Interaction between IGFBP-5 and TNFR1 


Vol. 31,  No. 7, pp. 2019-2024, Jul.  2010
10.5012/bkcs.2010.31.7.2019


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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 KD 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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  Cite this article

[IEEE Style]

E. J. Kim, M. S. Jeong, J. R. Hwang, J. H. Lee, S. B. Jang, "Interaction between IGFBP-5 and TNFR1," Bulletin of the Korean Chemical Society, vol. 31, no. 7, pp. 2019-2024, 2010. DOI: 10.5012/bkcs.2010.31.7.2019.

[ACM Style]

Eun Jung Kim, Mi Suk Jeong, Jae Ryoung Hwang, Je Ho Lee, and Se Bok Jang. 2010. Interaction between IGFBP-5 and TNFR1. Bulletin of the Korean Chemical Society, 31, 7, (2010), 2019-2024. DOI: 10.5012/bkcs.2010.31.7.2019.