Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Interaction between IGFBP-5 and TNFR1

  • Kim, Eun-Jung (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Jeong, Mi-Suk (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Hwang, Jae-Ryoung (Molecular Therapy Research Center, Sungkyunkwan University) ;
  • Lee, Je-Ho (Molecular Therapy Research Center, Sungkyunkwan University) ;
  • Jang, Se-Bok (Department of Molecular Biology, College of Natural Sciences, Pusan National University)
  • Received : 2010.04.19
  • Accepted : 2010.05.31
  • Published : 2010.07.20
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Abstract

Insulin-like growth factor binding protein 5 (IGFBP-5) plays an important role in controlling cell survival, differentiation and apoptosis. Apoptosis can be induced by an extrinsic pathway involving the ligand-mediated activation of death receptors such as tumor necrosis factor receptor 1 (TNFR1). To determine whether IGFBP-5 and TNFR1 interact as members of the same apoptosis pathway, recombinant IGFBP-5 and TNFR1 were isolated. The expression and purification of the full-length TNFR1 and truncated IGFBP-5 proteins were successfully performed in E. coli. The binding of both IGFBP-5 and TNFR1 proteins was detected by surface plasmon resonance spectroscopy (BIAcore), fluorescence measurement, electron microscopy, and size-exclusion column (SEC) chromatography. IGFBP-5 indeed binds to TNFR1 with an apparent $K_D$ of 9 nM. After measuring the fluorescence emission spectra of purified IGFBP-5 and TNFR1, it was found that the tight interaction of these proteins is accompanied by significant conformational changes of one or both. These results indicate that IGFBP-5 acts potently as a novel ligand for TNFR1.

