

Scientists at the Georg-August-University generated different monoclonal antibodies which specifically react with either Il-8RA (CXCR1, Cdw128A) or Il-8RB (CXCR2, Cdw128B), a G protein linked seven transmembrane domain protein, expressed on monocytes, granulocytes and on a subset of T cells. Interleukin-8 (IL-8) is a potent inflammatory mediator that belongs to the family of C-X-C chemokines. IL-8 promotes the activation and the extravasation of circulating neutrophils to the site of inflammation. Two IL-8 receptor isotypes (type A and B) are identified in human and rabbit neutrophils. Both receptor subtypes A and B bind with high affinity to human IL-8, but they exhibit distinct binding affinity to two functional and structurally related IL-8 peptides, melanoma growth-stimulating activity peptide (MGSA) and neutrophil-activating peptide-2 (NAP-2). Human IL-8 receptor A binds with low affinity to MGSA or NAP-2. In contrast, human IL-8 receptor B binds MGSA with high affinity, and NAP-2 with lesser affinity.
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