Analysis of the CD23-αv integrin interaction: a study with model peptides

Edkins, A.L., Borland, G., Kelly, S.M. , Cogdell, R.J. , Ozanne, B.W. and Cushley, W. (2012) Analysis of the CD23-αv integrin interaction: a study with model peptides. Biochemical and Biophysical Research Communications, 422(2), pp. 207-212. (doi:10.1016/j.bbrc.2012.04.076)

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Publisher's URL: http://dx.doi.org/10.1016/j.bbrc.2012.04.076

Abstract

The human CD23 protein binds to αvβ3 and αvβ5 integrins. The integrins recognize a short tripeptide motif of arg-lys-cys (RKC) in CD23, and peptides containing this motif inhibit the binding of CD23 to B cells and monocytes; neither fibronectin, nor vitronectin, which contain arg-gly-asp motifs, inhibit binding of RKC-containing peptides to cells. RKC-containing peptides derived from CD23 show dose-dependent, biphasic binding profiles to both αvβ3 and αvβ5 that are cation-independent but sensitive to high chloride ion concentrations. Substitution of one basic residue in the RKC motif with alanine reduces but does not abolish integrin binding or the ability of peptides to stimulate pre-B cell growth or cytokine release by monocytes. Substitution of both basic residues abolishes both integrin binding and biological activity of CD23-derived peptides. These features indicate that binding of RKC-containing peptides to αv integrins has clearly distinct characteristics to those for binding of RGD-containing ligands.

Item Type:Articles
Status:Published
Refereed:Yes
Glasgow Author(s) Enlighten ID:Cushley, Professor William and Borland, Dr Gillian and Cogdell, Professor Richard and Ozanne, Professor Bradford and Kelly, Dr Sharon
Authors: Edkins, A.L., Borland, G., Kelly, S.M., Cogdell, R.J., Ozanne, B.W., and Cushley, W.
College/School:College of Medical Veterinary and Life Sciences > Institute of Molecular Cell and Systems Biology
College of Medical Veterinary and Life Sciences > School of Life Sciences
College of Medical Veterinary and Life Sciences > Institute of Infection Immunity and Inflammation
Journal Name:Biochemical and Biophysical Research Communications
ISSN:0006-291X
Published Online:27 April 2012

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