Earticle

초록

영어

The epidermal growth factor receptor (EGFR) is a member of the ErbB family of transmembrane tyrosine kinase receptors, which includes ErbB1 (or HER-1, or EGFR), ErbB2 (or HER-2/neu), ErbB3 (or HER-3), and ErbB4 (or HER-4) [1, 2]. The expression of EGFR is common in a number
of normal epithelial tissues, but in several solid tumors EGFR was overexpressed. For example, in NSCLC (non-small-cell lung cancer), overexpression of EGFR has been reported to be present in over 50% of cases in several series. Several EGFR inhibitors have been developed in
recent years, which can be mainly categorized into two classes: small molecules that are inhibitors of the intracellular tyrosine kinase domain by interfering with autophosphorylation by adenosine triphosphate (ATP), and monoclonal antibodies to the extracellular domain of the EGFR [1, 2]. A mouse mAb (A431-96) was raised against EGFR-ECD (extracellular domain). The mAb efficiently inhibited proliferation of A431 cells, which overexpress EGFR on the cell surface and this mAb (A431-96) binds EGFR with affinity of 5.7 x 108 M-1. Here we describe epitope mapping of the mAb in domain level. In competition methods, we used Erbitux and
EGF as a competitor which already known the binding sites. Furthermore, using yeast surface display of EGFR fragments [3], we identified the domain-level epitope of mAb which is in the domain III of EGFR-ECD.

키워드

저자

• Chang-Goo KIM [ Department of Molecular Science and Technology, Ajou University ]
• Ki-Hwan CHANG [ Central Research Center, GREEN CROSS corp., Yong-in 446-770, Korea. ]
• Se-Ho KIM [ Central Research Center, GREEN CROSS corp., Yong-in 446-770, Korea. ]
• Yong-Sung KIM [ Department of Molecular Science and Technology, Ajou University ]

참고문헌

발행기관

간행물

표지보기 관심저널 등록

• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576