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人胎盘绒毛膜上皮刷状缘膜囊泡的血小板聚集抑制活性

Platelet aggregation inhibiting activity of human placental chorioepithelial brush border membrane vesicles.

作者信息

Iioka H, Akada S, Shimamoto T, Yamada Y, Sakamoto Y, Moriyama S I, Ichijo M

机构信息

Department of Obstetrics and Gynecology, Nara Medical University, Japan.

出版信息

Placenta. 1993 Jan-Feb;14(1):75-83. doi: 10.1016/s0143-4004(05)80250-4.

DOI:10.1016/s0143-4004(05)80250-4
PMID:8456091
Abstract

We investigated the platelet aggregation inhibiting activity of human placental brush border membrane vesicles (BBMV) and obtained the following results. A strong platelet aggregation inhibiting activity existed in placental BBMV. The BBMV inhibited the platelet aggregation induced by ADP, arachidonic acid, collagen and ristocetin in a dose-dependent manner. The protein concentration of BBMV giving 50 per cent inhibition was 52 +/- 6 micrograms/ml for ADP-induced platelet aggregation, 21 +/- 2 micrograms/ml for arachidonic acid-induced platelet aggregation, 19 +/- 2 micrograms/ml for collagen-induced platelet aggregation and 107 +/- 9 micrograms/ml for ristocetin-induced platelet aggregation. There was a high level of ADP degrading activity (ADPase activity) in the placental BBMV. ADP degrading activity of the BBMV: 10.5 +/- 0.5 mumol/mg protein/min was 21 times greater than that of homogenate of the placental villi. The placental BBMV inhibited platelet TXA2 production. In the 40 micrograms/ml protein concentration of placental BBMV, platelet TXA2 production was almost completely inhibited.

摘要

我们研究了人胎盘刷状缘膜囊泡(BBMV)的血小板聚集抑制活性,并获得了以下结果。胎盘BBMV存在较强的血小板聚集抑制活性。BBMV以剂量依赖的方式抑制由ADP、花生四烯酸、胶原和瑞斯托霉素诱导的血小板聚集。对于ADP诱导的血小板聚集,产生50%抑制作用的BBMV蛋白浓度为52±6微克/毫升;对于花生四烯酸诱导的血小板聚集为21±2微克/毫升;对于胶原诱导的血小板聚集为19±2微克/毫升;对于瑞斯托霉素诱导的血小板聚集为107±9微克/毫升。胎盘BBMV中存在高水平的ADP降解活性(ADP酶活性)。BBMV的ADP降解活性:10.5±0.5微摩尔/毫克蛋白/分钟,是胎盘绒毛匀浆的21倍。胎盘BBMV抑制血小板TXA2的产生。在胎盘BBMV蛋白浓度为40微克/毫升时,血小板TXA2的产生几乎被完全抑制。

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Platelet aggregation inhibiting activity of human placental chorioepithelial brush border membrane vesicles.人胎盘绒毛膜上皮刷状缘膜囊泡的血小板聚集抑制活性
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PLoS One. 2015 Nov 9;10(11):e0142538. doi: 10.1371/journal.pone.0142538. eCollection 2015.