Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Preparation of 125

  • Kim, Byoung-Soo (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Kim, Eun-Jung (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Lee, Hae-June (Laboratory of Radiation Effects, Korea Institute of Radiological and Medical Sciences) ;
  • Han, Sang-Jin (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Choi, Tae-Hyun (Radiopharmaceuticals Research Team, Korea Institute of Radiological and Medical Sciences) ;
  • Lee, Yun-Sil (Laboratory of Radiation Effects, Korea Institute of Radiological and Medical Sciences) ;
  • Cheon, Gi-Jeong (Department of Nuclear Medicine, Korea Institute of Radiological and Medical Sciences)
  • Received : 2010.06.17
  • Accepted : 2010.07.26
  • Published : 2010.09.20
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Abstract

$PKC{\delta}$-catalytic V5 Heptapeptide (FEQFLDI, FP7) interacts with heat shock protein 27 (HSP27) and inhibits HSP27-mediated resistance to cell death against various stimuli including radiation therapy. Here, we prepared radio-iodinated heptapeptide and further investigated its uptake properties in HSP27 expression cells. Peptide sequence of FP7 and a negative control peptide (WSLLEKR, QP7) was modified by substituting their C-terminus residue to tyrosine (FP6Y and QP6Y) to label radio-iodine. Iodinated peptides were confirmed by LC mass analysis with cold iodine reaction mixture. Accumulation of [$^{125}I$]iodo-FP6Y and [$^{125}I$]iodo-QP6Y in NCI-H1299 cell line, with higher level of HSP27, and NCI-H460 cell line, with lower level of HSP27, was measured by NaI(Tl) scintillation counter. The modification of substituting C-terminus residue of FP7 to tyrosine (FP6Y) did not affect its interaction with HSP27. Accumulation of [$^{125}I$]iodo-FP6Y in NCI-H1299 cells was 3 fold higher than in NCI-H460 cells. The novel radio-iodinated FP6Y would be used as a tracer for targeting HSP27 protein.

