Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Interaction between IGFBP-5 and TNFR1

  • Kim, Eun-Jung (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Jeong, Mi-Suk (Department of Molecular Biology, College of Natural Sciences, Pusan National University) ;
  • Hwang, Jae-Ryoung (Molecular Therapy Research Center, Sungkyunkwan University) ;
  • Lee, Je-Ho (Molecular Therapy Research Center, Sungkyunkwan University) ;
  • Jang, Se-Bok (Department of Molecular Biology, College of Natural Sciences, Pusan National University)
  • Received : 2010.04.19
  • Accepted : 2010.05.31
  • Published : 2010.07.20
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Abstract

Insulin-like growth factor binding protein 5 (IGFBP-5) plays an important role in controlling cell survival, differentiation and apoptosis. Apoptosis can be induced by an extrinsic pathway involving the ligand-mediated activation of death receptors such as tumor necrosis factor receptor 1 (TNFR1). To determine whether IGFBP-5 and TNFR1 interact as members of the same apoptosis pathway, recombinant IGFBP-5 and TNFR1 were isolated. The expression and purification of the full-length TNFR1 and truncated IGFBP-5 proteins were successfully performed in E. coli. The binding of both IGFBP-5 and TNFR1 proteins was detected by surface plasmon resonance spectroscopy (BIAcore), fluorescence measurement, electron microscopy, and size-exclusion column (SEC) chromatography. IGFBP-5 indeed binds to TNFR1 with an apparent $K_D$ of 9 nM. After measuring the fluorescence emission spectra of purified IGFBP-5 and TNFR1, it was found that the tight interaction of these proteins is accompanied by significant conformational changes of one or both. These results indicate that IGFBP-5 acts potently as a novel ligand for TNFR1.

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