Proteomic analysis of cellular response to osmotic stress in thick ascending limb of Henle's loop (TALH) cells

Molecular and Cellular Proteomics

Volumn 4, Issue 10, 2005, Pages 1445-1458

  Dihazi, Hassan ^a   Asif, Abdul R ^a   Agarwal, Nitin K ^a   Doncheva, Yuliana ^a   Müller, Gerhard A ^a  

^a UNIVERSITY OF GÖTTINGEN   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

ALDEHYDE REDUCTASE; ALPHA CRYSTALLIN; CALRETICULIN; CYTOKERATIN; CYTOSKELETON PROTEIN; ENOLASE; GLUCOSE REGULATED PROTEIN; GLUCOSE REGULATED PROTEIN 78; GLUTATHIONE TRANSFERASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; LACTATE DEHYDROGENASE; LIPOCORTIN 1; LIPOCORTIN 2; LIPOCORTIN 5; MALATE DEHYDROGENASE; PROTEIN DISULFIDE ISOMERASE; PROTEOME; SORBITOL; TRIOSEPHOSPHATE ISOMERASE; TROPOMYOSIN; TUBULIN; VIMENTIN;

AMINO ACID SEQUENCE; ANIMAL CELL; ARTICLE; CELL CULTURE; CELL LINE; DOWN REGULATION; ENDOPLASMIC RETICULUM; EPITHELIUM CELL; HENLE LOOP; KIDNEY CELL; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; OSMOTIC STRESS; OXIDATIVE STRESS; PHENOTYPE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN EXPRESSION; PROTEOMICS; TWO DIMENSIONAL GEL ELECTROPHORESIS; UPREGULATION; WESTERN BLOTTING;

ANIMALS; BLOTTING, WESTERN; CELL SHAPE; CELLS, CULTURED; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; EPITHELIAL CELLS; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION; HYDROGEN-ION CONCENTRATION; LOOP OF HENLE; OSMOTIC PRESSURE; PROTEOME; PROTEOMICS; RABBITS; SODIUM CHLORIDE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

ACACIA SEYAL; ANIMALIA;

EID: 27644495532     PISSN: 15359476     EISSN: None     Source Type: Journal    
DOI: 10.1074/mcp.M400184-MCP200     Document Type: Article

References (59)

