Table of Contents
Journal of Signal Transduction
Volume 2011 (2011), Article ID 768512, 8 pages
http://dx.doi.org/10.1155/2011/768512
Review Article

Erk in Kidney Diseases

1Division of Nephrology, Department of Medicine, O'Brien Kidney Research Center, University of Texas Health Science Center, San Antonio, TX 78229, USA
2South Texas Veterans Health Care System, San Antonio, TX 78229, USA

Received 7 October 2010; Accepted 1 February 2011

Academic Editor: Peter P. Ruvolo

Copyright © 2011 Denis Feliers and Balakuntalam S. Kasinath. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. W. Lieberthal and J. S. Levine, “The role of the mammalian target of rapamycin (mTOR) in renal disease,” Journal of the American Society of Nephrology, vol. 20, no. 12, pp. 2493–2502, 2009. View at Publisher · View at Google Scholar · View at Scopus
  2. B. S. Kasinath, M. M. Mariappan, K. Sataranatarajan, M. J. Lee, G. Ghosh Choudhury, and D. Feliers, “Novel mechanisms of protein synthesis in diabetic nephropathy - Role of mRNA translation,” Reviews in Endocrine and Metabolic Disorders, vol. 9, no. 4, pp. 255–266, 2008. View at Publisher · View at Google Scholar · View at Scopus
  3. T. S. Lewis, P. S. Shapiro, and N. G. Ahn, “Signal transduction through MAP kinase cascades,” Advances in Cancer Research, vol. 74, pp. 137–139, 1998. View at Google Scholar · View at Scopus
  4. J. M. Kyriakis and J. Avruch, “Mammalian mitogen-activated protein kinase signal transduction pathways activated by stress and inflammation,” Physiological Reviews, vol. 81, no. 2, pp. 807–869, 2001. View at Google Scholar · View at Scopus
  5. M. M. Mariappan, D. Senthil, K. S. Natarajan, G. G. Choudhury, and B. S. Kasinath, “Phospholipase Cγ-Erk axis in vascular endothelial growth factor-induced eukaryotic initiation factor 4E phosphorylation and protein synthesis in renal epithelial cells,” The Journal of Biological Chemistry, vol. 280, no. 31, pp. 28402–28411, 2005. View at Publisher · View at Google Scholar · View at Scopus
  6. S. K. Nigam and W. Lieberthal, “Acute renal failure. III. The role of growth factors in the process of renal regeneration and repair,” American Journal of Physiology, vol. 279, no. 1, pp. F3–F11, 2000. View at Google Scholar · View at Scopus
  7. I. Sinuani, I. Beberashvili, Z. Averbukh, M. Cohn, I. Gitelman, and J. Weissgarten, “Mesangial cells initiate compensatory tubular cell hypertrophy,” American Journal of Nephrology, vol. 31, no. 4, pp. 326–331, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. S. M. Jones and A. Kazlauskas, “Growth-factor-dependent mitogenesis requires two distinct phases of signalling,” Nature Cell Biology, vol. 3, no. 2, pp. 165–172, 2001. View at Publisher · View at Google Scholar · View at Scopus
  9. S. I. Reed, “Control of the G/S transition,” Cancer Surveys, vol. 29, pp. 7–23, 1997. View at Google Scholar · View at Scopus
  10. W. A. Wells, “Does size matter?” Journal of Cell Biology, vol. 158, no. 7, pp. 1156–1159, 2002. View at Publisher · View at Google Scholar · View at Scopus
  11. B. A. Edgar and K. J. Kim, “Sizing up the cell,” Science, vol. 325, no. 5937, pp. 158–159, 2009. View at Publisher · View at Google Scholar · View at Scopus
  12. I. Sinuani, J. Weissgarten, I. Beberashvili et al., “The cyclin kinase inhibitor p57 regulates TGF-β-induced compensatory tubular hypertrophy:effect of the immunomodulator AS101,” Nephrology Dialysis Transplantation, vol. 24, no. 8, pp. 2328–2338, 2009. View at Publisher · View at Google Scholar · View at Scopus
  13. R. Conradie, F. J. Bruggeman, A. Ciliberto et al., “Restriction point control of the mammalian cell cycle via the cyclin E/Cdk2:p27 complex,” FEBS Journal, vol. 277, no. 2, pp. 357–367, 2010. View at Publisher · View at Google Scholar · View at Scopus
