Proteomic profile of primary isolated rat mesangial cells in high-glucose culture condition and decreased expression of psma6 in renal cortex of diabetic rats

Biochemistry and Cell Biology

Volumn 88, Issue 4, 2010, Pages 635-648

  Li, Zhiguo ^a   Zhang, Haojun ^b   Dong, Xi ^b   Burczynski, Frank J ^c   Choy, Patrick ^c   Yang, Fang ^d   Liu, Hui ^d   Li, Ping ^b   Gong, Yuewen ^c  

^a GRADUATE SCHOOL OF PEKING UNION MEDICAL COLLEGE   (China)

^b CHINA JAPAN FRIENDSHIP HOSPITAL   (China)

^c UNIVERSITY OF MANITOBA   (Canada)

^d North China Coal Medical University   (China)

Author keywords

Diabetic nephropathy; High glucose concentration; Mesangial cells; Proteomics

Indexed keywords

CULTURE CONDITIONS; DIABETIC NEPHROPATHY; DIABETIC PATIENT; DIABETIC RATS; EXTRACELLULAR MATRIX PROTEIN; GLOMERULAR MESANGIAL CELLS; GLUCOSE CONCENTRATION; IDENTIFICATION OF PROTEINS; MALDI TOF MS; MALDI-TOF-MS ANALYSIS; MATRIX-ASSISTED LASER DESORPTION-IONIZATION TIME-OF-FLIGHT MASS; MESANGIAL CELLS; NORMAL CONTROLS; PEPTIDE MASS FINGERPRINT; PROLIFERATION RATE; PROTEIN EXTRACTION; PROTEIN PROFILES; PROTEIN SPOTS; PROTEOMIC ANALYSIS; PROTEOMIC PROFILES; PROTEOMIC TECHNIQUES; PROTEOMICS; RAT MESANGIAL CELL; RAT MODEL; RENAL CORTEX; STREPTOZOTOCIN; THERAPEUTIC TARGETS; TOTAL PROTEIN; TWO-DIMENSIONAL GEL ELECTROPHORESIS; TWO-DIMENSIONAL GEL ELECTROPHORESIS (2-DE); WESTERN BLOTS; WESTERN-BLOT ANALYSIS;

CELL CULTURE; CELLS; DESORPTION; ELECTROPHORESIS; GELS; GLUCOSE; INDUCTIVELY COUPLED PLASMA; MASS SPECTROMETRY; MOLECULAR BIOLOGY; POLYACRYLATES; RATS; THERMAL STRESS; TWO DIMENSIONAL;

PROTEINS;

BINDING PROTEIN; CELL PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; GLUCOSE; POLY(RC) BINDING PROTEIN 1; PROTEASOME SUBUNIT ALPHA TYPE 6; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; DIABETES MELLITUS; GLOMERULUS; KIDNEY CORTEX; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; MESANGIUM CELL; NONHUMAN; PROTEIN EXPRESSION; PROTEOMICS; RAT; TWO DIMENSIONAL GEL ELECTROPHORESIS; WESTERN BLOTTING;

ANIMALS; CELL CULTURE TECHNIQUES; CELLS, CULTURED; DIABETES MELLITUS, EXPERIMENTAL; DIABETIC NEPHROPATHIES; DOSE-RESPONSE RELATIONSHIP, DRUG; DOWN-REGULATION; GLUCOSE; KIDNEY CORTEX; MALE; MESANGIAL CELLS; METABOLOME; PROTEASOME ENDOPEPTIDASE COMPLEX; PROTEOMICS; RATS; RATS, INBRED OLETF; RATS, SPRAGUE-DAWLEY; STREPTOZOCIN;

RATTUS;

EID: 77954935279     PISSN: 08298211     EISSN: 12086002     Source Type: Journal    
DOI: 10.1139/O09-185     Document Type: Article

References (47)

