Earticle

초록

영어

Vascular endothelial growth factor (VEGF) and its receptors (VEGFR) have been implicated in promoting solid tumor growth and metastasis via stimulating tumor-associated angiogenesis. Models of murine tumor angiogenesis and receptor-specific antibodies are required to
evaluate roles of VEGF receptors in mouse xenograft models of human cancer. Human VEGFR-2 (also known as kinase insert domaincontaining receptor, KDR) and murine VEGFR-2 (or Fetal liver kinase-1, Flk-1) share 85% amino acid sequence identity in their extracellular domain. However, sequence homology of VEGF binding domain of KDR and Flk1 is less than 75%. Until now, none of available KDR neutralizing antibodies has species crossreactivity. We first describe here the development of fully human antibodies that cross-react with mouse, rat and human VEGFR-2. High-affinity, species cross-reactive, ScFv antibodies specific for KDR/Flk-1 were
selected from fully human naïve antibody phage display library we constructed. The selected and converted fully human IgG antibodies were found to bind to purified KDR with sub-nanomolar affinity. Their binding epitope locate in the IgG like domain 3 of extracellular domain of VEGFR-2, which is responsible for neutralizing effect of KDR function. I will discuss about recent in vivo data and part of preclinical data of anti-KDR antibody.

저자

• Jin-San Yoo [ Therapeutic Antibody Research Center, Korea Research Institute of Bioscience and Biotechnology, Daejeon, Republic of Korea ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576