  14. M. Zhang, D. Fraser, and A. Phillips, “ERK, p38, and Smad signaling pathways differentially regulate transforming growth factor-β1 autoinduction in proximal tubular epithelial cells,” American Journal of Pathology, vol. 169, no. 4, pp. 1282–1293, 2006. View at Publisher · View at Google Scholar · View at Scopus
  15. J. F. di Mari, R. Davis, and R. L. Safirstein, “MAPK activation determines renal epithelial cell survival during oxidative injury,” American Journal of Physiology, vol. 277, no. 2, pp. F195–F203, 1999. View at Google Scholar · View at Scopus
  16. D. S. Kwon, C. H. Kwon, J. H. Kim, J. S. Woo, and J. S. Jung, “Signal transduction of MEK/ERK and PI3K/Akt activation by hypoxia/reoxygenation in renal epithelial cells,” European Journal of Cell Biology, vol. 85, no. 11, pp. 1189–1199, 2006. View at Publisher · View at Google Scholar · View at Scopus
  17. K. M. Park, A. Chen, and J. V. Bonventre, “Prevention of kidney ischemia/reperfusion-induced functional injury and JNK, p38, and MAPK kinase activation by remote ischemic pretreatment,” The Journal of Biological Chemistry, vol. 276, no. 15, pp. 11870–11876, 2001. View at Publisher · View at Google Scholar · View at Scopus
  18. C. W. Yang, H. J. Ahn, J. Y. Jung et al., “Preconditioning with cyclosporine A or FK506 differentially regulates mitogen-activated protein kinase expression in rat kidneys with ischemia/reperfusion injury,” Transplantation, vol. 75, no. 1, pp. 20–24, 2003. View at Publisher · View at Google Scholar · View at Scopus
  19. O. R. Kunduzova, P. Bianchi, N. Pizzinat et al., “Regulation of JNK/ERK activation, cell apoptosis, and tissue regeneration by monoamine oxidases after renal ischemia-reperfusion,” The FASEB Journal, vol. 16, no. 9, pp. 1129–1131, 2002. View at Google Scholar · View at Scopus
  20. M. Alderliesten, M. de Graauw, J. Oldenampsen et al., “Extracellular signal-regulated kinase activation during renal ischemia/reperfusion mediates focal adhesion dissolution and renal injury,” American Journal of Pathology, vol. 171, no. 2, pp. 452–462, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. V. Cepeda, M. A. Fuertes, J. Castilla, C. Alonso, C. Quevedo, and J. M. Pérez, “Biochemical mechanisms of cisplatin cytotoxicity,” Anti-Cancer Agents in Medicinal Chemistry, vol. 7, no. 1, pp. 3–18, 2007. View at Publisher · View at Google Scholar
  22. M. H. Hanigan and P. Devarajan, “Cisplatin nephrotoxicity: molecular mechanisms,” Cancer Therapeutics, vol. 1, pp. 47–61, 2003. View at Google Scholar
  23. N. Pabla and Z. Dong, “Cisplatin nephrotoxicity: mechanisms and renoprotective strategies,” Kidney International, vol. 73, no. 9, pp. 994–1007, 2008. View at Publisher · View at Google Scholar · View at Scopus
  24. I. Arany and R. L. Safirstein, “Cisplatin nephrotoxicity,” Seminars in Nephrology, vol. 23, no. 5, pp. 460–464, 2003. View at Publisher · View at Google Scholar · View at Scopus
  25. I. Arany, J. K. Megyesi, H. Kaneto, P. M. Price, and R. L. Safirstein, “Cisplatin-induced cell death is EGFR/src/ERK signaling dependent in mouse proximal tubule cells,” American Journal of Physiology, vol. 287, no. 3, pp. F543–F549, 2004. View at Publisher · View at Google Scholar · View at Scopus
  26. G. Nowak, “Protein kinase C-α and ERK1/2 mediate mitochondrial dysfunction, decreases in active Na+ transport, and cisplatin-induced apoptosis in renal cells,” The Journal of Biological Chemistry, vol. 277, no. 45, pp. 43377–43388, 2002. View at Publisher · View at Google Scholar · View at Scopus
  27. S. K. Jo, W. Y. Cho, S. A. Sung, H. K. Kim, and N. H. Won, “MEK inhibitor, U0126, attenuates cisplatin-induced renal injury by decreasing inflammation and apoptosis,” Kidney International, vol. 67, no. 2, pp. 458–466, 2005. View at Publisher · View at Google Scholar · View at Scopus
  28. P. D. Wilson, “Polycystic kidney disease,” The New England Journal of Medicine, vol. 350, no. 2, pp. 151–164, 2004. View at Publisher · View at Google Scholar · View at Scopus
