alexa Novel highly efficient intrabody mediates complete inhibition of cell surface expression of the human vascular endothelial growth factor receptor-2 (VEGFR-2 KDR).
Molecular Biology

Molecular Biology

Journal of Cell Science & Therapy

Author(s): Bldicke T, Weber H, Mueller PP, Barleon B, Bernal M

Abstract Share this page

Abstract The human vascular endothelial growth factor receptor-2 (VEGFR-2/KDR) and its ligand vascular endothelial growth factor (VEGF) play an essential role in tumor angiogenesis and in haematological malignancies. To inhibit VEGF induced signalling, intrabodies derived from two scFv fragments recognizing the VEGF receptor were generated. When these intrabodies were expressed in endothelial cells, they blocked the transport of KDR to the cell surface. We developed a cell culture model using porcine aortic endothelial cells overexpressing KDR for testing the efficiency of anti-KDR intrabodies. The two intrabodies were targeted to the ER and colocalized with the KDR receptor in an intracellular compartment. No degradation of the receptor was observed. An immature incomplete glycosylated protein of 195 kDa was detected, suggesting that the intrabodies affect the maturation of the receptor. Despite the presence of significant amounts of receptor protein, the inactivation by one of the two intrabodies was highly effective, resulting in complete functional inhibition of KDR and inhibition of in vitro angiogenesis. The new intrabody appears to be a powerful tool with which to inhibit KDR function. This article was published in J Immunol Methods and referenced in Journal of Cell Science & Therapy

Relevant Expert PPTs

Relevant Speaker PPTs

Recommended Conferences

Relevant Topics

Peer Reviewed Journals
Make the best use of Scientific Research and information from our 700 + peer reviewed, Open Access Journals
International Conferences 2017-18
Meet Inspiring Speakers and Experts at our 3000+ Global Annual Meetings

Contact Us

© 2008-2017 OMICS International - Open Access Publisher. Best viewed in Mozilla Firefox | Google Chrome | Above IE 7.0 version