G-helix of maspin mediates effects on cell migration and adhesion

Ravenhill, Lorna, Wagstaff, Laura, Edwards, Dylan R. ORCID: https://orcid.org/0000-0002-3292-2064, Ellis, Vincent and Bass, Rosemary (2010) G-helix of maspin mediates effects on cell migration and adhesion. Journal of Biological Chemistry, 285 (47). pp. 36285-36292. ISSN 0021-9258

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Maspin is a member of the serine protease inhibitor (serpin) superfamily that lacks protease inhibitory ability, although displaying tumor metastasis-suppressing activity resulting from its influence on cell migration, invasion, proliferation, apoptosis, and adhesion. The molecular mechanisms of these actions of maspin are as yet undefined. Here, we sought to identify critical functional motifs by the expression of maspin with point mutations at sites potentially involved in protein-protein interactions: the G a-helix (G-helix), an internal salt bridge or the P1 position of the reactive center loop. Our findings indicate that only mutations in the G-helix attenuated inhibition of cell migration by maspin and that this structural element is also involved in the effect of maspin on cell adhesion. The action of maspin on cell migration could be mimicked by a 15-mer G-helix peptide, indicating that the G-helix is both essential and sufficient for this effect. In addition, we provide evidence that the effects of the G-helix of maspin are dependent on ß1 integrins. These data reveal that the major extracellular functions associated with the tumor suppressive action of maspin likely involve interactions in which the G-helix plays a key role.

Item Type: Article
Faculty \ School: Faculty of Science > School of Biological Sciences
UEA Research Groups: Faculty of Science > Research Groups > Cells and Tissues
Faculty of Medicine and Health Sciences > Research Groups > Cancer Studies
Faculty of Science > Research Groups > Biosciences Teaching and Education Research
Depositing User: Users 2731 not found.
Date Deposited: 23 May 2011 13:49
Last Modified: 14 Jul 2023 16:30
URI: https://ueaeprints.uea.ac.uk/id/eprint/31266
DOI: 10.1074/jbc.M110.177253

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