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Submitted on February 25, 2003
Accepted on April 11, 2003
1 Department of Biomedical Sciences, Ontario Veterinary College, University of Guelph, Guelph, ON, N1G 2W1, Canada; Millennium Pharmaceuticals Inc., Cambridge, MA, USA.
* To whom correspondence should be addressed. E-mail: a.summerlee{at}exec.uoguelph.ca.
This study reports the characterization of an adenoviral vector (rAd) containing a tetracycline-regulatable promoter, driving the bicistronic expression of the human H2 preprorelaxin (hH2) cDNA and enhanced green fluorescent protein, via an internal ribosomal entry site. A hH2 ELISA was used to measure the secreted levels of recombinant hH2 in transfected canine (CF33.Mt) and human (MDA-MB-435) mammary cancer cell lines over a 6-day period; secreted peptide peaked on days 2 and 4 for the canine and human cell types, respectively. An unprocessed hH2 immunoreactive form of approximately 18kD was identified by western blotting analysis and confirmed by mass spectrometry, suggesting that prorelaxin remains unprocessed in these cell types. The biological activity of the adenovirally-expressed human prorelaxin was measured in the established THP-1 cAMP ELISA and in an in vitro Transwell cell migration system. Exogenous recombinant hH2 and adenovirally-mediated delivery of prorelaxin to CF33.Mt cells conferred a significant migratory action in the cells, compared with controls. Cell proliferation assays were performed to discount the possibility that the effect of relaxin was mitogenic. Thus, we have demonstrated that prorelaxin has the ability to facilitate cell migration processes exclusive of its ability to stimulate cell proliferation. In validating this adenovirus-based system, we have created a potential tool for further exploration of the physiology of relaxin in mammalian systems.
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