Isolation and partial characterization of the formyl peptide receptor components on human neutrophils.
Isolation and partial characterization of the formyl peptide receptor components on human neutrophils.
复制标题
人中性粒细胞上甲酰基肽受体成分的分离和部分表征。
DOI：
10.1016/0006-291x(91)90488-s
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发表时间：
1991
影响因子：
3.1
通讯作者：
Genco,RJ
中科院分区：
文献类型：
--
作者：
DeNardin,E;Radel,SJ;Genco,RJ
据报道，甲酰化肽（如FMLP）的受体由糖蛋白成分组成，范围从24-95 kDa不等，并且对配体具有高亲和力和低亲和力。这些成分的分子大小和数量以及不同的亲和力是否代表不同的配体结合位点存在争议。在本研究中，发现该受体由分子大小为94,68和≈40 kDa的组分组成。竞争性结合抑制实验表明，FMLP与各组分的结合亲和力由高到低依次为：68 kDa >≈40 kDa > 94 kDa。我们的研究结果表明，人中性粒细胞的FMLP受体至少包含三种成分，每种成分对FMLP具有不同的亲和力。
The receptor for formylated peptides such as FMLP has been reported to consist of glycoprotein components ranging from 24–95 kDa, and to exhibit both high and low affinity for ligand. Controversy exists on the molecular size and number of these components, and whether the different affinities represent distinct ligand binding sites. In this study, the receptor was found to be comprised of components, of 94, 68, and ≈40 kDa molecular size. Competitive binding inhibition experiments showed that FMLP bound to the components in the following order from highest to lowest affinity: 68 kDa > ≈40 kDa > 94 kDa. Our findings suggest that the FMLP receptor of human neutrophils contains at least three components, and that each component has a different affinity for FMLP.