{"title":"无标题的","authors":"G. Green, I. Dymock, L. Polzer","doi":"10.1515/9781618116673-009","DOIUrl":null,"url":null,"abstract":"s 921 Three radioactive peaks ( approx. MW 97.000, I 20.000 and I 50 .000) were seen on subsequent SDS polyacrylamide gel electrophoresis of control platelets. Treatment of prelabeled platelets with thrombin did not reveal any changes in the \" specific\" radioactivity of the three peaks, indicating that no labeled fragments had been split off. Treatment with thrombin before iodination under conditions where the release reaction occurred, resulted in a. drastic reduction in the incorporation of radioactivity. When the release reaction was inhibited by antimycin and 2-deoxyglucose before thrombin treatment and subsequent iodination, very little or no effect could be observed on the incorporation of radioactivity. Aggregation of these platelet suspensions with bovine factor VIII, and ristocetin plus human ristocetin cofactor indicate that platelets which have undergone the release reaction aggregate poorly with these agents. The membrane conformation necessary for iodination of the three membrane polypeptides and the ability of the platelets to aggregate in the facbor VIII -dependant systems thus seem to be altered during thrombin-induced release reaction, possibly because of alterations in the membrane structure. D. R. Phillips, 0 . S. P. Jenkins, D . Meyer, M .-J. Lan·ieu and E. F. Luscher (Theodor Kocher Institute, Bern, Switzerland, and Institut de Pathologic Cellulaire, H6pital de Bicetre, 94270 Le Kremlin-Bicetre, France): Platelet JUembrane Glycoproteins and their Possible Relationship to the ADP Mechanism of Platelet Aggregation. (451) Platelets isolated from patients with Glanzmann's Thrombasthenia release in the presence of thrombin and other stimuli but fail to respond to ADP. Since the intial interaction between the platelet and ADP is at the membrane surface, it would appear that this surface lacks the necessary receptor for ADP. The surface structure of normal and t,Juomhasthenic platelets was compared using the lactoperoxidase iodination technique. Iodination of normal platelets results in the labelling of four glycoproteins, I, II a IIb and III, with relative ratios of l : l : l : 3 plus other non-characterised polypeptides. Thrombasthenic platelets similarly treated revealed a drastically altered expression of the glycoproteins on the membrane. The relative ratios (1.5: l: 0.4 : 0.5) revealed the decrease of glycoprotein IIb and the marked reduction of glycoprotein III. Arguments and data will be presented which point to the possibility that glycoprotein IIb is involved in ADP-induced aggregation. S. Levy-Toledano, R. Bredoux, F . Rendu, G. Tobelem, L. Degas and J . P . Oaen (H6pital Saint-Louis, 2, pl. du Dr. Fournier, F 75475 Paris Cedex 10, France): Specificity of an Acquired Antiplatelet Antibody OccUl'ing in a Polytransfused Thrombasthenic Patient . ( 452) An IgG antibody which developed in a polytransfused thrombasthenic patient reacted in cumplement fixation with platelets from 350 normal individuals but not with platelets from 8 other thrombasthenic patients. It agglutinates human platelets in PRP but not thrombasthenic platelets. This agglutination increased if the PRP >vas preincubated at 37° C or if the platelets were isolated before the additi on of the antibody. Dog but not rabbit platelets are agglutinated by the patient plasma. Neither adenosine, nor PGE l inhibit this agglutination which is slightly reduced by acatylsalicilic acid and disappears with EDTA and EGTA (3,8 mM). Its activity is reduced or abolished after incubation with control platelet membranes but not with those obtained from thrombasthenic or rabbit platelets. It does not inhibit the ADP-induced shape change of normal platelets, and it prevents all the ADP mediated platelet aggregations but not those induced by bovine factor VIII and ristocetin. This antibody seemed to be directed against a molecule absent or structurally modified in thrombasthenic platelets which would be involved in platelet aggregation and more especiall y in ADP mediated platelet aggregation. T hi s do cu m en t w as d ow nl oa de d fo r pe rs on al u se o nl y. U na ut ho riz ed d is tr ib ut io n is s tr ic tly p ro hi bi te d.","PeriodicalId":296417,"journal":{"name":"Words