A structural homologue of the N-formyl peptide receptor. Characterization and chromosome mapping of a peptide chemoattractant receptor family.
A structural homologue of the N-formyl peptide receptor. Characterization and chromosome mapping of a peptide chemoattractant receptor family.
复制标题
DOI：
10.1016/s0021-9258(18)42563-x
复制
发表时间：
1992-04
期刊：
影响因子：
--
通讯作者：
P. Murphy;Tayfun Ozgelikn;Richard T. KenneyS;H. Tiffany;David H. McDermott;Uta Francken
中科院分区：
文献类型：
--
作者：
P. Murphy;Tayfun Ozgelikn;Richard T. KenneyS;H. Tiffany;David H. McDermott;Uta Francken
许多高等物种的吞噬细胞表达细菌 N-甲酰肽的钙动员 G 蛋白偶联受体，介导趋化性、脱颗粒和呼吸爆发。编码 N-甲酰肽受体 (FPR) 的 cDNA 已被报道。我们现在报告了一个密切相关的 cDNA 的分离，长度为 2.6 KB，我们将其命名为 FPRL1 受体 cDNA（FPRL1 = 甲酰基肽受体样-1）。 FPR 和 FPRL1 受体源自小型单拷贝基因，两者均位于人类 19 号染色体上。基因位点分别指定为 FPR1 和 FPRL1。 FPR 和 FPRL1 cDNA 在高严格条件下与第三个基因（称为 FPRL2）交叉杂交，该基因似乎不在中性粒细胞中表达。相比之下，FPRL1 受体和 FPR 的转录物仅在分化的骨髓细胞中检测到。 N-甲酰肽结合位点的分布也仅限于成熟的骨髓细胞。 FPRL1 cDNA编码351个氨基酸的多肽，其序列与FPR的序列有69%相同。表现出这种程度的结构相似性的G蛋白偶联受体通常具有保守的配体特异性。然而，当在异源细胞类型中表达时，FPRL1 受体不结合原型 N-甲酰基肽配体。这些结果表明FPR1可能是中性粒细胞表达的唯一基因，其编码能够结合原型N-甲酰基肽的受体。此外，FPRL1 受体的发现表明存在另一种尚未鉴定的肽，它可能会将中性粒细胞募集到炎症部位。
Phagocytic cells of many higher species express calcium mobilizing G protein-coupled receptors for bacterial N-formyl peptides which mediate chemotaxis, degranulation, and the respiratory burst. cDNA encoding an N-formyl peptide receptor (FPR) has been reported. We now report the isolation of a closely related cDNA, 2.6 kilobase pairs in length, which we have designated as the FPRL1 receptor cDNA (FPRL1 = formyl peptide receptor like-1). FPR and the FPRL1 receptor derive from small, single-copy genes, both of which are located on human chromosome 19. The gene loci are designated FPR1 and FPRL1, respectively. Both FPR and FPRL1 cDNA cross-hybridize under high stringency conditions with a third gene, designated as FPRL2, which does not appear to be expressed in neutrophils. In contrast, transcripts for both the FPRL1 receptor and FPR are detected only in differentiated myeloid cells; the distribution of N-formyl peptide binding sites is also restricted to mature myeloid cells. FPRL1 cDNA encodes a 351-amino acid polypeptide whose sequence is 69% identical to that of FPR. G protein-coupled receptors that exhibit this degree of structural similarity typically possess a conserved ligand specificity. However, the FPRL1 receptor does not bind prototype N-formyl peptide ligands when expressed in heterologous cell types. These results suggest that FPR1 may be the only gene that is expressed by neutrophils that encodes a receptor capable of binding prototype N-formyl peptides. Moreover, discovery of the FPRL1 receptor indicates the existence of another as yet unidentified peptide that may recruit neutrophils to sites of inflammation.