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    Biochem Biophys Res Commun. 1992 Apr 30;184(2):582-9.

    Isolation of a cDNA that encodes a novel granulocyte N-formyl peptide receptor.

    Ye RD, Cavanagh SL, Quehenberger O, Prossnitz ER, Cochrane CG.

    Source

    Department of Immunology, Scripps Research Institute, La Jolla, CA 92037.

    Abstract

    A cDNA of 1650 base pairs was isolated by screening an HL-60 granulocyte library with an N-formyl peptide receptor (NFPR) cDNA probe under low stringency conditions. The cDNA encodes a protein of 351 amino acids tentatively named FPR2, with a calculated molecular weight of 39 kDa. Sequence analysis revealed that FPR2 is 69% identical in sequence to the human NFPR and shares extensive homology to several other chemoattractant receptors. FPR2 expressed in transfected cells mediated formyl peptide-stimulated calcium mobilization at micromolar concentrations of ligand. FPR2 messenger is detected in granulocytic HL-60 cells, but not in undifferentiated HL-60 cells. These findings suggest that FPR2 is a novel receptor for formyl peptide ligand and a new member of the chemoattractant receptor gene family.

    PMID:
    1374236
    [PubMed - indexed for MEDLINE]

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