https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:1418 Sat 24 Mar 2018 08:28:14 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:14877 Sat 24 Mar 2018 08:22:24 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:11336 Sat 24 Mar 2018 08:13:29 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:17425 Sat 24 Mar 2018 08:01:39 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:42806 27-IGF-II inhibits IGF-I:IGFBP:VN-stimulated breast cancer cell migration and proliferation in two- and three-dimensional assay systems. Peptide arrays screened to identify regions critical for the IGFBP-3/-5:VN and IGF-II:VN interactions demonstrated IGFBP-3/-5 and IGF-II binds VN through the hemopexin-2 domain, and VN binds IGFBP-3 at residues not involved in the binding of IGF-I to IGFBP-3. IGFBP-interacting VN peptides identified from these peptide arrays disrupted the IGF-I:IGFBP:VN complex, impeded the growth of primary tumor-like spheroids and, more importantly, inhibited the invasion of metastatic breast cancer cells in 3D assay systems. These studies provide first-in-field evidence for the utility of small peptides in antagonizing GF:ECM-mediated biologic functions and present data demonstrating the potential of these peptide antagonists as novel therapeutics.]]> Mon 05 Sep 2022 09:43:19 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:28221 Fri 16 Oct 2020 16:09:46 AEDT ]]>