Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor

Minghui Huang; Wan Ping Lai; Man Sau Wong; Mengsu Yang

doi:10.1016/S0014-5793(01)02780-6

Author(s)

Minghui Huang
Wan Ping Lai
Man Sau Wong
Mengsu Yang

Detail(s)

Original language	English
Pages (from-to)	31-36
Journal / Publication	FEBS Letters
Volume	505
Issue number	1
Publication status	Published - 7 Sept 2001

Link(s)

DOI	DOI https://doi.org/10.1016/S0014-5793(01)02780-6 Final Published version
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Link to Scopus	https://www.scopus.com/record/display.uri?eid=2-s2.0-0035823108&origin=recordpage
Permanent Link	https://scholars.cityu.edu.hk/en/publications/publication(6adaad4a-b8ac-448e-8c45-980cba0c5ee0).html

Abstract

A receptor binding assay based on the surface plasmon resonance (SPR) biosensor technique was developed to study the interaction between insulin-like growth factor-1 receptor (IGF-1R) and its intracellular substrate protein insulin receptor substrate-1 (IRS-1). The sensor surface was modified with anti-IGF-1R (α-subunit) monoclonal antibodies for the capturing of the receptor-containing membrane fragments from cell lysates. The IGF-1R was successfully immobilized on the sensor surface with binding capability for its intracellular substrates. SPR measurements showed that the tyrosine phosphorylation of IGF-1R induced by its extracellular ligand insulin-like growth factor-1 caused the receptor to bind with IRS-1 10 times faster than the unactivated receptor. As a result, the affinity constants of IRS-1 to phosphorylated and unphosphorylated IGF-1R were (8.06 ± 5.18) × 10⁹ M^-1 and (9.81 ± 4.61) × 10⁸ M^-1, respectively. © 2001 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.

Research Area(s)

Biosensor, Insulin receptor substrate-1, Insulin-like growth factor-1 receptor, Surface plasmon resonance, Tyrosine phosphorylation

SDG 3 - Good Health and Well-being

Citation Format(s)

[ RIS ] [ BibTeX ]

Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor. / Huang, Minghui; Lai, Wan Ping; Wong, Man Sau et al.
In: FEBS Letters, Vol. 505, No. 1, 07.09.2001, p. 31-36.

Research output: Journal Publications and Reviews › RGC 21 - Publication in refereed journal › peer-review

Huang, M, Lai, WP, Wong, MS & Yang, M 2001, 'Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor', FEBS Letters, vol. 505, no. 1, pp. 31-36. https://doi.org/10.1016/S0014-5793(01)02780-6

Huang, M., Lai, W. P., Wong, M. S., & Yang, M. (2001). Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor. FEBS Letters, 505(1), 31-36. https://doi.org/10.1016/S0014-5793(01)02780-6

Huang M, Lai WP, Wong MS, Yang M. Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor. FEBS Letters. 2001 Sept 7;505(1):31-36. doi: 10.1016/S0014-5793(01)02780-6

Huang, Minghui ; Lai, Wan Ping ; Wong, Man Sau et al. / Effect of receptor phosphorylation on the binding between IRS-1 and IGF-1R as revealed by surface plasmon resonance biosensor. In: FEBS Letters. 2001 ; Vol. 505, No. 1. pp. 31-36.