Abstract

Tumour expression of the urokinase plasminogen activator correlates with invasive capacity. Consequently, inhibition of this serine protease by physiological inhibitors should decrease invasion and metastasis. However, of the two main urokinase inhibitors, high tumour levels of the type 1 inhibitor actually promote tumour progression, whereas high levels of the type 2 inhibitor decrease tumour growth and metastasis. We propose that the basis of this apparently paradoxical action of two similar serine protease inhibitors lies in key structural differences controlling interactions with components of the extracellular matrix and endocytosis–signalling co-receptors.

Author affiliations

1. David R. Croucher is at the Cancer Research Program, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, New South Wales, Australia 2010.
2. Darren N. Saunders is at the Department of Pathology and Laboratory Medicine, University of British Columbia and the Molecular Oncology and Breast Cancer Program, British Columbia Cancer Research Centre, 675 West 10th Avenue, Vancouver, British Columbia, V5Z 1L3, Canada.
3. Sergei Lobov and Marie Ranson are at the School of Biological Sciences, University of Wollongong, Northfields Avenue, Wollongong, New South Wales 2522, Australia.

Correspondence to: Marie Ranson³ Email: mranson@uow.edu.au

Published online 12 June 2008

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