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Biochemistry (Moscow)

, Volume 81, Issue 3, pp 255–262 | Cite as

Tankyrase activity in organs and tissues of mice

  • A. N. KuimovEmail author
  • A. S. Zhozhikashvili
  • V. N. Manskikh
  • L. V. Platonova
  • T. G. Dyuzheva
Article
  • 86 Downloads

Abstract

Tankyrase, one of the NAD+ ADP-ribosyltransferases, is a target for drugs developed for their anticancer and other pharmacological activities. We designed an assay for estimation of the inhibition or activation of the enzyme in pre-clinical studies. In mice, the highest specific activity of tankyrase was observed in thymus, spleen, pancreas, and bone marrow. In murine liver, tankyrase is active in ontogenesis and during reparative regeneration; however, the basal activity is hardly detectable in normal liver and most of other organs of adult animals. We suggest that tankyrase is a part of the tissue growth and repair machinery, while its age-dependent inhibition, when an organism stops growing, turns on phenoptosis.

Key words

ADP-ribosyltransferase Essentiale N hepatic stimulator substance poly(ADP-ribosyl)ation regeneration 

Abbreviations

HSS

hepatic stimulator substance

PARP

poly(ADP-ribose) polymerase

TAA

thioacetamide

XAV939

tankyrase inhibitor

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References

  1. 1.
    Vyas, S., Matic, I., Uchima, L., Rood, J., Zaja, R., Hay, R. T., Ahel, I., and Chang, P. (2014) Family-wide analysis of poly(ADP-ribose) polymerase activity, Nat. Commun., 5, 4426.CrossRefPubMedPubMedCentralGoogle Scholar
  2. 2.
    Chiang, Y. J., Hsiao, S. J., Yver, D., Cushman, S. W., Tessarollo, L., Smith, S., and Hodes, R. J. (2008) Tankyrase 1 and tankyrase 2 are essential but redundant for mouse embryonic development, PLoS One, 3, e2639.CrossRefPubMedPubMedCentralGoogle Scholar
  3. 3.
    Chi, N. W., and Lodish, H. F. (2000) Tankyrase is a Golgi-associated mitogen-activated protein kinase substrate that interacts with IRAP in GLUT4 vesicles, J. Biol. Chem., 275, 38437–38444.CrossRefPubMedGoogle Scholar
  4. 4.
    Smith, S., Giriat, I., Schmitt, A., and De Lange, T. (1998) Tankyrase, a poly(ADP-ribose) polymerase at human telomeres, Science, 282, 1484–1487.CrossRefPubMedGoogle Scholar
  5. 5.
    Monz, D., Munnia, A., Comtesse, N., Fischer, U., Steudel, W. I., Feiden, W., Glass, B., and Meese, E. U. (2001) Novel tankyrase-related gene detected with meningioma-specific sera, Clin. Cancer Res., 7, 113–119.PubMedGoogle Scholar
  6. 6.
    Kuimov, A. N., Kuprash, D. V., Petrov, V. N., Vdovichenko, K. K., Scanlan, M. J., Jongeneel, C. V., Lagarkova, M. A., and Nedospasov, S. A. (2001) Cloning and characterization of TNKL, a member of tankyrase gene family, Genes Immun., 2, 52–55.CrossRefPubMedGoogle Scholar
  7. 7.
    Cook, B. D., Dynek, J. N., Chang, W., Shostak, G., and Smith, S. (2002) Role for the related poly(ADP-ribose) polymerases tankyrase 1 and 2 at human telomeres, Mol. Cell. Biol., 22, 332–342.CrossRefPubMedPubMedCentralGoogle Scholar
  8. 8.
    Huang, S. M., Mishina, Y. M., Liu, S., Cheung, A., Stegmeier, F., Michaud, G. A., Charlat, O., Wiellette, E., Zhang, Y., Wiessner, S., Hild, M., Shi, X., Wilson, C. J., Mickanin, C., Myer, V., Fazal, A., Tomlinson, R., Serluca, F., Shao, W., Cheng, H., Shultz, M., Rau, C., Schirle, M., Schlegl, J., Ghidelli, S., Fawell, S., Lu, C., Curtis, D., Kirschner, M. W., Lengauer, C., Finan, P. M., Tallarico, J. A., Bouwmeester, T., Porter, J. A., Bauer, A., and Cong, F. (2009) Tankyrase inhibition stabilizes axin and antagonizes Wnt signaling, Nature, 46, 614–620.CrossRefGoogle Scholar
  9. 9.
    Chen, B., Dodge, M. E., Tang, W., Lu, J., Ma, Z., Fan, C.-W., Wei, S., Hao, W., Kilgore, J., Williams, N. S., Roth, M. G., Amatruda, J. F., Chen, C., and Lum, L. (2009) Small molecule-mediated disruption of Wnt dependent signaling in tissue regeneration and cancer, Nat. Chem. Biol., 5, 100–107.CrossRefPubMedPubMedCentralGoogle Scholar
  10. 10.
