Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Molecular Dissection of the Interaction between hBLT2 and the G Protein Alpha Subunits

  • Vukoti, Krishna Moorthy (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Lee, Won-Kyu (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Kim, Ho-Jun (Department of Chemistry, Kookmin University) ;
  • Kim, Ick-Young (Division of Biotechnology and Genetic Engineering, College of Life and Environmental Sciences, Korea University) ;
  • Yang, Eun-Gyeong (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Lee, Cheol-Ju (Life Sciences Division, Korea Institute of Science and Technology) ;
  • Yu, Yeon-Gyu (Department of Chemistry, Kookmin University)
  • Published : 2007.06.20
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Abstract

Leukotriene B4 (LTB4) is a potent chemoattractant for leukocytes and considered to be an inflammatory mediator. Human BLT2 (hBLT2) is a low-affinity G-protein coupled receptor for LTB4 and mediates pertussis toxin-sensitive chemotactic cell movement. Here, we dissected the interaction between hBLT2 and G-protein alpha subunits using GST fusion proteins containing intracellular regions of hBLT2 and various Gα protein including Gα i1, Gα i2, Gα i3, Gα s1, Gα o1, and Gα z. Among the tested Gα subunits, Gα i3 showed the highest binding to the third intracellular loop region of hBLT2 with a dissociation constant (KD) of 5.0 × 10?6 M. These results suggest that Gα i3 has the highest affinity to hBLT2, and the third intracellular loop region of hBLT2 is the major component for the interaction with Gα i3.

