Skip to main content
SpringerLink
Log in

Negative regulation of transforming growth factor-β by the proteoglycan decorin

  • Letter
  • Published:

From Nature

View current issue Submit your manuscript

Abstract

DECORIN is a small chondroitin–dermatan sulphate proteoglycan consisting of a core protein and a single glycosaminoglycan chain1–3. Eighty per cent of the core protein consists of 10 repeats of a leucine-rich sequence of 24 amino acids2,4. Similar repeats have been found in two other proteoglycans, biglycan5 and fibromodulin6, and in several other proteins including Drosophila morphogenetic proteins7–11. Expression of high levels of decorin in Chinese hamster ovary cells has a dramatic effect on their morphology and growth properties1. We now report that this effect is due at least in part to the ability of decorin to bind transforming growth factor-β, an autocrine factor12,13 that stimulates the growth of Chinese hamster ovary cells. As transforming growth factor-β induces synthesis of decorin in many cell types14,15, our results suggest that decorin may be a component of a feedback system regulating cell growth.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Yamaguchi, Y. & Ruoslahti, E. Nature 336, 244–246 (1988).

    Article  ADS  CAS  PubMed  Google Scholar 

  2. Ruoslahti, E. A. Rev. Cell Biol. 4, 229–255 (1988).

    Article  CAS  Google Scholar 

  3. Krusius, T. & Ruoslahti, E. Proc. natn. Acad. Sci. U.S.A. 83, 7683–7687 (1986).

    Article  ADS  CAS  Google Scholar 

  4. Patthy, L. J. molec. Biol. 198, 567–577 (1987).

    Article  CAS  PubMed  Google Scholar 

  5. Fisher, L. W., Termine, J. D. & Young, M. F. J. biol. Chem. 264, 4571–4576 (1989).

    CAS  PubMed  Google Scholar 

  6. Oldberg, Å., Antonsson, P., Lindblom, K. & Heinegård, D. EMBO J. 8, 2601–2604 (1989).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  7. Takahashi, N., Takahashi, Y. & Putnam, F. W. Proc. natn. Acad. Sci. U.S.A. 82, 73–77 (1985).

    Article  ADS  CAS  Google Scholar 

  8. Titani, F., Takio, K., Handa, M. & Ruggeri, Z. M. Proc. natn. Acad. Sci. U.S.A. 82, 1906–1910 (1987).

    Google Scholar 

  9. Kataoka, T., Broek, D. & Wigler, M. Cell 43, 493–505 (1985).

    Article  CAS  PubMed  Google Scholar 

  10. Hashimoto, C., Hudson, K. L. & Anderson, K. V. Cell 52, 269–279 (1988).

    Article  CAS  PubMed  Google Scholar 

  11. Reinke, R., Krantz, D. E., Yen, D. & Zipursky, S. L. Cell 52, 291–301 (1987).

    Article  Google Scholar 

  12. Keski-Oja, J., Leof, E. B., Lyons, R. M., Coffey, Jr, J. R. & Moses, H. L. J. cell. Biochem. 33, 95–107 (1987).

    Article  CAS  PubMed  Google Scholar 

  13. Roberts, A. B. & Sporn, M. B. in Handbook exp. Pharmac. (eds Sporn, M. B. and Roberts, A. B.) Vol. 95, 419–472 (Springer, Heidelberg, 1990).

    Google Scholar 

  14. Bassols, A. & Massagué, J. J. biol. Chem. 263, 3039–3045 (1988).

    CAS  PubMed  Google Scholar 

  15. Okuda, S., Languino, L. R., Ruoslahti, E. & Border, W. A. J. clin. Invest. (in the press).

  16. Doege, K., Sasaki, M., Horigan, E., Hassell, J. R. & Yamada, Y. J. biol. Chem. 262, 17757–17767 (1987).

    CAS  PubMed  Google Scholar 

  17. Mann, D. M., Yamaguchi, Y., Bourdon, M. A. & Ruoslahti, E. J. biol. Chem. 265, 5317–5323 (1990).

    CAS  PubMed  Google Scholar 

  18. Ruoslahti, E. J. biol. Chem. 264, 13369–13372 (1989).

    CAS  PubMed  Google Scholar 

  19. Andres, J. L., Stanley, K., Chiefetz, S. & Massague, J. J. Cell Biol. 109, 3137–3145 (1989).

    Article  CAS  PubMed  Google Scholar 

  20. Voss, B., Glössl, J., Cully, Z. & Kresse, H. J. Histochem. Cytochem. 34, 1013–1019 (1986).

    Article  CAS  PubMed  Google Scholar 

  21. Rosenberg, L. C. et al. J. biol. Chem. 260, 6304–6313 (1985).

    CAS  PubMed  Google Scholar 

  22. Hoppe, W., Ranch, U. & Kresse, H. J. biol. Chem. 263, 5926–5932 (1988).

    CAS  PubMed  Google Scholar 

  23. Nugent, M. A., Lane, E. A., Keski-Oja, J., Moses, H. L. & Newman, M. J. Cancer Res. 49, 3884–3890 (1989).

    CAS  PubMed  Google Scholar 

  24. Cheifetz, S. et al. Cell 48, 409–415 (1987).

    Article  CAS  PubMed  Google Scholar 

  25. Derynck, R. et al. EMBO J. 7, 3737–3743 (1988).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

  26. Fisher, R. A. et al. Nature 331, 76–78 (1988).

    Article  ADS  CAS  PubMed  Google Scholar 

  27. Frolik, C. A., Wakefield, L. M., Smith, D. M. & Sporn, M. B. J. biol. Chem. 259, 10995–11000 (1984).

    CAS  PubMed  Google Scholar 

  28. Munson, P. J. & Ṙodbard, D. Analyt. Biochem. 107, 220–239 (1980).

    Article  CAS  PubMed  Google Scholar 

  29. Goetinck, P. F. in The Glycoconjugates Vol. 3 (ed. Horowitz, M. I.) (Academic, New York, 1982).

    Google Scholar 

  30. Oike, Y., Kimata, K., Shinomura, T., Nakazawa, K. & Suzuki, S. Biochem. J. 191, 193–207 (1980).

    Article  CAS  PubMed  PubMed Central  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Cancer Research Center, La Jolla Cancer Research Foundation, 10901 North Torrey Pines Road, La Jolla, California, 92037, USA

    Yu Yamaguchi, David M. Mann & Erkki Ruoslahti

Authors
  1. Yu Yamaguchi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. David M. Mann
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Erkki Ruoslahti
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yamaguchi, Y., Mann, D. & Ruoslahti, E. Negative regulation of transforming growth factor-β by the proteoglycan decorin. Nature 346, 281–284 (1990). https://doi.org/10.1038/346281a0

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1038/346281a0

  • Springer Nature Limited

This article is cited by

Search

Navigation