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Expression of a Soluble Functional Form of the Integrin α4β1 in Mammalian Cells
Abstract:The integrin α4β1(VLA4) has been expressed as a soluble, active, heterodimeric immunoglobulin fusion protein. cDNAs encoding the extracellular domains of the human α4 and β1 subunits were fused to the genomic DNA encoding the human γ1 immunoglobulin Fc domain and functional integrin fusion protein was expressed as a secreted, soluble molecule from a range of mammalian cell lines. Specific mutations were introduced into the Fc region of the molecules to promote α4β1 heterodimer formation. The soluble α4β1 Fc fusion protein exhibited divalent cation dependent binding to VCAM-1, which was blocked by the appropriate function blocking antibodies. The apparent Kd for VCAM-1 binding were similar for both the soluble and native forms of α4β1. In addition, the integrin–Fc fusion was shown to stain cells expressing VCAM-1 on their surface by FACs analysis. This approach for expressing soluble α4β1 should be generally applicable to a range of integrins.
Keywords:VLA-4  α4β1  soluble integrins  VCAM-1  immunoadhesin  Fc-fusion protein
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