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References

  1. Serhan, C. N.; Haeggstrom, J. Z.; Leslie, C. C. FASEB J. 1996, 10, 1147-1158 https://doi.org/10.1096/fasebj.10.10.8751717
  2. Ford-Hutchinson, A. W.; Bray, M. A.; Doig, M. V.; Shipley, M. E.; Smith, M. Nature 1990, 286, 264-265 https://doi.org/10.1038/286264a0
  3. Ng, C. F.; Sun, F. F.; Taylor, B. M.; Wolin, M. S.; Wong, P. Y. K. J. Immunol. 1991, 147, 3096-3103
  4. Huang, W. W.; Garcia-Zepeda, E. A.; Sauty, A.; Oettgen, H. C.; Rothenberg, M. E.; Luster, A. D. J. Exp. Med. 1998, 188, 1063- 1074 https://doi.org/10.1084/jem.188.6.1063
  5. Chen, X. S.; Sheller, J. R.; Johnson, E. N.; Funk, C. D. Nature 1994, 372, 179-182 https://doi.org/10.1038/372179a0
  6. Goulet, J. L.; Snouwaert, J. N.; Latour, A. M.; Coffman, T. M.; Koller, B. H. Proc. Natl. Acad. Sci. USA 1994, 91, 12852-12856 https://doi.org/10.1073/pnas.91.26.12852
  7. Griffiths, R. J.; Pettipher, E. R.; Koch, K.; Farrell, C. A.; Breslow, R.; Conklyn, M. J.; Smith, M. A.; Hackman, B. C.; Wimberly, D. J.; Milici, A. J.; Scampoli, D. N.; Cheng, J. B.; Pillar, J. S.; Pazoles, C. J.; Liston, T. E.; Showell, H. J. Proc. Natl. Acad. Sci. USA 1995, 92, 517-521 https://doi.org/10.1073/pnas.92.2.517
  8. Turner, C. R.; Breslow, R.; Conklyn, M. J.; Andresen, C. J.; Patterson, D. K.; Lopez-Anaya, A.; Owens, B.; Lee, P.; Watson, J. W.; Showell, H. J. J. Clin. Invest. 1996, 97, 381-387 https://doi.org/10.1172/JCI118426
  9. Sharon, P.; Stenson, M. F. Gastroenterology 1984, 86, 453-460
  10. Griffiths, R. J.; Smith, M. A.; Roach, M. L.; Stock, J. L.; Stam, E. J.; Milici, A. J.; Scampoli, D. N.; Eskra, J. D.; Byrum, R. S.; Koller, B. H.; McNeish, J. D. J. Exp. Med. 1997, 185, 1123- 1129 https://doi.org/10.1084/jem.185.6.1123
  11. Jackson, W. T.; Froelich, L. L.; Boyd, R. J.; Schrementi, J. P.; Saussy, D. L. Jr.; Schultz, R. M.; Sawyer, J. S.; Sofia, M. J.; Herron, D. K.; Goodson, T., Jr.; Snyder, D. W.; Pechous, P. A.; Spaethe, S. M.; Roman, C. R.; Fleisch, J. H. J. Pharmacol. Exp. Ther. 1999, 288, 286-294
  12. Showell, H. J.; Conklyn, M. J.; Alpert, R.; Hingorani, G. P.; Wright, K. F.; Smith, M. A.; Stam, E.; Salter, E. D.; Scampoli, D. N.; Meltzer, S.; Reiter, L. A.; Koch, K.; Piscopio, A. D.; Cortina, S. R.; Lopez-Anaya, A.; Pettipher, E. R.; Milici, A. J.; Griffiths, R. J. J. Pharmacol. Exp. Ther. 1998, 285, 946-954
  13. Kishikawa, K.; Tateishi, N.; Maruyama, T.; Seo, R.; Toda, M.; Miyamoto, T. Prostaglandins 1992, 442, 261-275
  14. Tager, A. M.; Luster, A. D. Prost. Leuko. Ess. Fatty Acids 2003, 69, 123-134 https://doi.org/10.1016/S0952-3278(03)00073-5
  15. Tryselius, Y.; Nilsson, N. E.; Kotarsky, K.; Olde, B.; Owman, C. Biochem. Biophys. Res. Comm. 2000, 274, 377-382 https://doi.org/10.1006/bbrc.2000.3152
  16. Yokomizo, T.; Kato, K.; Terawaki, K.; Izumi, T.; Shimizu, T. J. Exp. Med. 2000, 192, 421-431 https://doi.org/10.1084/jem.192.3.421
  17. Yokomizo, T.; Kato, K.; Hagiya, H.; Tizumi, T.; Shimizu, T. J. Biol. Chem. 2001, 276, 12454-12459 https://doi.org/10.1074/jbc.M011361200
  18. Yokomizo, T.; Izumi, T.; Chang, K.; Takuwa, Y.; Shimizu, T. Nature 1997, 387, 620-624 https://doi.org/10.1038/42506
  19. Yoo, M. H.; Song, H.; Woo, C. H.; Kim, H.; Kim, J. H. Oncogene 2004, 23, 9259-9268 https://doi.org/10.1038/sj.onc.1208151
  20. Tong, W. G.; Ding, X. A.; Henning, R.; Witt, R. C.; Standop, J.; Pour, P. M.; Adrian, T. E. Clic. Cancer Res. 2002, 8, 3232-3242
  21. Powell, W. S.; Macleod, R. J.; Gravel, S.; Gravelle, F.; Bhakar, A. J. Immunol. 1996, 156, 336-342
  22. Gaudreau, R.; Le Gouill, C.; Metaoui, S.; Lemire, S.; Stankova, J.; Rola-Pleszczynski, M. Biochem. J. 1998, 335, 15-18 https://doi.org/10.1042/bj3350015
  23. Kang, H.; Lee, W. K.; Choi, Y. H.; Vukoti, K. M.; Bang, W. G.; Yu, Y. G. Biochem. Biophys. Res. Comm. 2005, 329, 684-692 https://doi.org/10.1016/j.bbrc.2005.02.040
  24. Hamm, H. E.; Deretic, D.; Arendt, A.; Hargrave, P. A.; Koenig, B.; Hofmann, K. P. Science 1988, 241, 832-835 https://doi.org/10.1126/science.3136547
  25. Kisselev, O. G.; Kao, J.; Ponder, J. W.; Fann, Y. C.; Gautam, N.; Marshall, G. R. Proc. Natl. Acad. Sci. USA 1998, 95, 4270-4275 https://doi.org/10.1073/pnas.95.8.4270
  26. Itoh, Y.; Cai, K.; Khorana, H. G. Proc. Natl. Acad. Sci. USA 2001, 98, 4883-4887 https://doi.org/10.1073/pnas.051632998
  27. Savarese, T. M.; Fraserm, C. M. Biochem. J. 1992, 283, 1-19 https://doi.org/10.1042/bj2830001
  28. Garibay, J. L.; Kozasa, T.; Itoh, H.; Tsukamoto, T.; Matsuoka, M.; Kaziro, Y. Biochim. Biophys. Acta 1991, 1094, 192-199
  29. Kjelsberg, M. A.; Cotecchia, S.; Ostrowski, J.; Caron, M. G.; Lefkowitz, R. J. J. Biol. Chem. 1992, 267, 1430-1433
  30. Egan, C. T.; Herrick-Davis, K.; Teitler, M. J. Pharmacol. Exp. Ther. 1998, 286, 85-90
  31. Baneres, J. L.; Parello, J. J. Mol. Biol. 2003, 329, 815-829 https://doi.org/10.1016/S0022-2836(03)00439-X

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