  29. V. E. Torres and P. C. Harris, “Autosomal dominant polycystic kidney disease: the last 3 years,” Kidney International, vol. 76, no. 2, pp. 149–168, 2009. View at Publisher · View at Google Scholar
  30. J. J. Grantham, V. E. Torres, A. B. Chapman et al., “Volume progression in polycystic kidney disease,” The New England Journal of Medicine, vol. 354, no. 20, pp. 2122–2130, 2006. View at Publisher · View at Google Scholar · View at Scopus
  31. G. Aguiari, V. Trimi, M. Bogo et al., “Novel role for polycystin-1 in modulating cell proliferation through calcium oscillations in kidney cells,” Cell Proliferation, vol. 41, no. 3, pp. 554–573, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. C. L. Edelstein, “Mammalian target of rapamycin and caspase inhibitors in polycystic kidney disease,” Clinical Journal of the American Society of Nephrology, vol. 3, no. 4, pp. 1219–1226, 2008. View at Publisher · View at Google Scholar
  33. S. Omori, M. Hida, H. Fujita et al., “Extracellular signal-regulated kinase inhibition slows disease progression in mice with polycystic kidney disease,” Journal of the American Society of Nephrology, vol. 17, no. 6, pp. 1604–1614, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. G. Walz, K. Budde, M. Mannaa et al., “Everolimus in patients with autosomal dominant polycystic kidney disease,” The New England Journal of Medicine, vol. 363, no. 9, pp. 830–840, 2010. View at Publisher · View at Google Scholar
  35. A. L. Serra, D. Poster, A. D. Kistler et al., “Sirolimus and kidney growth in autosomal dominant polycystic kidney disease,” The New England Journal of Medicine, vol. 363, no. 9, pp. 820–829, 2010. View at Publisher · View at Google Scholar
  36. W. M. Bagchus, M. F. Jeunink, and J. D. Elema, “The mesangium in anti-Thy-1 nephritis. Influx of macrophages, mesangial cell hypercellularity, and macromolecular accumulation,” American Journal of Pathology, vol. 137, no. 1, pp. 215–223, 1990. View at Google Scholar · View at Scopus
  37. D. Bokemeyer, T. Ostendorf, U. Kunter, M. Lindemann, H. J. Kramer, and J. Floege, “Differential activation of mitogen-activated protein kinases in experimental mesangioproliferative glomerulonephritis,” Journal of the American Society of Nephrology, vol. 11, no. 2, pp. 232–240, 2000. View at Google Scholar · View at Scopus
  38. D. Bokemeyer, D. Panek, H. J. Kramer et al., “In vivo identification of the mitogen-activated protein kinase cascade as a central pathogenic pathway in experimental mesangioproliferative glomerulonephritis,” Journal of the American Society of Nephrology, vol. 13, no. 6, pp. 1473–1480, 2002. View at Publisher · View at Google Scholar · View at Scopus
  39. A. A. Reszka, R. Seger, C. D. Diltz, E. G. Krebs, and E. H. Fischer, “Association of mitogen-activated protein kinase with the microtubule cytoskeleton,” Proceedings of the National Academy of Sciences of the United States of America, vol. 92, no. 19, pp. 8881–8885, 1995. View at Publisher · View at Google Scholar · View at Scopus
  40. S. Torii, K. Nakayama, T. Yamamoto, and E. Nishida, “Regulatory mechanisms and function of ERK MAP kinases,” Journal of Biochemistry, vol. 136, no. 5, pp. 557–561, 2004. View at Publisher · View at Google Scholar · View at Scopus
  41. E. Formstecher, J. W. Ramos, M. Fauquet et al., “PEA-15 Mediates Cytoplasmic Sequestration of ERK MAP Kinase,” Developmental Cell, vol. 1, no. 2, pp. 239–250, 2001. View at Publisher · View at Google Scholar · View at Scopus
  42. C. Kahan, K. Seuwen, S. Meloche, and J. Pouyssegur, “Coordinate, biphasic activation of p44 mitogen-activated protein kinase and S6 kinase by growth factors in hamster fibroblasts. Evidence for thrombin-induced signals different from phosphoinositide turnover and adenylylcyclase inhibition,” The Journal of Biological Chemistry, vol. 267, no. 19, pp. 13369–13375, 1992. View at Google Scholar · View at Scopus
