Involvement of fibrinogen specific binding in erythrocyte aggregation
Involvement of fibrinogen specific binding in erythrocyte aggregation
复制标题
DOI：
10.1016/s0014-5793(02)02575-9
复制
发表时间：
2002-04-24
期刊：
影响因子：
3.5
通讯作者：
Dean, WL
中科院分区：
文献类型：
--
作者：
Lominadze, D;Dean, WL
纤维蛋白原浓度升高和红细胞聚集是各种心脑血管疾病的重要危险因素。目前，纤维蛋白原诱导的红细胞聚集被认为是由非特异性结合机制引起的。然而，已发表的关于高血压期间红细胞聚集变化的数据表明可能存在其他机制。因此，我们测试的假设，纤维蛋白原的特异性结合参与红细胞聚集。发现俄勒冈州绿色488标记的人纤维蛋白原特异性结合大鼠红细胞膜，K-d为1.3 μ M。进一步的实验表明，肽Arg-Gly-Asp-Ser阻断纤维蛋白原诱导的完整红细胞聚集和纤维蛋白原与红细胞膜的特异性结合。这些结果表明，除了非特异性结合，特异性结合机制也参与纤维蛋白原诱导的红细胞聚集。(C)2002年欧洲生物化学学会联合会。由Elsevier Science B. V.出版，版权所有。
Increased fibrinogen concentration and erythrocyte aggregation are significant risk factors during various cardiovascular diseases and cerebrovascular disorders. Currently, fibrinogen-induced erythrocyte aggregation is thought to be caused by a non-specific binding mechanism. However, the published data on changes in erythrocyte aggregation during hypertension point to the possible existence of other mechanism(s). Therefore, we tested the hypothesis that specific binding of fibrinogen is involved in erythrocyte aggregation. It was found that Oregon Green 488-labeled human fibrinogen specifically binds rat erythrocyte membranes with a K-d of 1.3 muM. Further experiments showed that the peptide Arg-Gly-Asp-Ser blocked both fibrinogen-induced aggregation of intact erythrocytes and specific binding of fibrinogen to the erythrocyte membranes. These results suggest that in addition to non-specific binding, a specific binding mechanism is also involved in fibrinogen-induced erythrocyte aggregation. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.