CHARACTERIZATION OF PROTEIN DISULFIDE-ISOMERASE RELEASED FROM ACTIVATED PLATELETS
CHARACTERIZATION OF PROTEIN DISULFIDE-ISOMERASE RELEASED FROM ACTIVATED PLATELETS
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DOI：
10.1111/j.1365-2141.1995.tb05169.x
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发表时间：
1995-06-01
影响因子：
6.5
通讯作者：
ESSEX, DW
中科院分区：
文献类型：
--
作者：
CHEN, K;DETWILER, TC;ESSEX, DW
活化的血小板释放蛋白质二硫化物异构酶（PDI）活性。在本研究中，从血小板纯化PDI，发现其表观质量、pi和N-末端序列与其他人PDI相似。产生兔抗体并用于确定，在活化时，血小板释放免疫学上与PDI相同的蛋白质：在血小板中，约10%的总血小板PDI由凝血酶释放，20%由钙离子载体释放。该抗体用于通过电子显微镜证实血小板外表面上的PDI。流式细胞术用于证明，在用离子载体活化血小板后，PDI通过囊泡化释放。由于血小板存在并在血管损伤部位活化，血小板PDI可能在血小板参与的各种止血和组织重塑过程中发挥作用。
Protein disulphide isomerase (PDI) activity is released by activated platelets, Ln this study, PDI was purified from platelets and found to have an apparent mass, pi and N-terminal sequence similar to those for other human PDIs. Rabbit antibodies were generated and used to establish that, on activation, platelets release a protein immunologically identical to PDI: in platelets, Approximately 10% of total platelet PDI was released by thrombin and 20% by calcium ionophore, The antibody was used to demonstrate PDI on the external surface of platelets by electron microscopy. Flow cytometry was used to demonstrate that upon activation of platelets with ionophore PDI was released by vesiculation. Since platelets are present and become activated at sites of vascular injury, platelet PDI may play a role in the various haemostatic and tissue remodelling processes in which platelets are involved.