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Korean Society for Biochemistry and Molecular Biology (생화학분자생물학회)
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Identification and Characterization of a Novel Angiostatin-binding Protein by the Display Cloning Method

  • Kang, Ha-Tan (Division of Life Sciences, Korea Institute of Science and Technology) ;
  • Bang, Won-Ki (Division of Biotechnology and Genetic Engineering, College of Life and Environmental Sciences, Korea University) ;
  • Yu, Yeon-Gyu (Division of Life Sciences, Korea Institute of Science and Technology)
  • Published : 2004.03.31
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Abstract

Angiostatin is a potent anti-angiogenic protein. To examine the angiostatin-interacting proteins, we used the display-cloning method with a T7 phage library presenting human cDNAs. The specific T7 phage clone that bound to the immobilized angiostatin was isolated, and a novel gene encoding the displayed polypeptide on the isolated T7 phage was identified. The displayed angiostatin-binding sequence was expressed in E. coli as a soluble protein and purified to homogeneity. This novel angiostatin-binding region interacted specifically to angiostatin with a dissociation constant of $3.4{\times}10^{-7}\;M$. A sequence analysis showed that the identified sequence was a part of the large ORF of 1,998 amino acids, whose function has not yet been characterized. A Northern analysis indicated that the gene containing the angiostatin-binding sequence was expressed differentially in the developmental stages or cell types.

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