1. Garcia-Perez, A., and Burg, M. R. (1991) Renal medullary organic osmolytes. Physiol. Rev. 71, 1081-1115
2. Yancey, P. H., Clark, M. E., Hand, S. C., Bowlus, R. D., and Somero, G. N. (1982) Living with water stress: evolution of osmolyte systems. Science 217, 1214-1222
3. Cohen, D. M., and Gullans, S. R. (1993) Urea selectively induces DNA synthesis in renal epithelial cells. Am. J. Physiol. 264, F601-F607
4. Grunewald, R. W., Fahr, M., Fiedler, G. M., Jehle, P. M., and Müller, G. A. (2001) Volume regulation of thick ascending limb of Henle cells: significance of organic osmolytes. Exp. Nephrol. 9, 81-89
5. Gullans, S. R., Blumenfeld, J. D., Balschi, J. A., Kaleta, M., Brenner, R. M., Heilig, C. W., and Herbert, S. C. (1988) Accumulation of major organic osmolytes in rat renal inner medulla in dehydration. Am. J. Physiol. 255, F626-F634
6. Bagnasco, S. M., Balaban, R., Fales, H. M., Yang, Y. M., and Burg, M. B. (1986) Predominant osmotically active organic solutes in rat and rabbit renal medullas. J. Biol. Chem. 261, 5872-5877
7. Ohta, M., Tanimoto, T., and Tanaka, A. (1991) Localization, isolation and properties of three NADPH-dependent aldehyde reducing enzymes from dog kidney. Biochim. Biophys. Acta 1078, 395-403
8. Petrash, J. M., and Srivastava, S. K. (1982) Purification and properties of human liver aldehyde reductases. Biochim. Biophys. Acta 707, 106-114
9. Srivastava, S. K., Ansari, N. H., Hair, G. A., and Das, B. (1984) Aldose and aldehyde reductases in human tissues. Biochim. Biophys. Acta 800, 220-227
10. Das, B., and Srivastava, S. K. (1985) Purification and properties of aldose reductase and aldehyde reductase II from human erythrocyte. Biochim. Biophys. Acta 238, 670-679
11. Grunewald, R. W., Wagner, M., Schubert, I., Franz, H. E., Müller, G. A., and Steffgen, J. (1998) Rat renal expression of mRNA coding for aldose reductase and sorbitol dehydrogenase and its osmotic regulation in inner medullary collecting duct cells. Cell. Physiol. Biochem. 8, 293-303
12. Beck, F. X., Burger-Kentischer, A., and Müller, E. (1998) Cellular response to osmotic stress in the renal medulla. Pluegers Arch.-Eur. J. Physiol. 436, 814-827
13. Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254
14. Neuhoff, V., Arold, N., Taube, D., and Ehrhardt, W. (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 9, 255-262
15. Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567
16. Towbin, H., Staehelin, T., and Gordon, J. (1979) Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76, 4350-4354
17. Yancey, P. H., and Burg, M. B. (1989) Distribution of major organic osmolytes in rabbit kidneys in diuresis and antidiuresis. Am. J. Physiol. 257, F602-F607
18. Bagnosco, S. M., Uchida, S., Balban, R. S., and Kador, P. F. (1987) Induction of aldose reductase and sorbitol in renal inner medullary cells by elevated extracellular NaCl. Proc. Natl. Acad Sci. U. S. A. 84, 1718-1720
19. Burg, M. B. (1995) Molecular basis of osmotic regulation. Am. J. Physiol. 268, F983-F996
20. Woo, S. K., Lee, S. D., Na, K. Y., Park, W. K., and Kwon, H. M. (2002) TonEBP/NFAT5 stimulates transcription of HSP70 in response to hypertonicity. Mol. Cell. Biol. 22, 5753-5760
21. Schüttert, J. B., Fiedler, G. M., Grupp, C., Blaschke, S., and Grunewald, R. W. (2002) Sorbitol transport in rat renal inner medullary interstitial cells. Kidney Int. 61, 1407-1415
22. Grunewald, R. W., Eckstein, A., Reisse, C. H., and Müller, G. A. (2001) Characterization of aldose reductase from the tick ascending limb of Henle's loop of rabbit kidney. Nephron 89, 73-81
23. Beck, F. X., Grünbein, R., Lugmayr, K., and Neuhofer, W. (2000) Heat shock proteins and the cellular response to osmotic stress. Cell. Physiol. Biochem. 10, 303-306
24. Bortner, C. D., and Cidlowski, J. A. (1996) Absence of volume regulatory mechanisms contributes to the rapid activation of apoptosis in thymocytes. Am. J. Physiol. 271, C950-C961
25. Grunewald, R. W., and Kinne, R. K. (1989) Intracellular sorbitol content in isolated rat inner medullary collecting duct cells. Pfluegers Arch. 414, 178-184
26. Bagnasco, S. M., Murphy, H. R., Bedford, J. J., and Burg, M. B. (1988) Osmoregulation by slow changes in aldose reductase and rapid changes in sorbitol flux. Am. J. Physiol. 254, C788-C792
27. Cowley, B. D., Ferraris, J. D., Jr., Carper, D., and Burg, M. (1990) In vivo osmoregulation of aldose reductase mRNA, protein, and sorbitol in renal medulla. Am. J. Physiol. 258, F154-F161
28. Smardo, F. L., Burg, M. B., Jr., and Carcia-Perez, A. (1992) Kidney aldose reductase gene transcription is osmotically regulated. Am. J. Physiol. 262, C776-C782
29. Garcia-Perez, A., Martin, B., Murphy, H. R., Uchida, S., Murer, H., Cowley, B. D., Jr., Handler, J. S., and Burg, M. B. (1989) Molecular cloning of cDNA coding for kidney aldose reductase: regulation of specific mRNA accumulation by NaCl-mediated osmotic stress. J. Biol. Chem. 264, 16815-16821
30. Uchida, S., Carcia-Perez, A., Murphy, H., and Burg, M. (1989) Signal for induction of aldose reductase in renal medullary cells by high external NaCl. Am. J. Physiol. 256, C614-C620
31. Tamarit, J., Cabiscol, E., and Ros, J. (1998) Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J. Biol. Chem. 273, 3027-3032
