Comparison of Fibrinogen Association With Normal and Thrombasthenic Platelets on Exposure to ADP or Chymotrypsin
Comparison of Fibrinogen Association With Normal and Thrombasthenic Platelets on Exposure to ADP or Chymotrypsin
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暴露于 ADP 或胰凝乳蛋白酶后纤维蛋白原与正常血小板和凝血无力的血小板关联的比较
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发表时间：
1979
期刊：
影响因子：
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通讯作者：
K. Pai
中科院分区：
文献类型：
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作者：
J. Mustard;R. Kinlough;M. Packham;D. Perry;E. Harfenist;K. Pai
降解血小板膜糖蛋白。泰恩斯。虽然洗涤的人血小板在悬浮介质中没有纤维蛋白原的情况下会因二磷酸腺苷而改变形状，但除非有纤维蛋白原存在，否则它们不会聚集。�9最近研究表明，在腺苷二磷酸诱导的形状改变和聚集过程中，纤维蛋白原与人的血小板相关；当血小板解聚时，纤维蛋白原就会丢失。9血栓形成的血小板在��p2�4的反应下会改变形状，但不会聚集，并且已经被证明其膜糖蛋白II和IIl有异常。��“一些研究人员的8 22报告说，与正常的血小板相比，与血栓形成有关的纤维蛋白原较少。在这项研究中，我们研究了血小板功能缺陷可能是由于暴露于ADP后不能与纤维蛋白原相关。二磷酸腺苷和牛腱胶原来自密苏里州圣路易斯的Sigma Chemical Company；来自新泽西州弗里霍尔德的沃辛顿生化公司的胰凝乳蛋白酶；以及来自密歇根州底特律的Parke Davis and Co.的牛凝血酶。所有溶质均溶于0.85%生理盐水或改良泰氏液(不含钙或镁)。23人纤维蛋白原(L，Kabi级)用二异丙基氟磷酸盐(DFP，Sigma)处理以灭活任何促凝剂材料。24纤维蛋白原用251(amersham/Searle)标记。阿灵顿高地，III。)用单氯化碘。25测得~(25)I-荧光素制剂的比放射性为33,312 cpm/.lg。当纤维蛋白原凝结时
to degrade platelet membrane glycopro- them. teins. More 1261-fibrinogen became assoA LTHOUGH washed human platelets change shape in response to adenosine diphosphate (ADP) in the absence of fibrinogen in the suspending medium, they do not aggregate unless fibrinogen is present.’�9 It has recently been shown that ‘251-fibrinogen becomes associated with human platelets during ADP-induced shape change and aggregation;9” the fibrinogen is lost when the platelets deaggregate.9 Thrombasthenic platelets change shape but do not aggregate in response to ��p2�4 and have been shown to have abnormalities of their membrane glycoproteins II and IIl.�� “ Several investigators’8 22 have reported that less fibrinogen is associated with thrombasthenic platelets than with normal platelets. In this study, we have investigated the possibility that the functional defect of thrombasthenic platelets may be an inability to become associated with fibrinogen upon exposure to ADP. Adenosine diphosphate and bovine tendon collagen were obtained from Sigma Chemical Company, St. Louis, Mo.; chymotrypsin from Worthington Biochemical Corp., Freehold, N.J.; and bovine thrombin from Parke Davis and Co., Detroit, Mich. All solutes were dissolved in either 0.85% saline solution or modified Tyrode solution (no calcium or magnesium). Suspensions of finely divided collagen were prepared as previously described.23 Human fibrinogen (Grade L, Kabi) was treated with diisopropylfluorophosphate (DFP, Sigma) to inactivate any procoagulant material.24 Fibrinogen was labeled with 251 (Amersham/Searle. Arlington Heights, III.) using iodine monochloride.25 The specific radioactivity of the ‘25I-flbrinogen preparation was 33,312 cpm/.Lg. When this fibrinogen was clotted