JBC Focus on PI3-Kinase with Echelon

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Originally published In Press as doi:10.1074/jbc.C200532200 on October 15, 2002

J. Biol. Chem., Vol. 277, Issue 49, 46845-46848, December 6, 2002
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
277/49/46845    most recent
C200532200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bass, R.
Right arrow Articles by Ellis, V.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bass, R.
Right arrow Articles by Ellis, V.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

ACCELERATED PUBLICATION
Maspin Inhibits Cell Migration in the Absence of Protease Inhibitory Activity*

Rosemary Bass, Ana-María Moreno Fernández, and Vincent EllisDagger

From the School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, United Kingdom

Maspin is a member of the serpin family of protease inhibitors and is a tumor suppressor gene acting at the level of tumor invasion and metastasis. This in vivo activity correlates with the ability of maspin to inhibit cell migration in vitro. This behavior suggests that maspin inhibits matrix-degrading proteases, such as those of the plasminogen activation system, in a similar manner to the serpin PAI-1. However, there is controversy concerning the protease inhibitory activity of maspin. It is devoid of activity against a wide range of proteases, in common with other non-inhibitory serpins, but has recently been reported to inhibit plasminogen activators associated with cells and other biological surfaces (Sheng, S. J., Truong, B., Fredrickson, D., Wu, R. L., Pardee, A. B., and Sager, R. (1998) Proc. Natl. Acad. Sci. U. S. A. 95, 499-504; McGowen, R., Biliran, H., Jr., Sager, R., and Sheng, S. (2000) Cancer Res. 60, 4771-4778). We have compared the effects of maspin with those of PAI-1 in a range of situations in which plasminogen activation is potentiated, reflecting the biological context of this proteolytic system: urokinase-type plasminogen activator bound to its receptor on the surface of tumor cells, tissue-type plasminogen activator specifically bound to vascular smooth muscle cells, fibrin, and the prion protein. Maspin was found to have no inhibitory effect in any of these situations, in contrast to the efficient inhibition observed with PAI-1, but nevertheless maspin inhibited the migration of both tumor and vascular smooth muscle cells. We conclude that maspin is a non-inhibitory serpin and that protease inhibition does not account for its activity as a tumor suppressor.

* This work was supported by Grant PG/1999079 from the British Heart Foundation.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger Senior Research Fellow of the British Heart Foundation. To whom correspondence should be addressed: School of Biological Sciences, University of East Anglia, Norwich NR4 7TJ, UK. Tel.: 44-1603-592570; Fax: 44-1603-592250; E-mail: v.ellis@uea.ac.uk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Biol. Chem.Home page
M. Al-Ayyoubi, B. S. Schwartz, and P. G. W. Gettins
Maspin Binds to Urokinase-type and Tissue-type Plasminogen Activator through Exosite-Exosite Interactions
J. Biol. Chem., July 6, 2007; 282(27): 19502 - 19509.
[Abstract] [Full Text] [PDF]

Home page
 Mol Hum ReprodHome page
A. Dokras, J. Coffin, L. Field, A. Frakes, H. Lee, A. Madan, T. Nelson, G.-Y. Ryu, J.-G. Yoon, and A. Madan
Epigenetic regulation of maspin expression in the human placenta
Mol. Hum. Reprod., October 1, 2006; 12(10): 611 - 617.
[Abstract] [Full Text] [PDF]

Home page
 FASEB J.Home page
N. Cella, A. Contreras, K. Latha, J. M. Rosen, and M. Zhang
Maspin is physically associated with {beta}1 integrin regulating cell adhesion in mammary epithelial cells
FASEB J, July 1, 2006; 20(9): 1510 - 1512.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
R. H. P. Law, J. A. Irving, A. M. Buckle, K. Ruzyla, M. Buzza, T. A. Bashtannyk-Puhalovich, T. C. Beddoe, K. Nguyen, D. M. Worrall, S. P. Bottomley, et al.
The High Resolution Crystal Structure of the Human Tumor Suppressor Maspin Reveals a Novel Conformational Switch in the G-helix
J. Biol. Chem., June 10, 2005; 280(23): 22356 - 22364.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
K. Latha, W. Zhang, N. Cella, H. Y. Shi, and M. Zhang
Maspin Mediates Increased Tumor Cell Apoptosis upon Induction of the Mitochondrial Permeability Transition
Mol. Cell. Biol., March 1, 2005; 25(5): 1737 - 1748.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
M. Al-Ayyoubi, P. G. W. Gettins, and K. Volz
Crystal Structure of Human Maspin, a Serpin with Antitumor Properties: REACTIVE CENTER LOOP OF MASPIN IS EXPOSED BUT CONSTRAINED
J. Biol. Chem., December 31, 2004; 279(53): 55540 - 55544.
[Abstract] [Full Text] [PDF]

Home page
 Cancer Res.Home page
B. J. Nickoloff, M. W. Lingen, B.-D. Chang, M. Shen, M. Swift, J. Curry, P. Bacon, B. Bodner, and I. B. Roninson
Tumor Suppressor Maspin Is Up-Regulated during Keratinocyte Senescence, Exerting a Paracrine Antiangiogenic Activity
Cancer Res., May 1, 2004; 64(9): 2956 - 2961.
[Abstract] [Full Text] [PDF]

Home page
 DevelopmentHome page
F. Gao, H. Y. Shi, C. Daughty, N. Cella, and M. Zhang
Maspin plays an essential role in early embryonic development
Development, April 1, 2004; 131(7): 1479 - 1489.
[Abstract] [Full Text] [PDF]

Home page
 J. Immunol.Home page
S. Wen, C. P. Felley, H. Bouzourene, M. Reimers, P. Michetti, and Q. Pan-Hammarstrom
Inflammatory Gene Profiles in Gastric Mucosa during Helicobacter pylori Infection in Humans
J. Immunol., February 15, 2004; 172(4): 2595 - 2606.
[Abstract] [Full Text] [PDF]

Home page
 BloodHome page
M. Demeule, Y. Bertrand, J. Michaud-Levesque, J. Jodoin, Y. Rolland, R. Gabathuler, and R. Beliveau
Regulation of plasminogen activation: a role for melanotransferrin (p97) in cell migration
Blood, September 1, 2003; 102(5): 1723 - 1731.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
C. Ngamkitidechakul, D. J. Warejcka, J. M. Burke, W. J. O'Brien, and S. S. Twining
Sufficiency of the Reactive Site Loop of Maspin for Induction of Cell-Matrix Adhesion and Inhibition of Cell Invasion: CONVERSION OF OVALBUMIN TO A MASPIN-LIKE MOLECULE
J. Biol. Chem., August 22, 2003; 278(34): 31796 - 31806.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
M. L. Cher, H. R. Biliran Jr., S. Bhagat, Y. Meng, M. Che, J. Lockett, J. Abrams, R. Fridman, M. Zachareas, and S. Sheng
Maspin expression inhibits osteolysis, tumor growth, and angiogenesis in a model of prostate cancer bone metastasis
PNAS, June 24, 2003; 100(13): 7847 - 7852.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.