Analysis of the CD23-伪v integrin interaction: A study with model peptides

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• 作者：Adrienne L. Edkins^a ; ¹ ; Gillian Borland^a ; ² ; Sharon M. Kelly^a ; Richard J. Cogdell^a ; Bradford W. Ozanne^b ; William Cushley^a ; ^{William.Cushley@glasgow.ac.uk}
• 关键词：CD23 ; 伪v Integrins ; Surface plasmon resonance
• 刊名：Biochemical and Biophysical Research Communications
• 出版年：2012
• 期刊代码：159_0006291x
• 类别：bio
• 出版时间：1 June, 2012
• 卷：422
• 期：2
• 页码：207-212
• 文件大小：789 K

摘要

The human CD23 protein binds to 伪v尾3 and 伪v尾5 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 伪v尾3 and 伪v尾5 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 伪v integrins has clearly distinct characteristics to those for binding of RGD-containing ligands.