LOCALIZATION OF PROTEIN DISULFIDE-ISOMERASE TO THE EXTERNAL SURFACE OF THE PLATELET PLASMA-MEMBRANE

LOCALIZATION OF PROTEIN DISULFIDE-ISOMERASE TO THE EXTERNAL SURFACE OF THE PLATELET PLASMA-MEMBRANE
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DOI:
10.1182/blood.v86.6.2168.bloodjournal8662168
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发表时间:
1995-09-15
期刊:
影响因子:
20.3
通讯作者:
SWIATKOWSKA, M
SWIATKOWSKA, M
中科院分区:
医学1区
文献类型:
--
作者:
ESSEX, DW;CHEN, K;SWIATKOWSKA, M

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蛋白质二硫键异构酶(PDI)是一种催化二硫键形成和异构化的酶。在这项研究中,针对PDI的抗体被用来显示血小板表面的PDI抗原通过间接免疫荧光显微镜和流式细胞术。血小板未被活化,如通过不存在针对P-选择素的抗体染色所证明的。通过间接免疫荧光显微镜观察,透化血小板的胞质PDI很小,表明大部分血小板PDI位于血小板表面。完整血小板显示出对“乱序”RNA酶的PDI活性。该活性被PDI的抑制剂和针对PDI的抗体抑制。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。(C)1995年,美国血液学会。
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. (C) 1995 by The American Society of Hematology.