Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 14-Day Trial for You or Your Team.

Learn More →

Session 11: Novel Technology

Session 11: Novel Technology Human Antibodies 19 (2010) 57–60 DOI 10.3233/HAB-2010-0227 IOS Press Friday 16th April 2010. Moderators: Mark C. Glassy and Jim W. Larrick [13.30–14.00] ‘Novel antibody functions from novel antibody structures’ 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 beneficial 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Human Antibodies IOS Press

Session 11: Novel Technology

Human Antibodies , Volume 19 (2) – Jan 1, 2010

Loading next page...
 
/lp/ios-press/session-11-novel-technology-TqUwIlv5KX

References

References for this paper are not available at this time. We will be adding them shortly, thank you for your patience.

Publisher
IOS Press
Copyright
Copyright © 2010 by IOS Press, Inc
ISSN
1093-2607
eISSN
1875-869X
DOI
10.3233/HAB-2010-0227
Publisher site
See Article on Publisher Site

Abstract

Human Antibodies 19 (2010) 57–60 DOI 10.3233/HAB-2010-0227 IOS Press Friday 16th April 2010. Moderators: Mark C. Glassy and Jim W. Larrick [13.30–14.00] ‘Novel antibody functions from novel antibody structures’ 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 beneficial 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

Journal

Human AntibodiesIOS Press

Published: Jan 1, 2010

There are no references for this article.