Evidence for specific annexin I-binding proteins on human monocytes
Evidence for specific annexin I-binding proteins on human monocytes
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DOI：
10.1042/bj3160593
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发表时间：
1996-06-01
影响因子：
4.1
通讯作者：
Guyre, PM
中科院分区：
文献类型：
--
作者：
Goulding, NJ;Pan, LY;Guyre, PM
利用重组人膜联蛋白I和该蛋白特异性单克隆抗体（mAb 1B）研究了该膜联蛋白家族成员与外周血单核细胞的表面结合。流式细胞术分析显示，膜联蛋白I对胰蛋白酶敏感，可与人外周血单核细胞饱和结合，但不与受欢迎的淋巴细胞结合。单克隆抗体阻断了膜联蛋白I的抗磷脂酶活性，也阻断了其与单核细胞的结合，这些发现表明单核细胞上存在特异性的结合位点。此外，利用表面碘化、免疫沉淀和SDS/PAGE分析鉴定了两个膜联蛋白I结合蛋白在单核细胞表面，分子质量分别为15 kDa和18 kDa。这些膜联蛋白I结合分子的鉴定和表征将有助于我们更好地理解膜联蛋白I与单核细胞的特异性相互作用，从而导致促炎细胞功能的下调。
Recombinant human annexin I and a monoclonal antibody specific for this protein (mAb 1B) were used to investigate surface binding of this member of the annexin family of proteins to peripheral blood monocytes, Flow cytometric analysis demonstrated trypsin-sensitive, saturable binding of annexin I to human peripheral blood monocytes but not to admired lymphocytes. A monoclonal antibody that blocks the anti-phospholipase activity of annexin I also blocked its binding to monocytes, These findings suggest the presence of specific binding sites on monocytes, Furthermore, surface iodination, immunoprecipitation and SDS/PAGE analysis were used to identify two annexin I-binding proteins on the surface of monocytes with molecular masses of 15 kDa and 18 kDa respectively. The identification and characterization of these annexin I-binding molecules should help us to better understand the specific interactions of annexin I with monocytes that lead to down-regulation of pro-inflammatory cell functions.