Essex D W, Chen K, Swiatkowska M
Department of Medicine, State University of New York, Health Science Center at Brooklyn 11203, USA.
Blood. 1995 Sep 15;86(6):2168-73.
Protein disulfide isomerase (PDI) is an enzyme that catalyzes the formation as well as the isomerization of disulfide bonds. In this study, antibodies against PDI were used to show PDI antigen on the platelet surface by indirect immunofluorescence microscopy and by flow cytometry. The platelets were not activated, as evidenced by the absence of staining by an antibody against P-selectin. Permeabilized platelets showed little cytosolic PDI by indirect immunofluorescence microscopy, suggesting that the majority of platelet PDI is localized to the platelet surface. PDI activity against "scrambled" RNase was shown with intact platelets. The activity was inhibited by inhibitors of PDI and by an antibody against PDI. Other blood cells showed little PDI. Platelet surface PDI may play a role in the various physiological and pathophysiologic processes in which platelets are involved.
蛋白质二硫键异构酶（PDI）是一种催化二硫键形成及异构化的酶。在本研究中，通过间接免疫荧光显微镜和流式细胞术，使用抗PDI抗体来显示血小板表面的PDI抗原。血小板未被激活，这可通过抗P-选择素抗体染色缺失得到证明。经透化处理的血小板通过间接免疫荧光显微镜显示出很少的胞质PDI，这表明血小板中的大多数PDI定位于血小板表面。完整血小板显示出针对“杂乱”核糖核酸酶的PDI活性。该活性被PDI抑制剂和抗PDI抗体所抑制。其他血细胞显示出很少的PDI。血小板表面PDI可能在血小板参与的各种生理和病理生理过程中发挥作用。
