Biochemistry (Moscow)

, Volume 68, Issue 7, pp 776–782 | Cite as

Role of Calcium Ions in Rapid Effects of L-Thyroxine on Phosphoinositide Metabolism in Rat Liver Cells

  • O. A. Krasilnikova
  • N. S. Kavok
  • N. A. Babenko


The role of calcium ions in the L-thyroxine-induced initiation of hydrolysis of phosphatidylinositol 4,5-bisphosphate (PtdInsP2) and also the course of releasing individual fractions of inositol phosphates and diacylglycerides (DAG) were studied in liver cells during early stages of the hormone effect. L-Thyroxine stimulated a rapid hydrolysis in hepatocytes of PtdInsP2 labeled with [14C]linoleic acid and [3H]inositol mediated by phosphoinositide-specific phospholipase C. This was associated with accumulation of [14C]DAG, total inositol phosphates, [3H]inositol 1,4,5-trisphosphate (Ins1,4,5P3) and [3H]inositol 1,4-bisphosphate (Ins1,4P2). Elimination of calcium ions from the incubation medium of hepatocytes did not abolish the effect of thyroxine on the accumulation of [14C]DAG and total [3H]inositol phosphates. Preincubation of liver cells with TMB-8 increased the stimulatory effect of L-thyroxine on the accumulation of [14C]DAG. During the incubation of hepatocytes in the presence of the hormone the content of 14C-labeled fatty acids did not change. The L-thyroxineinduced accumulation of [3H]Ins1,4,5P3 and [3H]Ins1,4P2 did not depend on the presence of calcium ions in the incubation medium of the cells.

thyroxine hepatocytes phospholipase C phosphatidylinositol 4,5-bisphosphate diacylglycerol inositol 1,4,5-trisphosphate calcium 


