Endocrine

, Volume 25, Issue 1, pp 27–32 | Cite as

Androgen receptor regulates expression of skeletal muscle-specific proteins and muscle cell types

  • Saleh Altuwaijri
  • Dong Kun Lee
  • Kuang-Hsiang Chuang
  • Huei-Ju Ting
  • Zhiming Yang
  • Qingquan Xu
  • Meng-Yin Tsai
  • Shuyuan Yeh
  • LeRoy A. Hanchett
  • Hong-Chiang Chang
  • Chawnshang Chang
Original Articles

Abstract

C2C12 myoblasts expressing the androgen receptor (AR) were used to analyze the role of androgen-AR signaling pathway in skeletal muscle development. Marked up-regulation of AR expression was observed in differentiated myotubes. A nuclear run-on transcription assay demonstrated that transcription of the AR gene is increased during skeletal muscle cell differentiation. Regulation of skeletal muscle-specific protein expression by the androgen-AR signaling pathway was further analyzed using quadriceps skeletal muscle from wild-type (WT) and AR knock-out (ARKO) male mice. A histological analysis of quadriceps skeletal muscle indicates no morphological differences between ARKO and WT mice. However, the androgen-AR signaling pathway increases expression of slow-twitch-specific skeletal muscle proteins and downregulates fast-twitch-specific skeletal muscle proteins, resulting in an increase of slow-twitch muscle fiber type cells in quadriceps muscle.

Key Words

Androgen receptor skeletal muscle slowtwitch fiber type testosterone 

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References

  1. 1.
    Chang, C., Saltzman, A., Yeh, S., et al. (1995). Critic Rev. Eukayrotic Gene Expression 5, 97–125.Google Scholar
  2. 2.
    Tindall, D. J. (2000). Androgen receptors in prostate and skeletal muscle. Mayo Clin. Proc. 75(Suppl), S26-S31.PubMedGoogle Scholar
  3. 3.
    Lubahn, D. B., Joseph, D. R., Sullivan, P. M., Willard, H. F., French, F. S., and Wilson, E. M. (1988). Science 240, 327–330.PubMedCrossRefGoogle Scholar
  4. 4.
    Trapman, J., Klaasen, P., Kuiper, G. G. J. M., et al. (1988). Biochem. Biophys. Res. Comm. 153, 241–248.PubMedCrossRefGoogle Scholar
  5. 5.
    McKenna, N. J., Lanz, R. B., and O’Malley, B. W. (1999). Endocr. Rev. 20, 321–344.PubMedCrossRefGoogle Scholar
  6. 6.
    Robyr, D., Wolffe, A. P., and Wahli, W. (2000). Mol. Endocrinol. 14, 329–347.PubMedCrossRefGoogle Scholar
  7. 7.
    Heinlein, C. and Chang, C. (2002). Endocr. Rev. 23, 175–2000.PubMedCrossRefGoogle Scholar
  8. 8.
    Nishimura, K., Ting, H. J., Harada, Y., et al. (2003). Cancer Res. 63, 4888–4894.PubMedGoogle Scholar
  9. 9.
    Hickson, R. C., Galassi, T. M., Kurowski, T. T., Daniels, D. G., and Chatterton, R. T. (1983). Steroid Biochem. 19, 1705–1712.CrossRefGoogle Scholar
  10. 10.
    Hickson, R. C., Kurowski, T. T., Galassi, T. M., Daniels, D. G., and Chatterton, R. J. (1985). Can. J. Biochem. Cell Biol. 63, 348–354.PubMedCrossRefGoogle Scholar
  11. 11.
    Sheffield-Moore, M. (2000). Ann. Med. 32, 181–186.PubMedGoogle Scholar
  12. 12.
    Bhasin, S., Woodhouse, L., and Storer, T. W. (2001). J. Endocrinol. 170, 27–38.PubMedCrossRefGoogle Scholar
  13. 13.
    Lieber, R. L. (2002). In: Skeletal muscle structure, function, and plasticity. Tim Julet (ed.). Lippincott Williams & Wilkins: Baltimore, pp. 1–44.Google Scholar
  14. 14.
    Lieber, R. L. (2002). In: Skeletal muscle structure, function, and plasticity. Tim Julet (ed.). Lippincott Williams & Wilkins: Baltimore, pp. 45–112.Google Scholar
  15. 15.
    Sabourin, L. A. and Rudnicki, M. A. (2000). Clin. Genet. 57, 16–25.PubMedCrossRefGoogle Scholar
  16. 16.
    Naya, F. J. and Olson, E. (1999). Curr. Opinion Cell. Biol. 11, 683–688.PubMedCrossRefGoogle Scholar
  17. 17.
    Lee, D. K. (2002). Biochem. Biophys. Res. Commun. 294, 408–413.PubMedCrossRefGoogle Scholar
  18. 18.
    Yeh, S., Tsai, M. Y., Xu, Q., et al. (2002). Proc. Natl. Acad. Sci. USA 99, 13498–13503.PubMedCrossRefGoogle Scholar
  19. 19.
    Lee, D. K., Duan, H., and Chang, C. (2001). J. Biol. Chem. 276, 9978–9984.PubMedCrossRefGoogle Scholar
  20. 20.
    Galbiati, F., Volonte, D., Engelman, J. A., Scherer, P., and Lisanti, M. P. (1999). J. Biol. Chem. 274, 0315–30321.Google Scholar
  21. 21.
    Mizokami, A., Yeh, S., and Chang, C. (1994). Mol. Endocrinol. 8, 77–88.PubMedCrossRefGoogle Scholar
  22. 22.
    Eick, D., Kohlhuber, F., Wolf, D. A., and Strobl, L. J. (1994). Anal. Biochem. 218, 347–351.PubMedCrossRefGoogle Scholar
  23. 23.
    Gregory, C. W., Johnson, R. T., Mohler, J., French, F., and Wilson, E. M. (2001). Cancer Res. 61, 2892–2898.PubMedGoogle Scholar
  24. 24.
    Altuwaijri, S., Lin, H. K., Chuang, K. H., et al. (2003). Cancer Res. 63, 7106–7112.PubMedGoogle Scholar
  25. 25.
    Sasaki, M., Tanaka, Y., Perinchery, G., et al. (2001). J. Natl. Cancer Inst. 94, 384–390.Google Scholar
  26. 26.
    Bottinelli, R., Schiaffino, S., and Reggiani, C. (1991). J. Physiology 437, 655–672.Google Scholar
  27. 27.
    Marin, P., Krotkiewski, M., and Bjorntorp, P. (1992). Eur. J. Med. 1, 329–336.PubMedGoogle Scholar

Copyright information

© Humana Press Inc 2004

Authors and Affiliations

  • Saleh Altuwaijri
    • 1
  • Dong Kun Lee
    • 1
  • Kuang-Hsiang Chuang
    • 1
  • Huei-Ju Ting
    • 1
  • Zhiming Yang
    • 1
  • Qingquan Xu
    • 1
  • Meng-Yin Tsai
    • 2
  • Shuyuan Yeh
    • 1
  • LeRoy A. Hanchett
    • 1
  • Hong-Chiang Chang
    • 3
  • Chawnshang Chang
    • 1
  1. 1.George Whipple Lab for Cancer Research, Departments of Pathology, Urology, and Cancer CenterUniversity of Rochester Medical CenterRochester
  2. 2.Department of OB/GYNChang Gang UniversityKaohsiungTaiwan
  3. 3.Department of UrologyNational Taiwan UniversityTaipeiTaiwan

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