Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

De-mystifying the mechanism(s) of maspin

Recent findings indicate that p53 regulates the expression of the tumor suppressor gene maspin, providing new mechanistic information about the factors that negatively regulate tumor cell metastasis.

This is a preview of subscription content, access via your institution

Relevant articles

Open Access articles citing this article.

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Hypothetical model for the expression of maspin (mammary serine protease inhibitor) in a normal mammary epithelial cell, in which the tumor suppressive function of maspin is intact along with transactivation through the (Ets) element.

References

  1. Zou, Z. et al. Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. Science 263, 526–529 (1994).

    Article  CAS  Google Scholar 

  2. Sager, R., Sheng, S., Pemberton, P.A. & Hendrix, M.J.C. in Current Topics in Microbiology and Immunology 213 (eds. Buntert and W. Birchmeier) 51–64 (Springer-Verlag, Berlin, 1996).

    Google Scholar 

  3. Zhou, Z. et al. P53 regulates the expression of the tumor suppressor gene. J. Biol. Chem. 275, 6051–6054 (2000).

    Article  Google Scholar 

  4. Sheng, S., Pemberton, P.A. & Sager, R. Production, purification, and characterization of recombinant maspin proteins. J. Biol. Chem. 269, 30988–30993 (1994).

    CAS  PubMed  Google Scholar 

  5. Sager, R. Function of maspin. Science 265, 1893 (1994).

    Article  Google Scholar 

  6. Pemberton, P.A. et al. The tumor suppressor maspin does not undergo the stress to relaxed transition or inhibit trypsin-like serine proteases. J. Biol. Chem. 270, 15832–15837 (1995).

    Article  CAS  Google Scholar 

  7. Fitzpatrick, P.A., Wong, D.T., Barr, P.J. & Pemberton, P.A. Functional implications of the modeled structure of maspin. Protein Eng. 9, 585–589 (1996).

    Article  CAS  Google Scholar 

  8. Pemberton, P.A. et al. Maspin is an intracellular serpin that partitions into secretory vesicles and is present at the cell surface. J. Histochem. Cytochem. 45, 1697–1706 (1997).

    Article  CAS  Google Scholar 

  9. Sheng, S. et al. Tissue-type plasminogen activator is a target of the tumor suppressor gene maspin. Proc. Natl. Acad. Sci. USA 95, 499–504 (1998).

    Article  CAS  Google Scholar 

  10. Liu T., Pemberton, P.A. & Robertson, A.D. Three-state unfolding and self-association of maspin, a tumor-suppressing serpin. J. Biol. Chem. 274,29628–29632 (1999).

    Article  CAS  Google Scholar 

  11. Sheng, S. et al. Maspin acts at the cell membrane to inhibit invasion and motility of mammary and prostatic cancer cells. Proc. Natl. Acad. Sci. USA 93, 11669–11674 (1996).

    Article  CAS  Google Scholar 

  12. Sternlicht, M.D. et al. Characterizations of the extracellular matrix and proteinase inhibitor content of human myoepithelial tumors. Laboratory Invest. 74, 781–796 (1996).

    CAS  Google Scholar 

  13. Sternlicht, M.D. et al. The human myoepithelial cell is a natural tumor suppressor. Clinical Cancer Res. 3, 1949–1958 (1997).

    CAS  Google Scholar 

  14. Seftor, R.E.B. et al. Maspin suppresses the invasive phenotype of human breast carcinoma. Cancer Res. 58, 5681–5685 (1998).

    CAS  PubMed  Google Scholar 

  15. Zhang, M., Volpert, O., Shi, Y.H. & Bouck N. Maspin is an angiogenesis inhibitor. Nature Med. 6,196–199 (2000).

    Article  Google Scholar 

  16. Zhang, M., David, M. & Sager, R. Expression of maspin in prostate cells is regulated by a positive Ets element and a negative hormonal responsive element site recognized by androgen receptor. Proc. Natl. Acad. Sci. USA 94, 5673–5678 (1997).

    Article  CAS  Google Scholar 

  17. Domann, F.E., Rice, J.C., Hendrix, M.J.C. & Futscher, B.W. Epigenetic silencing of maspin gene expression in human breast cancers. Int. J. Cancer 85, 805, 810 (2000).

    Article  CAS  Google Scholar 

  18. Li, J.-J., Colburn, N.H. & Oberley, L.W. Maspin gene expression in tumor suppression induced by overexpressing manganese-containing superoxide dismutase cDNA in human breast cancer cells. Carcinogenesis 19,833–839 (1998).

    Article  CAS  Google Scholar 

  19. Mashimo, T. et al. The expression of the KAI1 gene, a tumor metastasis suppressor, is directly activated by P53. Proc. Natl. Acad. Sci. USA 95, 11307–11311 (1998).

    Article  CAS  Google Scholar 

  20. Effert, P.J., Neubauer, A., Walther, P.J. & Liu, E.T. Alterations of the P53 gene are associated with the progression of a human prostate carcinoma. J. Urol. 147, 789–793 (1992).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hendrix, M. De-mystifying the mechanism(s) of maspin. Nat Med 6, 374–376 (2000). https://doi.org/10.1038/74624

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/74624

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing