Journal article
Simultaneous Binding of the Anti-Cancer IgM Monoclonal Antibody PAT-SM6 to Low Density Lipoproteins and GRP78
Z Rosenes, YF Mok, S Yang, MDW Griffin, TD Mulhern, DM Hatters, F Hensel, GJ Howlett
Plos One | PUBLIC LIBRARY SCIENCE | Published : 2013
Abstract
The tumour-derived monoclonal IgM antibody PAT-SM6 specifically kills malignant cells by an apoptotic mechanism linked to the excessive uptake of plasma lipids. The mechanism is postulated to occur via the multi-point attachment of PAT-SM6 to the unfolded protein response regulator GRP78, located on the surface of tumour cells, coupled to the simultaneous binding of plasma low density lipoprotein (LDL). We prepared and characterised LDL and oxidized LDL using sedimentation velocity and small-angle X-ray scattering (SAXS) analysis. Enzyme-linked immunosorbent (ELISA) techniques indicated apparent dissociation constants of approximately 20 nM for the binding of LDL or oxidized LDL to PAT-SM6. ..
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Awarded by Patrys
Funding Acknowledgements
This work is supported by an ARC linkage grant (LP100100392) and by Patrys Ltd, a company currently conducting clinical trials of PAT-SM6 as a potential anti-cancer treatment. FH is the managing director of Patrys, GmbH. The PAT-SM6 antibody is proprietary to Patrys Limited and the company agrees to make to make freely available any materials and information described in their publication that may be reasonably requested for the purpose of academic, non-commercial research. Due to the proprietary nature of the antibody parties will need to enter into a material transfer agreement. This does not alter the authors' adherence to all the PLOS ONE policies on sharing data and materials. The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.