1. Abhary, S., Hewitt, A.W., Burdon, K.P., and Craig, J.E. 2009. A systematic meta-analysis of genetic association studies for diabetic retinopathy. Diabetes, 58(9): 2137-2147. doi:10.2337/db09-0059. PMID:19587357.
2. Arrigo, A.P. 2000. sHsp as novel regulators of programmed cell death and tumorigenicity. Pathol. Biol. (Paris), 48(3): 280-288.
3. Arrigo, A.P. 2001. Hsp27: novel regulator of intracellular redox state. IUBMB Life, 52(6): 303-307. doi:10.1080/152165401317291156. PMID:11895079.
4. Biron, D.G., Brun, C., Lefevre, T., Lebarbenchon, C., Loxdale, H.D., Chevenet, F., et al. 2006. The pitfalls of proteomics experiments without the correct use of bioinformatics tools. Proteomics, 6(20): 5577-5596. doi:10.1002/pmic.200600223. PMID:16991202.
5. Bradford, M.M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle Published by NRC Research Press of protein-dye binding. Anal. Biochem. 72(1-2): 248-254. doi:10.1016/0003-2697(76)90527-3. PMID:942051.
6. Cherney, D.Z., Scholey, J.W., and Miller, J.A. 2008. Insights into the regulation of renal hemodynamic function in diabetic mellitus. Curr. Diabetes Rev. 4(4): 280-290. doi:10.2174/157339908786241151. PMID:18991597.
7. Clarkson, M.R., Murphy, M., Gupta, S., Lambe, T., Mackenzie, H.S., Godson, C., et al. 2002. High glucose-altered gene expression in mesangial cells. Actin-regulatory protein gene expression is triggered by oxidative stress and cytoskeletal disassembly. J. Biol. Chem. 277(12): 9707-9712. doi:10.1074/jbc.M109172200. PMID:11784718.
8. Collins, G.A., and Tansey, W.P. 2006. The proteasome: a utility tool for transcription? Curr. Opin. Genet. Dev. 16(2): 197-202. doi:10.1016/j.gde.2006.02.009. PMID:16503126.
9. Ding, Q., Xiao, L., Xiong, S., Jia, Y., Que, H., Guo, Y., and Liu, S. 2003. Unmatched masses in peptide mass fingerprints caused by cross-contamination: an updated statistical result. Proteomics, 3(7): 1313-1317. doi:10.1002/pmic.200300452. PMID:12872232.
10. Foidart, J.B., Dechenne, C.A., Mahieu, P., Creutz, C.E., and de Mey, J. 1979. Tissue culture of normal rat glomeruli. Isolation and morphological characterization of two homogeneous cell lines. Invest. Cell Pathol. 2(1): 15-26. PMID:511605.
11. Fujita, H., Fujishima, H., Chida, S., Takahashi, K., Qi, Z., Kanetsuna, Y., et al. 2009. Reduction of renal superoxide dismutase in progressive diabetic nephropathy. J. Am. Soc. Nephrol. 20(6): 1303-1313. doi:10.1681/ASN.2008080844. PMID: 19470681.
12. Gong, D., Chen, X., Middleditch, M., Huang, L., Vazhoor Amarsingh, G., Reddy, S., et al. 2009. Quantitative proteomic profiling identifies new renal targets of copper(II)-selective chelation in the reversal of diabetic nephropathy in rats. Proteomics, 9(18): 4309-4320. doi:10.1002/pmic.200900285. PMID: 19634143.
13. Gorg, A., Obermaier, C., Boguth, G., Harder, A., Scheibe, B., Wildgruber, R., and Weiss, W. 2000. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis, 21(6): 1037-1053. doi:10.1002/(SICI)1522-2683(20000401)21:6<1037::AID-ELPS1037>3.0.CO;2-V. PMID:10786879.
14. Gross, J.L., de Azevedo, M.J., Silveiro, S.P., Canani, L.H., Caramori, M.L., and Zelmanovitz, T. 2005. Diabetic nephropathy: diagnosis, prevention, and treatment. Diabetes Care, 28(1): 164-176. doi:10.2337/diacare.28.1.164. PMID:15616252.
15. Gruden, G., Perin, P.C., and Camussi, G. 2005. Insight on the pathogenesis of diabetic nephropathy from the study of podocyte and mesangial cell biology. Curr. Diabetes Rev. 1(1): 27-40. doi:10.2174/1573399052952622. PMID:18220580.
16. Gruden, G., Bruno, G., Chaturvedi, N., Burt, D., Schalkwijk, C., Pinach, S., et al.; EURODIAB Prospective Complications Study Group. 2008. Serum heat shock protein 27 and diabetes complications in the EURODIAB prospective complications study: a novel circulating marker for diabetic neuropathy. Diabetes, 57(7): 1966-1970. doi:10.2337/db08-0009. PMID:18390793.