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  1. 1.
    Abdel-Latif, A. A. (1986) Pharmacol. Rev., 38, 227-272.Google Scholar
  2. 2.
    Lin, H. Y., Davis, F. B., Gordinier, J. K., Martino, L. J., and Davis, P. J. (1999) Am. J. Physiol., 276, 1014-1024.Google Scholar
  3. 3.
    Kavok, N. S., Krasilnikova, O. A., and Babenko, N. A. (2001) BMC Cell Biol., 2, 5.Google Scholar
  4. 4.
    Williams, S., Mesaeli, N., and Panagia, V. (1995) Ann. N. Y. Acad. Sci., 752, 187-191.Google Scholar
  5. 5.
    Hashizume, K., Yamauchi, K., Kobayashi, M., and Miyamoto, T. (1985) Endocrinol. Jpn, 32, 481-487.Google Scholar
  6. 6.
    Hummerich, H., and Soboll, S. (1989) Biochem. J., 258, 363-367.Google Scholar
  7. 7.
    Melin, P. M., Sundler, R., and Jergil, B. (1986) FEBS Lett., 198, 85-88.Google Scholar
  8. 8.
    Hofman, S. L., and Majerus, P. W. (1982) J. Biol. Chem., 275, 14359-14363.Google Scholar
  9. 9.
    Kanaeva, I. A., Karyagina, A. V., Alenicheva, T. V., Burmantova, G. A., Alimov, G. A., Archakov, A. I., and Zenkovich, G. D. (1975) Tsitologiya, 17, 545-551.Google Scholar
  10. 10.
    Bligh, E. G., and Dyer, W. J. (1959) Can. J. Biochem. Physiol., 37, 911-917.Google Scholar
  11. 11.
    Andrews, W. V., and Conn, P. M. (1987) Meth. Enzymol., 141, 156-168.Google Scholar
  12. 12.
    De Boland, A. R., Morelli, S., and Boland, R. (1994) J. Biol. Chem., 269, 8675-8679.Google Scholar
  13. 13.
    Jones, M. J., and Murray, A. W. (1995) J. Biol. Chem., 270, 5007-5013.Google Scholar
  14. 14.
    Rhee, S. G., and Bae, Y. S. (1997) J. Biol. Chem., 272, 15045-15048.Google Scholar
  15. 15.
    Bertagnolo, V., Mazzoni, M., Ricci, D., Carini, C., Neri, L. M., Previati, M., and Capitani, S. (1995) Cell Signal., 7, 669-678.Google Scholar
  16. 16.
    Grobler, J. A., and Hurley, J. H. (1998) Biochemistry, 37, 5020-5028.Google Scholar
  17. 17.
    Pawelczyk, T., and Matecki, A. (1998) Eur. J. Biochem., 257, 169-177.Google Scholar
  18. 18.
    Segal, J. (1990) Endocrinology, 126, 2693-2702.Google Scholar
  19. 19.
    Lin, H. Y., Shih, A., Davis, F. B., and Davis, P. J. (1999) Biochem. J., 338, 427-432.Google Scholar
  20. 20.
    Nunez, J. (1989) in Hormones and Their Actions (Cooke, B. A., King, R. J. B., and van der Molen, H. J., eds.) Elsevier Science Publishers, Amsterdam, pp. 61-80.Google Scholar
  21. 21.
    Berridge, M. J. (1986) Biol. Chem. Hoppe-Seyler, 367, 447-456.Google Scholar
  22. 22.
    Igwe, O. J., and Filla, M. B. (1995) Neuroscience, 69, 1239-1251.Google Scholar
  23. 23.
    Nishizuka, Ya. (1987) in Prospects in Biochemical Studies [Russian translation], Mir, Moscow, pp. 100-106.Google Scholar
  24. 24.
    Cobbold, P. H., Cuthbertson, K. S. R., and Woods, N. M. (1987) in Inositol Lipids Cell Signal, Banbury Meeting, 1987, Cold Spring Harbor, N. Y., pp. 119-124.Google Scholar
  25. 25.
    Kavok, N. S., Krasil'nikova, O. A., Sidorkina, O. M., and Babenko, N. A. (2000) Biochemistry (Moscow), 65, 1331-1336.Google Scholar
  26. 26.
    Besterman, J. M., Pollenz, R. S., Booker, E. L., Jr., and Cuatrecasas, P. (1986) Proc. Natl. Acad. Sci. USA, 83, 9378-9382.Google Scholar
  27. 27.
    Sakane, F., Yamada, K., Kanoh, H., Yokoyama, C., and Tanabe, T. (1990) Nature, 344, 345-348.Google Scholar
  28. 28.
    Bell, R. L., Kennerly, D. A., Stanford, N., and Majerus, P. W. (1979) Proc. Natl. Acad. Sci. USA, 76, 3238-3241.Google Scholar
  29. 29.
    Tsubokawa, H., Oguro, K., Robinson, H. P., Masuzawa, T., and Kawai, N. (1996) J. Physiol., 497, 67-78.Google Scholar
  30. 30.
    Laxminarayan, K. M., Chan, B. K., Tetaz, T., Bird, P. I., and Mitchell, C. A. (1994) J. Biol. Chem., 269, 17305-17310.Google Scholar
  31. 31.
    Pitcher, J. A., Freedman, N. J., and Lefkowitz, R. J. (1998) Ann. Rev. Biochem., 67, 653-692.Google Scholar
  32. 32.
    Auethavekiat, V., Abrams, C. S., and Majerus, P. W. (1997) J. Biol. Chem., 272, 1786-1790.Google Scholar
  33. 33.
    Krasil'nikova, O. A., and Babenko, N. A. (1996) Biochemistry (Moscow), 61, 1008-1014.Google Scholar

Copyright information

© MAIK “Nauka/Interperiodica” 2003

Authors and Affiliations

  • O. A. Krasilnikova
    • 1
  • N. S. Kavok
    • 1
  • N. A. Babenko
    • 1
  1. 1.Institute of BiologyKharkov National University, pl. Svobody 4KharkovUkraine

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