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References

  1. Ritossa, F. Experimentia 1962, 18, 571-573. https://doi.org/10.1007/BF02172188
  2. Garrido, C.; Gurbuxani, S.; Ravagnan, L.; Kroemer, G. Biochem.Biophys. Res. Commun. 2001, 286, 433-442. https://doi.org/10.1006/bbrc.2001.5427
  3. Ciocca, D. R.; Oesterreich, S.; Chamness, G. C.; McGuire, W. L.;Fuqua, S. A. J. Natl. Cancer Inst. 1993, 85, 1558-1570. https://doi.org/10.1093/jnci/85.19.1558
  4. Jaattela, M. Int. J. Cancer 1995, 60, 689693.
  5. Garrido, C.; Fromentin, A.; Bonnotte, B.; Favre, N.; Moutet, M.;Arrigo, A. P. Cancer Res. 1998, 58, 5495-5499.
  6. Cornford, P. A.; Dodson, A. R.; Parsons, K. F.; Desmond, A. D.;Woolfenden, A.; Fordham, M. Cancer Res. 2000, 60, 7099-7105.
  7. van de Vijver, M. J.; He, Y. D.; van’t Veer, L. J.; Dai, H.; Hart, A.A.; Voskuil, D. W. N. Engl. J. Med. 2000, 34, 1999-2009.
  8. van’t Veer, L. J.; Dai, H.; van de Vijver, M. J.; He, Y. D.; Hart, A.A.; Mao, M. Nature 2002, 415, 530-536. https://doi.org/10.1038/415530a
  9. Garrido, C.; Brunet, M.; Didelot, C.; Zermati, Y.; Schmitt, E.; Kroemer,G. Cell Cycle 2006, 5, 2592-2601. https://doi.org/10.4161/cc.5.22.3448
  10. Didelot, C.; Schmitt, E.; Brunet, M.; Maingret, L.; Parcellier, A.;Garrido, C. Handb. Exp. Pharmacol. 2006, 172, 171-198. https://doi.org/10.1007/3-540-29717-0_8
  11. Bruey, J. M.; Ducasse, C.; Bonniaud, P.; Ravagnan, L.; Susin, S. A.;Diaz-Latoud, C. Nat. Cell Biol. 2000, 2, 645-652. https://doi.org/10.1038/35023595
  12. Watanabe, T.; Ono, Y.; Taniyama, Y.; Hazama, K.; Igarashi, K.;Ogita, K. Proc. Natl. Acad. Sci. USA 1992, 89, 10159-10163. https://doi.org/10.1073/pnas.89.21.10159
  13. Miyamoto, A.; Nakayama, K.; Imaki, H.; Hirose, S.; Jiang, Y.;Abe, M. Nature 2002, 416, 865-869. https://doi.org/10.1038/416865a
  14. Illera, V. A.; Perandones, C. E.; Stunz, L. L.; Mower, D. A.; Ashman,R. F. J. Immunol. 1993, 151, 2965-2973.
  15. Lucas, M.; Sanchez-Margalet, V. Gen. Pharmacol. 1995. 265,881-887.
  16. Lu, Z.; Hornia, A.; Jiang, Y. W.; Zang, Q.; Ohno, S.; Foster, D. A.Mol. Cell Bio. 1997, 17, 3418-3428
  17. Lee, Y. J.; Lee, D. H.; Cho, C. K.; Bae, S., Jhon, G. J.; Lee, S. J. J.Biol. Chem. 2005, 280, 18108-18119 https://doi.org/10.1074/jbc.M501131200
  18. Kim, E. H.; Lee, H. J.; Lee, D. H.; Bae, S.; Soh, J. W.; Jeoung, D.Cancer Res. 2007, 67, 6333-6341. https://doi.org/10.1158/0008-5472.CAN-06-4344
  19. Hunter, W. M.; Greenwood, F. C. Nature 1962, 194, 495-496. https://doi.org/10.1038/194495a0
  20. Salacinski, P. R. P.; McLean, C.; Sykes, J. E. C.; Clement-Jones,V. V.; Lowry, P. J. Anal. Biochem. 1981, 117, 136-146. https://doi.org/10.1016/0003-2697(81)90703-X
  21. Marchalonis, J. J. Biochem. J. 1969, 113, 299-305.
  22. Loot, A. E.; van Buiten, A.; Roks, A. J. M.; Henning, R. H. J.Pharmacol. Toxicol. Methods 2005, 51, 51-55. https://doi.org/10.1016/j.vascn.2004.07.005
  23. Blower, P. J.; Puncher, M. R.; Kettle, A. G.; George, S.; Dorsch,S.; Leak, A.; Naylor, L. H.; O’Doherty, M. J. Eur. J. Nucl. Med.1998, 25, 101-108. https://doi.org/10.1007/s002590050200
  24. Park, S. H.; Lee, S. J.; Chung, H. Y.; Kim, T. H.; Cho, C. K.; Yoo,S. Y. Radiat. Res. 2000, 153, 318-326. https://doi.org/10.1667/0033-7587(2000)153[0318:IHSPII]2.0.CO;2
  25. Tai, H. H. ; Korsch, B.; Chey, W. Y. Anal. Biochem. 1975, 69, 34-42. https://doi.org/10.1016/0003-2697(75)90562-X
  26. Tai, C. L.; Tai, H. H. Prostaglandins. Leukot. Med. 1984, 14, 243-254. https://doi.org/10.1016/0262-1746(84)90208-7
  27. Tai, H. H.; Yuan, B. Anal. Biochem. 1978, 87, 343- 349. https://doi.org/10.1016/0003-2697(78)90683-8
  28. Tashtoush, B. M.; Traboulsi, A. A.; Dittert, L.; Hussain, A. A. Anal.Biochem. 2001, 288, 16-21. https://doi.org/10.1006/abio.2000.4832
  29. Vergote, V.; Baert, B.; Vandermeulen, E.; Peremans, K.; van Bree,H.; Slegers, G.; Burvenich, C.; Spiegeleer, B. D. J. Pharm. Biomed.Anal. 2008, 46, 127-136. https://doi.org/10.1016/j.jpba.2007.10.005
  30. Inui, K. I.; Terada, T.; Masuda, S.; Saito, H. Nephrol. Dial. Transplant.2000, 15, 11-13.