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References

  1. Stewart, C. E.; Rotwein, P. Physiol. Rev. 1996, 76, 1005-1026.
  2. Clemmons, D. R. Cytokine Growth Factor Rev. 1997, 8, 45-62. https://doi.org/10.1016/S1359-6101(96)00053-6
  3. Rajaram, S.; Baylink, D. J.; Mohan, S. Endocr. Rev. 1997, 18,801-831. https://doi.org/10.1210/er.18.6.801
  4. Conover, C. A. Prog. Growth Factor Res. 1995, 6, 301-309. https://doi.org/10.1016/0955-2235(95)00032-1
  5. Butt, A. J.; Dickson, K. A.; McDougall, F.; Baxter, R. C. J. Biol. Chem. 2003, 278, 29676-29685. https://doi.org/10.1074/jbc.M301965200
  6. Butt, A. J.; Firth, S. M.; King, M. A.; Baxter, R. C. J. Biol. Chem.2000, 275, 39174-39181. https://doi.org/10.1074/jbc.M908888199
  7. Butt, A. J.; Fraley, K. A.; Firth, S. M.; Baxter, R. C. Endocrinology2002, 143, 2693-2699. https://doi.org/10.1210/en.143.7.2693
  8. Gill, Z. P.; Perks, C. M.; Newcomb, P. V.; Holly, J. M. P. J. Biol. Chem. 1997, 272, 25602-25607. https://doi.org/10.1074/jbc.272.41.25602
  9. Rajah, R.; Valentinis, B.; Cohen, P. J. Biol. Chem. 1997, 272,12181-12188. https://doi.org/10.1074/jbc.272.18.12181
  10. Schedlich, L. J.; Le Page, S. L.; Firth, S.; Briggs, L. J.; Jans, D.A.; Baxter, R. C. J. Biol. Chem. 2000, 275, 23462-23470. https://doi.org/10.1074/jbc.M002208200
  11. Schedlich, L. J.; Young, T. Y.; Firth, S. M.; Baxter, R. C. J. Biol. Chem. 1998, 273, 18347-18352. https://doi.org/10.1074/jbc.273.29.18347
  12. McCaig, C.; Perks, C. M.; Holly, J. M. J. Cell Sci. 2002, 115,4293-4303. https://doi.org/10.1242/jcs.00097
  13. Andress, D. L. J. Biol. Chem. 1995, 270, 28289-28296.
  14. Andress, D. L. Am. J. Physiol. 1998, 274, E744-E750.
  15. Oh, Y.; Muller, H. L.; Pham, H.; Rosenfeld, R. G. J. Biol. Chem.1993, 268, 26045-26048.
  16. Aggarwal, B. B. Nat. Rev. Immunol. 2003, 3, 745-756. https://doi.org/10.1038/nri1184
  17. Feldmann, M.; Maini, R. N. Nat. Med. 2003, 9, 1245-1250. https://doi.org/10.1038/nm939
  18. Kooloos, W. M.; de Jong, D. J.; Huizinga, T. W.; Guchelaar, H.J. Drug Discov. 2007, 12, 125-131.
  19. Rutgeerts, P.; Assche, G. V.; Vermeire, S. Gastroenterology 2004,126, 1593-1610. https://doi.org/10.1053/j.gastro.2004.02.070
  20. Locksley, R. M.; Killeen N.; Lenardo, M. J. Cell 2001, 104, 487-501. https://doi.org/10.1016/S0092-8674(01)00237-9
  21. Tartaglia, L. A.; Ayres, T. M.; Wong, G. H. W.; Goeddel, D. V.Cell 1993, 74, 845-853. https://doi.org/10.1016/0092-8674(93)90464-2
  22. Boone, E.; Vansevoorde, V.; De Wilde, G.; Haegeman, G. FEBS Lett. 1998, 441, 275-280. https://doi.org/10.1016/S0014-5793(98)01567-1
  23. Hsu, H.; Xiong, J.; Goeddel, D. V. Cell 1995, 81, 495-504. https://doi.org/10.1016/0092-8674(95)90070-5
  24. Stanger, B. Z.; Leder, P.; Lee, T. H.; Kim, E.; Seed, B. Cell 1995,81, 513-523. https://doi.org/10.1016/0092-8674(95)90072-1
  25. Chinnaiyan, A. M.; O'Rourke, K.; Tewari, M.; Dixit, V. M. Cell1995, 81, 505-512. https://doi.org/10.1016/0092-8674(95)90071-3
  26. Qijin, X.; Ben, Y.; Shenghua, L.; Cunming, D. J. Biol. Chem. 2004,279, 4269-4277. https://doi.org/10.1074/jbc.M311586200
  27. Gharahdaghi, F.; Weinberg, C. R.; Meagher, D. A.; Imai, B. S.;Mische, S. M. Electrophoresis 1999, 20, 601-605. https://doi.org/10.1002/(SICI)1522-2683(19990301)20:3<601::AID-ELPS601>3.0.CO;2-6
  28. Spencer, E. M.; Chan, K. Prog. Growth Factor Res. 1995, 6, 209-214. https://doi.org/10.1016/0955-2235(96)00008-7
  29. Wajant, H.; Pfizenmaier, K.; Scheurich, P. Cell Death and Differentiation2003, 10, 45-65. https://doi.org/10.1038/sj.cdd.4401189
  30. Hong, J.; Jeong, M. S.; Kim, J. H.; Kim, B. G.; Holbrook, S. R.;Jang, S. B. Bull. Korean Chem. Soc. 2008, 29, 381-388. https://doi.org/10.5012/bkcs.2008.29.2.381
  31. Ha, J. H.; Jeong, M. S.; Jo, W.; Jeong, M.; Jang, S. B. Bull. Korean Chem. Soc. 2010, 2, 275-280.
  32. Ashkenazi, A.; Dixit, V. M. Science 1998, 281, 1305-1308. https://doi.org/10.1126/science.281.5381.1305
  33. Beg, A. A.; Baltimore, D. Science 1996, 274, 782-787. https://doi.org/10.1126/science.274.5288.782

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