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A Flow Cytometry-based Assay to Identify Compounds That Disrupt Binding of Fluorescently-labeled CXC Chemokine Ligand 12 to CXC Chemokine Receptor 4

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CD14 is a ligand for the integrin alpha4beta1.

Jonathan D Humphries¹, Martin J Humphries

¹Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Michael Smith Building, Oxford Road, Manchester M13 9PT, United Kingdom.

|February 6, 2007

Summary

The integrin alpha4beta1 directly binds to CD14, a lipopolysaccharide receptor. This novel interaction is activation-dependent, similar to other alpha4beta1 ligand interactions, and warrants further investigation.

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Area of Science:

Immunology
Cell Biology
Molecular Biology

Background:

Integrin alpha4beta1 mediates crucial cell adhesion processes.
CD14, the lipopolysaccharide receptor, has diverse functions, some overlapping with alpha4beta1.
Potential overlap suggests a direct interaction between alpha4beta1 and CD14.

Purpose of the Study:

To investigate the direct interaction between integrin alpha4beta1 and CD14.
To characterize the binding properties of this novel interaction.

Main Methods:

Adhesion assays using Jurkat T cells (alpha4beta1(+)) and K562 cells (alpha4beta1(-)) with CD14-Fc.
Re-expression of the alpha4-subunit in K562 cells.
Solid-phase binding assays with affinity-purified alpha4beta1 and CD14-Fc.
Activation-dependent binding studies using anti-beta1 mAbs.

Main Results:

Jurkat T cells adhered to CD14-Fc via alpha4beta1; K562 cells did not, but gained the ability upon alpha4 re-expression.
Adhesion to CD14 was activation-dependent, mirroring alpha4beta1 binding to VCAM-1.
CD14-Fc bound directly to purified alpha4beta1 in an activation-dependent manner.
JY cells (alpha4beta7(+)) also showed alpha4-dependent attachment to CD14-Fc.

Conclusions:

CD14 is identified as a novel ligand for integrin alpha4beta1.
The binding is activation-dependent, consistent with known alpha4beta1 ligand interactions.
Further studies are needed to explore the biological significance of this alpha4beta1-CD14 interaction.