culture. Delayed replication, disturbed cell cycle, and accelerated death. Diabetes 1985, 34, 621-627.
28. Lee, Y. J., Lee, Y. J., Han, H. J., Regulatory mechanisms of Na(+)/ glucose cotransporters in renal proximal tubule cells. Kidney Int. Suppl. 2007, 106, S27-S35.
29. Piast, M., Kustrzeba-Wojcicka, I., Matusiewicz, M., Banas, T., Molecular evolution of enolase. Acta Biochim. Pol. 2005, 52, 507-513.
30. Pancholi, V., Multifunctional alpha-enolase: Its role in diseases. Cell Mol. Life Sci. 2001, 58, 902-920.
31. Merkulova, T., Lucas, M., Jabet, C., Biochemical characterization of the muscle-specific enolase: Developmental changes in electrophoretic variants and selective binding to other proteins. Biochem. J. 1997, 323, 791-800.
32. Foucault, G., Vacher, M., Merkulova, T., Keller, A. et al., Presence of enolase in the M-band of skeletal muscle and possible indirect interaction with the cytosolic muscle isoform of creatine kinase. Biochem. J. 1999, 338, 115-121.
33. Lee, K. H., Chung, H. S., Kim, H. S., Oh, S. H. et al., Human alpha-enolase from endothelial cells as a target antigen of anti-endothelial cell antibody in Behçet's disease. Arthritis Rheum. 2003, 48, 2025-2035.
34. Fontan, P. A., Pancholi, V., Nociari, M. M., Fischetti, V. A., Antibodies to streptococcal surface enolase react with human alpha-enolase: Implications in poststreptococcal sequelae. J. Infect. Dis. 2002, 182, 1712-1721.
35. Arza, B., Felez, J., Lopez-Alemany, R., Miles, L. A., Munoz-Canoves, P., Identification of an epitope of alpha-enolase (a candidate plasminogen receptor) by phage display. Thromb. Haemost. 1997, 78, 1097-1103.
36. Kim, P. K., Kim, M. R., Kim, H. J., Yoo, H. S. et al., Proteome analysis of the rat hepatic stellate cells under high concentrations of glucose. Proteomics 2007, 13, 2184-2188.
37. Miles, L. A., Dahlberg, C. M., Plescia, J., Felez, J. et al., Role of cell-surface lysines in plasminogen binding to cells: Identification of alpha-enolase as a candidate plasminogen receptor. Biochemistry 1991, 30, 1682-1691.
38. Redlitz, A., Fowler, B. J., Plow, E. F., Miles, L. A., The role of an enolase-related molecule in plasminogen binding to cells. Eur. J. Biochem. 1995, 227, 407-415.
39. Kursula, I., Partanen, S., Lambeir, A. M., Antonov, D. M. et al., Structural determinants for ligand binding and catalysis of triosephosphate isomerase. Eur. J. Biochem. 2001, 268, 5189-5196.
40. Brownlee, M., Biochemistry and molecular cell biology of diabetic complications. Nature 2001, 414, 813-820.
41. Randle, P. J., Phosphorylation-dephosphorylation cycles and the regulation of fuel selection in mammals. Curr. Topics Cell Reg. 1981, 18, 107-129.
42. Wieland, O., Siess, E., Schulze-Wethmar, F. H., Van Funcke, H. G., Winton, B., Active and inactive forms of pyruvate dehydrogenase in rat heart and kidney: Effect of diabetes, fasting and refeeding on pyruvate dekinase hydrogenase inter conversion. Arch. Biochem. Biophys. 1971, 143, 593-601.
43. Kerbey, A. L., Randle, P. J., Cooper, R. H., Whithehouse, S. et al., Regulation of pyruvate dehydrogenase in rat heart. Mechanism of proportions of dephosphorylated and phosphorylated enzyme by oxidation of fatty acids and ketone bodies and of effects of diabetes: Role of co-enzyme A, acetyl-coenzyme A and reduced and oxidized nicotinamide adenine dinucleotide. Biochem. J. 1976, 154, 327-348.
44. Randle, P. J., Pridstman, D. A., Mistry, S. C., Halsall, A., Mechanisms modifying glucose oxidation in diabetes mellitus. Diabetologia 1994, 37, S155-S161.
45. Liu, Y. Q., Moibi, J. A., Leahy, J. L., Chronic high glucose lowers pyruvate dehydrogenase activity in islets through enhanced production of long chain acyl-CoA: Prevention of impaired glucose oxidation by enhanced pyruvate recycling through the malate-pyruvate shuttle. J. Biol. Chem. 2004, 279, 7470-7475.
46. De La Peña, V. A., Diz Dios, P., Tojo Sierra, R., Relationship between lactate dehydrogenase activity in saliva and oral health status. Arch. Oral. Biol. 2007, 52, 911-915.
47. Liu, S. Q., Kang, J., Li, C. J., Tang, E. J. et al., Differences in expression of retinal proteins between diabetic and normal rats. World J. Gastroenterol. 2007, 13, 2118-2124.
48. Huang, C., Kim, Y., Caramori, M. L., Moore, J. H. et al., Diabetic nephropathy is associated with gene expression levels of oxidative phosphorylation and related pathways. Diabetes 2006, 55, 1826-1831.