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Human Antibodies 19 (2010) 57â60 DOI 10.3233/HAB-2010-0227 IOS Press Friday 16th April 2010. Moderators: Mark C. Glassy and Jim W. Larrick [13.30â14.00] âNovel antibody functions from novel antibody structuresâ James W. Larrick, Manley Huang, Andrew Mendelsohn, Vikram Sharma, Susan C. Wright, Jianming Wang and Jeff Fang Panorama Research Institute (PRI), Sunnyvale, California, USA Hepatocyte growth factor (HGF) is a pleiotropic cytokine that promotes cell proliferation, motility, survival, and morphogenesis. HGF binds to its receptor c-Met tyrosine kinase and triggers signal transduction that protects cells against apoptosis and enhances cell growth for tissue regeneration. The profound effects of HGF to prevent cell death and to promote tissue regeneration make HGF an interesting drug candidate for therapeutic use. However, the activation of c-Met by HGF also lead to enhanced tumor metastasis and invasion. This pro-invasive feature of HGF has raised concerns regarding its clinical applications. It would be ideal to separate the beneï¬cial cell-protective signals from the pro-invasive signals of HGF. To test this possibility, Michieli et al., (Nature Biotechnology 20:488; 2002) created a recombinant single-chain chimera consisting of a truncated HGF α-chain and a truncated MSP (macrophage-stimulating protein, a cytokine with high homology to HGF) α-chain linked by a
Human Antibodies – IOS Press
Published: Jan 1, 2010
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