The study describes the cloning of a cDNA encoding a functional human interleukin-8 (IL-8) receptor. The receptor was identified through RNA hybridization experiments using a cDNA probe from the human IL-8 receptor. The results showed that the receptor was expressed in neutrophils and certain cell lines, but not in monocytes. The receptor shares 77% amino acid identity with another human neutrophil receptor and 69% with a rabbit N-formyl peptide receptor. The receptor has a unique structure, including a short third intracellular loop and several serine and threonine residues that may function as phosphorylation sites. The receptor also contains acidic residues in the NH2-terminal extracellular region, which may be involved in binding to IL-8, a basic protein with a pI of ~9.5. The IL-8 receptor is a G protein-coupled receptor that activates intracellular calcium stores upon binding to IL-8. The receptor has a low affinity for IL-8 and is expressed in neutrophils and certain cell lines. The receptor also binds to structurally related ligands, including MGSA and NAP-2, with varying degrees of potency. The receptor is not activated by C5a, a structurally unrelated chemoattractant. The study also describes the genomic analysis of the IL-8 receptor, showing that it is encoded by a single gene in the human genome. The receptor is expressed in neutrophils and certain cell lines, but not in monocytes. The receptor shares less than 30% amino acid identity with other G protein-coupled receptors, including the human N-formyl peptide receptor. The study concludes that the IL-8 receptor is a functional receptor for IL-8 and is expressed in neutrophils and certain cell lines. The receptor has a unique structure and function, and its expression is regulated by specific mechanisms. The study also highlights the importance of the receptor in immune responses and the potential for further research into its function and regulation.The study describes the cloning of a cDNA encoding a functional human interleukin-8 (IL-8) receptor. The receptor was identified through RNA hybridization experiments using a cDNA probe from the human IL-8 receptor. The results showed that the receptor was expressed in neutrophils and certain cell lines, but not in monocytes. The receptor shares 77% amino acid identity with another human neutrophil receptor and 69% with a rabbit N-formyl peptide receptor. The receptor has a unique structure, including a short third intracellular loop and several serine and threonine residues that may function as phosphorylation sites. The receptor also contains acidic residues in the NH2-terminal extracellular region, which may be involved in binding to IL-8, a basic protein with a pI of ~9.5. The IL-8 receptor is a G protein-coupled receptor that activates intracellular calcium stores upon binding to IL-8. The receptor has a low affinity for IL-8 and is expressed in neutrophils and certain cell lines. The receptor also binds to structurally related ligands, including MGSA and NAP-2, with varying degrees of potency. The receptor is not activated by C5a, a structurally unrelated chemoattractant. The study also describes the genomic analysis of the IL-8 receptor, showing that it is encoded by a single gene in the human genome. The receptor is expressed in neutrophils and certain cell lines, but not in monocytes. The receptor shares less than 30% amino acid identity with other G protein-coupled receptors, including the human N-formyl peptide receptor. The study concludes that the IL-8 receptor is a functional receptor for IL-8 and is expressed in neutrophils and certain cell lines. The receptor has a unique structure and function, and its expression is regulated by specific mechanisms. The study also highlights the importance of the receptor in immune responses and the potential for further research into its function and regulation.