Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

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Horuk, R. et al.

The human erythrocyte inflammatory peptide (chemokine) receptor. Biochemical characterization, solubilization, and development of a binding assay for the soluble receptor.

In addition to the two human interleukin-8 (IL-8) receptors that have been cloned, IL-8RA and IL-8RB, we recently described a binding protein in human erythrocytes that binds IL-8 and monocyte chemotactic peptide-1 (MCP-1), which we have termed the chemokine (CK) receptor. This communication describes the biochemical characterization, detergent solubilization, and development of a solubilized receptor binding assay for the erythrocyte CK receptor. Competitive 125I-IL-8 binding studies in cells transfected with IL-8RA and IL-8RB revealed that only IL-8 and MGSA were able to displace the radiolabeled IL-8 from these cells. In contrast, a whole array of chemokines were able to cross-compete with 125I-IL-8 for binding to the CK receptor in erythrocyte ghosts. Scatchard analysis of 125I-IL-8 binding to erythrocyte membranes and to dodecyl beta-maltoside solubilized CK receptors revealed a single class of high affinity binding sites in both cases with KD values of 9.5 nM +/- 3.6 and 15.4 nM +/- 5.0, respectively. Chemical cross-linking studies with erythrocyte membranes and with solubilized CK receptors indicated that the CK receptor has a lower molecular mass than the cloned IL-8 receptors (39 kDa compared to 57-69 kDa). Treatment of the cross-linked 47-kDA protein with N-glycanase reduced its molecular mass to 42 kDa.[1]

References

The human erythrocyte inflammatory peptide (chemokine) receptor. Biochemical characterization, solubilization, and development of a binding assay for the soluble receptor. Horuk, R., Colby, T.J., Darbonne, W.C., Schall, T.J., Neote, K. Biochemistry (1993) [Pubmed]

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