  43. S. Meloche, K. Seuwen, G. Pages, and J. Pouyssegur, “Biphasic and synergistic activation of p44(mapk) (ERK1) by growth factors: correlation between late phase activation and mitogenicity,” Molecular Endocrinology, vol. 6, no. 5, pp. 845–854, 1992. View at Publisher · View at Google Scholar · View at Scopus
  44. S. Meloche, “Cell cycle reentry of mammalian fibroblasts is accompanied by the sustained activation of p44(mapk) and p42(mapk) isoforms in the G1 phase and their inactivation at the G1/S transition,” Journal of Cellular Physiology, vol. 163, no. 3, pp. 577–588, 1995. View at Publisher · View at Google Scholar · View at Scopus
  45. R. J. Davis, “Transcriptional regulation by MAP kinases,” Molecular Reproduction and Development, vol. 42, no. 4, pp. 459–467, 1995. View at Publisher · View at Google Scholar · View at Scopus
  46. J. W. Pippin, R. Durvasula, A. Petermann, K. Hiromura, W. G. Couser, and S. J. Shankland, “DNA damage is a novel response to sublytic complement C5b-9-induced injury in podocytes,” Journal of Clinical Investigation, vol. 111, no. 6, pp. 877–885, 2003. View at Publisher · View at Google Scholar · View at Scopus
  47. A. V. Cybulsky, T. Takano, J. Papillon, K. Bijian, and J. Guillemette, “Activation of the extracellular signal-regulated kinase by complement C5b-9,” American Journal of Physiology, vol. 289, no. 3, pp. F593–F603, 2005. View at Publisher · View at Google Scholar · View at Scopus
  48. T. Masaki, R. Foti, P. A. Hill, Y. Ikezumi, R. C. Atkins, and D. J. Nikolic-Paterson, “Activation of the ERK pathway precedes tubular proliferation in the obstructed rat kidney,” Kidney International, vol. 63, no. 4, pp. 1256–1264, 2003. View at Publisher · View at Google Scholar · View at Scopus
  49. B. Pat, T. Yang, C. Kong, D. Watters, D. W. Johnson, and G. Gobe, “Activation of ERK in renal fibrosis after unilateral ureteral obstruction: modulation by antioxidants,” Kidney International, vol. 67, no. 3, pp. 931–943, 2005. View at Publisher · View at Google Scholar · View at Scopus
  50. Y. Han, T. Masaki, L. A. Hurst et al., “Extracellular signal-regulated kinase-dependent interstitial macrophage proliferation in the obstructed mouse kidney,” Nephrology, vol. 13, no. 5, pp. 411–418, 2008. View at Publisher · View at Google Scholar · View at Scopus
  51. R. O. Estacio and R. W. Schrier, “Diabetic nephropathy: pathogenesis, diagnosis, and prevention of progression,” Advances in Internal Medicine, vol. 46, pp. 359–408, 2001. View at Google Scholar · View at Scopus
  52. M. E. Molitch, R. A. DeFronzo, M. J. Franz et al., “Nephropathy in diabetes,” Diabetes Care, vol. 27, supplement 1, pp. S79–S83, 2004. View at Google Scholar
  53. T. H. Hostetter, “Progression of renal disease and renal hypertrophy,” Annual Review of Physiology, vol. 57, pp. 263–278, 1995. View at Google Scholar · View at Scopus
  54. T. H. Hostetter, “Hyperfiltration and glomerulosclerosis,” Seminars in Nephrology, vol. 23, no. 2, pp. 194–199, 2003. View at Publisher · View at Google Scholar · View at Scopus
  55. M. K. Holz, B. A. Ballif, S. P. Gygi, and J. Blenis, “mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events,” Cell, vol. 123, no. 4, pp. 569–580, 2005. View at Publisher · View at Google Scholar · View at Scopus
  56. B. S. Kasinath, D. Feliers, K. Sataranatarajan, G. G. Choudhury, M. J. Lee, and M. M. Mariappan, “Regulation of mRNA translation in renal physiology and disease,” American Journal of Physiology, vol. 297, no. 5, pp. F1153–F1165, 2009. View at Publisher · View at Google Scholar · View at Scopus
  57. B. S. Kasinath, M. M. Mariappan, K. Sataranatarajan, M. J. Lee, and D. Feliers, “mRNA translation: unexplored territory in renal science,” Journal of the American Society of Nephrology, vol. 17, no. 12, pp. 3281–3292, 2006. View at Publisher · View at Google Scholar · View at Scopus