32. Cabiscol, E., Piulats, E., Echave, P., Herrero, E., and Ros, J. (2000) Oxidative stress promotes specific protein damage in Saccharomyces, cerevisiae. J. Biol. Chem. 275, 27393-27398
33. Castegna, A., Aksenov, M., Thongboonkerd, V., Klein, J. B., Pierce, W. M., Booze, R., Markesbery, W. R., and Butterfield, D. A. (2002) Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71. J. Neurochem. 82, 1524-1532
34. Paron, I., D'Elia, A., D'Ambrosio, C., Scaloni, A., D'Aurizio, F., Prescott, A., Damante, G., and Tell, G. (2004) A proteomic approach to identify early molecular targets of oxidative stress in human epithelial lens cells. Biochem. J. 378, 929-937
35. Kawamoto, R. M., and Caswell, A. H. (1986) Autophosphorylation of glyceraldehyde phosphate dehydrogenase and phosphorylation of protein from skeletal muscle microsomes. Biochemistry 25, 657-661
36. Durrieu, C., Bernier-Valentin, F., and Rousset, B. (1987) Microtubules bind glyceraldehyde-3-phosphate dehydrogenase and modulate its enzyme activity and quaternary structure. Arch. Biochem. Biophys. 252, 32-40
37. Glaser, P. E., and Gross, R. W. (1995) Rapid plasmenylethanolamine-selective fusion of membrane bilayers catalyzed by an isoform of glyceraldehyde-3-phosphate dehydrogenase: discrimination between glycolytic and fusogenic roles of individual isoforms. Biochemistry 34, 12193-121203
38. Brune, B., and Lapetina, E. G. (1996) Nitric oxide-induced covalent modification of glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. Methods Enzymol. 269, 400-407
39. +-binding region (Rossmann fold). J. Biol. Chem. 270, 2755-2763
40. Dastoor, Z., and Dreyer, J. L. (2001) Potential role of nuclear translocation of glyceraldehyde-3-phosphate dehydrogenase in apoptosis and oxidative stress. J. Cell Sci. 114, 1643-1653
41. Janssen, E., Terzic, A., Wieringa, B., and Dzeja, P. P. (2003) Impaired intracellular energetic communication in muscles from creatine kinase and adenylate kinase (M-CK/AK1) double knock-out mice. J. Biol. Chem. 278, 30441-30449
42. Mountain, I., Waelkens, E., Missiaen, L., and van Driessche, W. (1998) Changes in actin cytoskeleton during volume regulation in C6 glial cells. Eur. J. Cell Biol. 77, 196-204
43. Tilly, B. C., Edixhoven, M. J., Tertoolen, L. G., Morii, N., Saitoh, Y., Narumiya, S., and de Jonge, H. R. (1996) Activation of the osmo-sensitive chloride conductance involves P21rho and is accompanied by a transient reorganization of the F-actin cytoskeleton. Mol. Biol. Cell 7, 1419-1427
44. Chou, Y. H., and Goldman, R. D. (2000) Intermediate filament on the move. J. Cell Biol. 150, F101-F105
45. Fischer, R. S., Lee, A., and Fowler, V. M. (2000) Tropomodulin and tropomyosin mediate lens actin cytoskeleton reorganisation in vitro. Investig. Ophthalmol. Vis. Sci. 41, 166-174
46. Ellis, R. J., and Hemmingsen, S. M. (1989) Molecular chaperon: proteins essential for the biogenesis of some macromolecular structures. Trends Biochem. Sci. 14, 339-342
47. Beck, F. X., Neuhofer, W., and Müller, E. (2000) Molecular chaperones in the kidney: distribution, putative roles, and regulation. Am. J. Physiol. 279, F203-F215
48. Cohen, D. M., Wasserman, J. C., and Gullans, S. R. (1991) Immediate early gene and HSP70 expression in hyperosmotic stress in MDCK cells. Am. J. Physiol. 261, C594-C601
49. Head, M. W., Corbin, E., and Goldman, J. E. (1994) Coordinate and independent regulation of αB-crystallin and hsp27 expression in response to physiological stress. J. Cell. Physiol. 159, 41-50
50. Kegel, K. B., Iwaki, A., Iwaki, T., and Goldman, J. E. (1996) αB-Crystallin protects glial cells from hypertonic stress. Am. J. Physiol. 270, C903-C909
51. Borer, R. A., Lehner C. F., Eppenberger, H. M., and Nigg, E. A. (1989) Major nucleolar proteins shuttle between nucleus and cytoplasm. Cell 56, 379-390
52. Yang, C., Maiguel, D. A., and Carrier, F. (2002) Identification of nucleolin and nucleophosmin as genotoxic stress-responsive RNA-binding proteins. Nucleic Acids Res. 30, 2251-2260
53. Black, A. R., and Subjeck, J. R. (1991) The biology and physiology of the heat shock and glucose-regulated stress protein systems. Methods Achiev. Exp. Pathol. 15, 126-166
54. Lee, A. S. (1992) Mammalian stress response: induction of the glucose-regulated protein family. Curr. Opin. Cell Biol. 4, 267-273
55. Brostrom, M. A., Cade, C., Prostko, C. R., Gmitter-Yellen, D., and Brostrom, C. O. (1990) Accommodation of protein synthesis to chronic deprivation of intracellular sequestered calcium. A putative role for GRP78. J. Biol. Chem. 265, 20539-20546
56. Little, E., and Lee, A. S. (1995) Generation of a mammalian cell line deficient in glucose-regulated protein stress induction through targeted ribozyme driven by a stress-inducible promoter. J. Biol. Chem. 270, 9526-9534
57. Gomer, C. J., Ferrario, A., Rucker, N., Wong, S., and Lee, A. S. (1991) Glucose regulated protein induction and cellular resistance to oxidative stress mediated by porphyrin photosensitization. Cancer Res. 51, 6574-6579
58. Hughes, C. S., Shen, J. W., and Subjeck, J. R. (1989) Resistance to etoposide induced by three glucose-regulated stresses in Chinese hamster ovary cells. Cancer Res. 49, 4452-4454
59. Shen, J., Hughes, C., Chao, C., Cai, J., Bartels, C., Gessner, T., and Subjeck, J. (1987) Coinduction of glucose-regulated proteins and doxorubicin resistance in Chinese hamster cells. Proc. Natl. Acad. Sci. U. S. A. 84, 3278-3282