17. Haneda, M., Koya, D., Isono, M., and Kikkawa, R. 2003. Overview of glucose signaling in mesangial cells in diabetic nephropathy. J. Am. Soc. Nephrol. 14(5): 1374-1382. doi:10.1097/01.ASN. 0000064500.89551.76. PMID:12707407.
18. Hu, Z., Zhang, Z., Doo, E., Coux, O., Goldberg, A.L., and Liang, T.J. 1999. Hepatitis B virus X protein is both a substrate and a potential inhibitor of the proteasome complex. J. Virol. 73(9): 7231-7240. PMID: 10438810.
19. Kim, J.H., Sohn, S.Y., Benedict Yen, T.S., and Ahn, B.Y. 2008. Ubiquitin-dependent and -independent proteasomal degradation of hepatitis B virus X protein. Biochem. Biophys. Res. Commun. 366(4): 1036-1042. doi:10.1016/j.bbrc.2007.12.070. PMID:18155658.
20. Konstantinova, I.M., Tsimokha, A.S., and Mittenberg, A.G. 2008. Role of proteasomes in cellular regulation. Int Rev Cell Mol Biol, 267: 59-124. doi:10.1016/S1937-6448(08)00602-3. PMID: 18544497.
21. Kuan, C.J., al-Douahji, M., and Shankland, S.J. 1998. The cyclin kinase inhibitor p21WAF1, CIP1 is increased in experimental diabetic nephropathy: potential role in glomerular hypertrophy. J. Am. Soc. Nephrol. 9(6): 986-993. PMID:9621281.
22. Liu, S.Q., Kang, J., Li, C.J., Tang, E.J., Wen, B., Cai, R., and Yang, H.J. 2007. Differences in expression of retinal proteins between diabetic and normal rats. World J. Gastroenterol. 13(14): 2118-2124. PMID:17465459.
23. Mason, R.M., and Wahab, N.A. 2003. Extracellular matrix metabolism in diabetic nephropathy. J. Am. Soc. Nephrol. 14(5): 1358-1373. doi:10.1097/01.ASN.0000065640.77499.D7. PMID: 12707406.
24. Masson, E., Lagarde, M., Wiernsperger, N., and El Bawab, S. 2006. Hyperglycemia and glucosamine-induced mesangial cell cycle arrest and hypertrophy: Common or independent mechanisms? IUBMB Life, 58(7): 381-388. doi:10.1080/15216540600755980. PMID:16801212.
25. Mehlen, P., Mehlen, A., Godet, J., and Arrigo, A.P. 1997. hsp27 as a switch between differentiation and apoptosis in murine embryonic stem cells. J. Biol. Chem. 272(50): 31657-31665. doi:10.1074/jbc.272.50.31657. PMID:9395507.
26. Murphy, M., Crean, J., Brazil, D.P., Sadlier, D., Martin, F., and Godson, C. 2008. Regulation and consequences of differential gene expression in diabetic kidney disease. Biochem. Soc. Trans. 36(5): 941-945. doi:10.1042/BST0360941. PMID: 18793165.
27. Padival, A.K., Crabb, J.W., and Nagaraj, R.H. 2003. Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells. FEBS Lett. 551(1-3): 113-118. doi:10.1016/S0014-5793(03)00874-3. PMID:12965214.
28. Parcellier, A., Brunet, M., Schmitt, E., Col, E., Didelot, C., Hammann, A., et al. 2006. HSP27 favors ubiquitination and proteasomal degradation of p27Kip1 and helps S-phase re-entry in stressed cells. FASEB J. 20(8): 1179-1181. doi:10.1096/fj.05-4184fje. PMID:16641199.
29. Ramachandra Rao, S.P., Wassell, R., Shaw, M.A., and Sharma, K. 2007. Profiling of human mesangial cell subproteomes reveals a role for calmodulin in glucose uptake. Am. J. Physiol. Renal Physiol. 292(4): F1182-F1189. PMID:17200159.
30. Shin, A.H., Kil, I.S., Yang, E.S., Huh, T.L., Yang, C.H., and Park, J.W. 2004. Regulation of high glucose-induced apoptosis by mitochondrial NADP+-dependent isocitrate dehydrogenase. Biochem. Biophys. Res. Commun. 325(1): 32-38. doi:10.1016/j. bbrc.2004.09.218. PMID:15522197.
31. Sjakste, T., Poudziunas, I., Ninio, E., Perret, C., Pirags, V., Nicaud, V., et al. 2007. SNPs of PSMA6 gene[UNKNOWN ENTITY-]investigation of possible association with myocardial infarction and type 2 diabetes mellitus. Genetika, 43(4): 553-559. PMID:17555133.
32. Sol, E.R., Hovsepyan, M., and Bergsten, P. 2009. Proteins altered by elevated levels of palmitate or glucose implicated in impaired glucose-stimulated insulin secretion. Proteome Sci. 7(1): 7-24. doi:10.1186/1477-5956-7-24. PMID:19607692.