    Lu, J., Ma, Z., Hsieh, J.-C., Fan, C.-W., Chen, B., Longgood, J. C., Williams, N. S., Amatruda, J. F., Lum, L., and Chen, C. (2009) Structure–activity relationship studies of small-molecule inhibitors of Wnt response, Bioorg. Med. Chem. Lett., 19, 3825–3827.CrossRefPubMedPubMedCentralGoogle Scholar
  11. 11.
    Kuimov, A. N., and Terekhov, S. M. (2003) Soluble tankyrase located in cytosol of human embryonic kidney cell line 293, Biochemistry (Moscow), 68, 260–268.CrossRefGoogle Scholar
  12. 12.
    Sidorova, N., Zavalishina, L., Kurchashova, S., Korsakova, N., Nazhimov, V., Frank, G., and Kuimov, A. (2006) Immunohistochemical detection of tankyrase 2 in human breast tumors and normal renal tissue, Cell Tissue Res., 323, 137–145.CrossRefPubMedGoogle Scholar
  13. 13.
    Gal’perin, E. I., Djuzheva, T. G., Abakumova, O. Ju., and Platonova, L. V. (2015) Method for Producing Substance Stimulating Injured Liver Repair, Patent RF No. 2548750, Byull. No. 11.Google Scholar
  14. 14.
    Smith, S., and De Lange, T. (1999) Cell cycle dependent localization of the telomeric PARP, tankyrase, to nuclear pore complexes and centrosomes, J. Cell. Sci., 112, 3649–3656.PubMedGoogle Scholar
  15. 15.
    Lau, T., Chan, E., Callow, M., Waaler, J., Boggs, J., Blake, R. A., Magnuson, S., Sambrone, A., Schutten, M., Firestein, R., Machon, O., Korinek, V., Choo, E., Diaz, D., Merchant, M., Polakis, P., Holsworth, D. D., Krauss, S., and Costa, M. (2013) A novel tankyrase small-molecule inhibitor suppresses APC mutation-driven colorectal tumor growth, Cancer Res., 73, 3132–3144.CrossRefPubMedGoogle Scholar
  16. 16.
    Gatzidou, E., Kouraklis, G., and Theocharis, S. (2006) Insights on augmenter of liver regeneration cloning and function, World J. Gastroenterol., 12, 4951–4958.CrossRefPubMedPubMedCentralGoogle Scholar
  17. 17.
    Hagiya, M., Francavilla, A., Polimeno, L., Ihara, L. I., Sakai, H., Seki, T., Shimonishi, M., Porter, K. A., and Starzl, T. E. (1994) Cloning and sequence analysis of the rat augmenter of liver regeneration (ALR) gene: expression of biologically active recombinant ALR and demonstration of tissue distribution, Proc. Natl. Acad. Sci. USA, 91, 8142–8146.CrossRefPubMedPubMedCentralGoogle Scholar
  18. 18.
    Li, Y., Li, M., Xing, G. C., Hu, Z., Wang, Q., Dong, C., Wei, H., Fan, G., Chen, J., Yang, X., Zhao, S., Chen, H., Guan, K., Wu, C., Zhang, C., and He, F. (2000) Stimulation of the mitogen-activated protein kinase cascade and tyrosine phosphorylation of the epidermal growth factor receptor by hepatopoietin, J. Biol. Chem., 275, 37443–37447.CrossRefPubMedGoogle Scholar
  19. 19.
    Ponsot, E., Echaniz-Laguna, A., Delis, A.-M., and Kadi, F. (2012) Telomere length and regulatory proteins in human skeletal muscle with and without ongoing regenerative cycles, Exp. Physiol., 97, 774–784.CrossRefPubMedGoogle Scholar
  20. 20.
    Lupo, B., and Trusolino, L. (2014) Inhibition of poly(ADP-ribosyl)ation in cancer: old and new paradigms revisited, Biochim. Biophys. Acta, 1846, 201–215.PubMedGoogle Scholar
  21. 21.
    Hsiao, S. J., Poitras, M. F., Cook, B. D., Liu, Y., and Smith, S. (2006) Tankyrase 2 poly(ADP-ribose) polymerase domain-deleted mice exhibit growth defects but have normal telomere length and capping, Mol. Cell. Biol., 26, 2044–2054.CrossRefPubMedPubMedCentralGoogle Scholar
  22. 22.
    Longo, V. D., Mitteldorf, J., and Skulachev, V. P. (2005) Programmed and altruistic ageing, Nat. Rev. Genet., 6, 866–872.CrossRefPubMedGoogle Scholar
  23. 23.
    Skulachev, V. P. (2012) What is “phenoptosis” and how to fight it? Biochemistry (Moscow), 77, 689–706.CrossRefGoogle Scholar

Copyright information

© Pleiades Publishing, Ltd. 2016

Authors and Affiliations

  • A. N. Kuimov
    • 1
    Email author
  • A. S. Zhozhikashvili
    • 1
  • V. N. Manskikh
    • 2
  • L. V. Platonova
    • 3
  • T. G. Dyuzheva
    • 3
  1. 1.Belozersky Institute of Physico-Chemical BiologyLomonosov Moscow State UniversityMoscowRussia
  2. 2.Institute of MitoengineeringLomonosov Moscow State UniversityMoscowRussia
  3. 3.Sechenov First Moscow State Medical UniversityMoscowRussia

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