Authors
Hongqi Lue, Manfred Dewor, Juergen Bernhagen, and Christian Weber
Summary
Based on an observed apparent structural homology between the monomeric structure of the cytokine MIF and the CXCL8 dimer, we have tested whether MIF can directly interact with the cognate CXCL8 receptor CXCR2. Functional interaction between a ligand or agonist and its receptor can reliably be determined by studying internalization of the receptor, a process that follows binding of the ligand. Applying a receptor internalization assay in human epithelial kidney cells (HEK) or RAW 264.7 macrophages stably overexpressing CXCR2 and other biochemical interaction assays, we found that MIF in fact interacts with CXCR2, leading to a comparable internalization rate of CXCR2 as that induced by the cognate ligand CXCL8 (ref. 1).Further details
The protocol was published on Protocol Exchange in 2007. To see the entire protocol, click on the source link.Advertisement
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