33. Steffes, M.W., Osterby, R., Chavers, B., and Mauer, S.M. 1989. Mesangial expansion as a central mechanism for loss of kidney function in diabetic patients. Diabetes, 38(9): 1077-1081. doi:10.2337/diabetes.38.9.1077. PMID:2670639.
34. Stokoe, D., Engel, K., Campbell, D.G., Cohen, P., and Gaestel, M. 1992. Identification of MAPKAP kinase 2 as a major enzyme responsible for the phosphorylation of the small mammalian heat shock proteins. FEBS Lett. 313(3): 307-313. doi:10.1016/0014-5793(92)81216-9. PMID:1332886.
35. Strippoli, G.F., Craig, M.C., Schena, F.P., and Craig, J.C. 2006. Role of blood pressure targets and specific antihypertensive agents used to prevent diabetic nephropathy and delay its progression. J. Am. Soc. Nephrol. 17(4 Suppl. 2): S153-S155. doi:10.1681/ASN.2005121337. PMID:16565242.
36. Tanaka, K. 2009. The proteasome: overview of structure and functions. Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. 85(1): 12-36. doi:10.2183/pjab.85.12. PMID:19145068.
37. Tessari, P., Puricelli, L., Iori, E., Arrigoni, G., Vedovato, M., James, P., et al. 2007. Altered chaperone and protein turnover regulators expression in cultured skin fibroblasts from type 1 diabetes mellitus with nephropathy. J. Proteome Res. 6(3): 976-986. doi:10.1021/pr060443n. PMID:17330940.
38. Thongboonkerd, V., Barati, M.T., McLeish, K.R., Benarafa, C., Remold-O'Donnell, E., Zheng, S., et al. 2004. Alterations in the renal elastin-elastase system in type 1 diabetic nephropathy identified by proteomic analysis. J. Am. Soc. Nephrol. 15(3): 650-662. doi:10.1097/01.ASN.0000115334.65095.9B. PMID: 14978167.
39. Tokumoto, T., Kondo, A., Miwa, J., Horiguchi, R., Tokumoto, M., Nagahama, Y., et al. 2003. Regulated interaction between polypeptide chain elongation factor-1 complex with the 26S protea-some during Xenopus oocyte maturation. BMC Biochem. 4(1): 6-16. doi:10.1186/1471-2091-4-6. PMID:12864926.
40. Wolf, G., Schroeder, R., Ziyadeh, F.N., Thaiss, F., Zahner, G., and Stahl, R.A. 1997. High glucose stimulates expression of p27Kip1 in cultured mouse mesangial cells: relationship to hy hypertrophy. Am. J. Physiol. 273(3 Pt 2): F348-F356. PMID:9321907.
41. Wolf, G., Schroeder, R., Thaiss, F., Ziyadeh, F.N., Helmchen, U., and Stahl, R.A. 1998. Glomerular expression of p27Kip1 in diabetic db/db mouse: role of hyperglycemia. Kidney Int. 53(4): 869-879. doi:10.1111/j.1523-1755.1998.00829.x. PMID:9551393.
42. Yalin, S., Hatungil, R., Tamer, L., Ates, N.A., Dogruer, N., Yildirim, H., et al. 2007. Glutathione S-transferase gene polymorphisms in Turkish patients with diabetes mellitus. Cell Biochem. Funct. 25(5): 509-513. doi:10.1002/cbf.1339. PMID:16927413.
43. Yan, X.X., Lu, L., Peng, W.H., Wang, L.J., Zhang, Q., Zhang, R.Y., et al. 2009. Increased serum HMGB1 level is associated with coronary artery disease in nondiabetic and type 2 diabetic patients. Atherosclerosis, 205(2): 544-548. doi:10.1016/j.atherosclerosis.2008.12.016. PMID:19150066.
44. Yang, S., Liu, T., Li, S., Zhang, X., Ding, Q., Que, H., et al. 2008. Comparative proteomic analysis of brains of naturally aging mice. Neuroscience, 154(3): 1107-1120. doi:10.1016/j.neuroscience.2008.04.012. PMID:18495355.
45. Zeeberg, B.R., Feng, W., Wang, G., Wang, M.D., Fojo, A.T., Sunshine, M., et al. 2003. GoMiner: a resource for biological interpretation of genomic and proteomic data. Genome Biol. 4(4): R28-R35. doi:10.1186/gb-2003-4-4-r28. PMID:12702209.
46. Zhang, Z., Torii, N., Furusaka, A., Malayaman, N., Hu, Z., and Liang, T.J. 2000. Structural and functional characterization of interaction between hepatitis B virus X protein and the proteasome complex. J. Biol. Chem. 275(20): 15157-15165. doi:10.1074/jbc.M910378199. PMID:10748218.
47. Zhang, F., Paterson, A.J., Huang, P., Wang, K., and Kudlow, J.E. 2007. Metabolic control of proteasome function. Physiology (Bethesda), 22: 373-379. PMID:18073410.