  58. N. Sonenberg and A. G. Hinnebusch, “Regulation of translation initiation in eukaryotes: mechanisms and biological targets,” Cell, vol. 136, no. 4, pp. 731–745, 2009. View at Publisher · View at Google Scholar · View at Scopus
  59. J. R. Lorsch and T. E. Dever, “Molecular view of 43 S complex formation and start site selection in eukaryotic translation initiation,” The Journal of Biological Chemistry, vol. 285, no. 28, pp. 21203–21207, 2010. View at Publisher · View at Google Scholar · View at Scopus
  60. A. Pause, G. J. Belsham, A. C. Gingras et al., “Insulin-dependent stimulation of protein synthesis by phosphorylation of a regulator of 5-cap function,” Nature, vol. 371, no. 6500, pp. 762–767, 1994. View at Publisher · View at Google Scholar · View at Scopus
  61. A. J. Waskiewicz, A. Flynn, C. G. Proud, and J. A. Cooper, “Mitogen-activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2,” EMBO Journal, vol. 16, no. 8, pp. 1909–1920, 1997. View at Publisher · View at Google Scholar · View at Scopus
  62. A. J. Waskiewicz, J. C. Johnson, B. Penn, M. Mahalingam, S. R. Kimball, and J. A. Cooper, “Phosphorylation of the cap-binding protein eukaryotic translation initiation factor 4E by protein kinase Mnk1 in vivo,” Molecular and Cellular Biology, vol. 19, no. 3, pp. 1871–1880, 1999. View at Google Scholar · View at Scopus
  63. X. Wang, A. Flynn, A. J. Waskiewicz et al., “The phosphorylation of eukaryotic initiation factor eIF4E in response to phorbol esters, cell stresses, and cytokines is mediated by distinct MAP kinase pathways,” The Journal of Biological Chemistry, vol. 273, no. 16, pp. 9373–9377, 1998. View at Publisher · View at Google Scholar · View at Scopus
  64. D. Feliers, S. Duraisamy, J. L. Barnes, G. Ghosh-Choudhury, and B. S. Kasinath, “Translational regulation of vascular endothelial growth factor expression in renal epithelial cells by angiotensin II,” American Journal of Physiology, vol. 288, no. 3, pp. F521–F529, 2005. View at Publisher · View at Google Scholar · View at Scopus
  65. A. Kuhn and I. Grummt, “Dual role of the nucleolar transcription factor UBF: trans-activator and antirepressor,” Proceedings of the National Academy of Sciences of the United States of America, vol. 89, no. 16, pp. 7340–7344, 1992. View at Google Scholar
  66. A. Kuhn, V. Stefanovsky, and I. Grummt, “The nucleolar transcription activator UBF relieves Ku antigen-mediated repression of mouse ribosomal gene transcription,” Nucleic Acids Research, vol. 21, no. 9, pp. 2057–2063, 1993. View at Google Scholar · View at Scopus
  67. D. Drygin, W. G. Rice, and I. Grummt, “The RNA polymerase i transcription machinery: an emerging target for the treatment of cancer,” Annual Review of Pharmacology and Toxicology, vol. 50, pp. 131–156, 2010. View at Publisher · View at Google Scholar · View at Scopus
  68. V. Y. Stefanovsky, F. Langlois, D. Bazett-Jones, G. Pelletier, and T. Moss, “ERK modulates DNA bending and enhancesome structure by phosphorylating HMG1-boxes 1 and 2 of the RNA polymerase I transcription factor UBF,” Biochemistry, vol. 45, no. 11, pp. 3626–3634, 2006. View at Publisher · View at Google Scholar · View at Scopus
  69. V. Y. Stefanovsky, G. Pelletier, R. Hannan, T. Gagnon-Kugler, L. I. Rothblum, and T. Moss, “An immediate response of ribosomal transcription to growth factor stimulation in mammals is mediated by ERK phosphorylation of UBF,” Molecular Cell, vol. 8, no. 5, pp. 1063–1073, 2001. View at Publisher · View at Google Scholar · View at Scopus
  70. R. Voit and I. Grummt, “Phosphorylation of UBF at serine 388 is required for interaction with RNA polymerase I and activation of rDNA transcription,” Proceedings of the National Academy of Sciences of the United States of America, vol. 98, no. 24, pp. 13631–13636, 2001. View at Publisher · View at Google Scholar · View at Scopus
  71. R. Voit, M. Hoffmann, and I. Grummt, “Phosphorylation by G-specific cdk-cyclin complexes activates the nucleolar transcription factor UBF,” EMBO Journal, vol. 18, no. 7, pp. 1891–1899, 1999. View at Google Scholar · View at Scopus
  72. M. M. Mariappan, K. D'Silva, M. J. Lee et al., “Ribosomal biogenesis induction by high glucose requires activation of upstream binding factor in kidney glomerular epithelial cells,” American Journal of Physiology, vol. 300, no. 1, pp. F219–F230, 2011. View at Publisher · View at Google Scholar
  73. H. Lempiäinen and D. Shore, “Growth control and ribosome biogenesis,” Current Opinion in Cell Biology, vol. 21, no. 6, pp. 855–863, 2009. View at Publisher · View at Google Scholar · View at Scopus
  74. I. Ruvinsky, N. Sharon, T. Lerer et al., “Ribosomal protein S6 phosphorylation is a determinant of cell size and glucose homeostasis,” Genes and Development, vol. 19, no. 18, pp. 2199–2211, 2005. View at Publisher · View at Google Scholar · View at Scopus
  75. S. Ferrari, H. R. Bandi, J. Hofsteenge, B. M. Bussian, and G. Thomas, “Mitogen-activated 70K S6 kinase. Identification of in vitro 40 S ribosomal S6 phosphorylation sites,” The Journal of Biological Chemistry, vol. 266, no. 33, pp. 22770–22775, 1991. View at Google Scholar · View at Scopus
  76. M. Pende, S. H. Um, V. Mieulet et al., “S6K1/S6K2 mice exhibit perinatal lethality and rapamycin-sensitive 5-terminal oligopyrimidine mRNA translation and reveal a mitogen-activated protein kinase-dependent S6 kinase pathway,” Molecular and Cellular Biology, vol. 24, no. 8, pp. 3112–3124, 2004. View at Publisher · View at Google Scholar · View at Scopus
  77. R. J. Salmond, J. Emery, K. Okkenhaug, and R. Zamoyska, “MAPK, phosphatidylinositol 3-kinase, and mammalian target of rapamycin pathways converge at the level of ribosomal protein S6 phosphorylation to control metabolic signaling in CD8 T cells,” Journal of Immunology, vol. 183, no. 11, pp. 7388–7397, 2009. View at Publisher · View at Google Scholar · View at Scopus
  78. U. A. Bommer, G. Lutsch, J. Stahl, and H. Bielka, “Eukaryotic initiation factors eIF-2 and eIF-3: interactions, structure and localization in ribosomal initiation complexes,” Biochimie, vol. 73, no. 7-8, pp. 1007–1019, 1991. View at Google Scholar · View at Scopus
  79. J. Kim, L. S. Chubatsu, A. Admon, J. Stahl, R. Fellous, and S. Linn, “Implication of mammalian ribosomal protein S3 in the processing of DNA damage,” The Journal of Biological Chemistry, vol. 270, no. 23, pp. 13620–13629, 1995. View at Publisher · View at Google Scholar · View at Scopus
  80. S. Yadavilli, V. Hegde, and W. A. Deutsch, “Translocation of human ribosomal protein S3 to sites of DNA damage is dependant on ERK-mediated phosphorylation following genotoxic stress,” DNA Repair, vol. 6, no. 10, pp. 1453–1462, 2007. View at Publisher · View at Google Scholar
  81. D. Feliers, S. Duraisamy, J. L. Faulkner et al., “Activation of renal signaling pathways in db/db mice with type 2 diabetes,” Kidney International, vol. 60, no. 2, pp. 495–504, 2001. View at Publisher · View at Google Scholar · View at Scopus
  82. R. M. Mason and N. A. Wahab, “Extracellular matrix metabolism in diabetic nephropathy,” Journal of the American Society of Nephrology, vol. 14, no. 5, pp. 1358–1373, 2003. View at Publisher · View at Google Scholar
  83. M. M. Mariappan, D. Feliers, S. Mummidi, G. G. Choudhury, and B. S. Kasinath, “High glucose, high insulin, and their combination rapidly induce laminin-β1 synthesis by regulation of mRNA translation in renal epithelial cells,” Diabetes, vol. 56, no. 2, pp. 476–485, 2007. View at Publisher · View at Google Scholar · View at Scopus
  84. B. K. Bhandari, D. Feliers, S. Duraisamy et al., “Insulin regulation of protein translation repressor 4E-BP1, an eIF4E-binding protein, in renal epithelial cells,” Kidney International, vol. 59, no. 3, pp. 866–875, 2001. View at Publisher · View at Google Scholar · View at Scopus