for War","volume":"140 1","pages":"0"},"PeriodicalIF":0.0000,"publicationDate":"2019-12-31","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Untitled\",\"authors\":\"G. Green, I. Dymock, L. Polzer\",\"doi\":\"10.1515/9781618116673-009\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"s 921 Three radioactive peaks ( approx. MW 97.000, I 20.000 and I 50 .000) were seen on subsequent SDS polyacrylamide gel electrophoresis of control platelets. Treatment of prelabeled platelets with thrombin did not reveal any changes in the \\\" specific\\\" radioactivity of the three peaks, indicating that no labeled fragments had been split off. Treatment with thrombin before iodination under conditions where the release reaction occurred, resulted in a. drastic reduction in the incorporation of radioactivity. When the release reaction was inhibited by antimycin and 2-deoxyglucose before thrombin treatment and subsequent iodination, very little or no effect could be observed on the incorporation of radioactivity. Aggregation of these platelet suspensions with bovine factor VIII, and ristocetin plus human ristocetin cofactor indicate that platelets which have undergone the release reaction aggregate poorly with these agents. The membrane conformation necessary for iodination of the three membrane polypeptides and the ability of the platelets to aggregate in the facbor VIII -dependant systems thus seem to be altered during thrombin-induced release reaction, possibly because of alterations in the membrane structure. D. R. Phillips, 0 . S. P. Jenkins, D . Meyer, M .-J. Lan·ieu and E. F. Luscher (Theodor Kocher Institute, Bern, Switzerland, and Institut de Pathologic Cellulaire, H6pital de Bicetre, 94270 Le Kremlin-Bicetre, France): Platelet JUembrane Glycoproteins and their Possible Relationship to the ADP Mechanism of Platelet Aggregation. (451) Platelets isolated from patients with Glanzmann's Thrombasthenia release in the presence of thrombin and other stimuli but fail to respond to ADP. Since the intial interaction between the platelet and ADP is at the membrane surface, it would appear that this surface lacks the necessary receptor for ADP. The surface structure of normal and t,Juomhasthenic platelets was compared using the lactoperoxidase iodination technique. Iodination of normal platelets results in the labelling of four glycoproteins, I, II a IIb and III, with relative ratios of l : l : l : 3 plus other non-characterised polypeptides. Thrombasthenic platelets similarly treated revealed a drastically altered expression of the glycoproteins on the membrane. The relative ratios (1.5: l: 0.4 : 0.5) revealed the decrease of glycoprotein IIb and the marked reduction of glycoprotein III. Arguments and data will be presented which point to the possibility that glycoprotein IIb is involved in ADP-induced aggregation. S. Levy-Toledano, R. Bredoux, F . Rendu, G. Tobelem, L. Degas and J . P . Oaen (H6pital Saint-Louis, 2, pl. du Dr. Fournier, F 75475 Paris Cedex 10, France): Specificity of an Acquired Antiplatelet Antibody OccUl'ing in a Polytransfused Thrombasthenic Patient . ( 452) An IgG antibody which developed in a polytransfused thrombasthenic patient reacted in cumplement fixation with platelets from 350 normal individuals but not with platelets from 8 other thrombasthenic patients. It agglutinates human platelets in PRP but not thrombasthenic platelets. This agglutination increased if the PRP >vas preincubated at 37° C or if the platelets were isolated before the additi on of the antibody. Dog but not rabbit platelets are agglutinated by the patient plasma. Neither adenosine, nor PGE l inhibit this agglutination which is slightly reduced by acatylsalicilic acid and disappears with EDTA and EGTA (3,8 mM). Its activity is reduced or abolished after incubation with control platelet membranes but not with those obtained from thrombasthenic or rabbit platelets. It does not inhibit the ADP-induced shape change of normal platelets, and it prevents all the ADP mediated platelet aggregations but not those induced by bovine factor VIII and ristocetin. This antibody seemed to be directed against a molecule absent or structurally modified in thrombasthenic platelets which would be involved in platelet aggregation and more especiall y in ADP mediated platelet aggregation. T hi s do cu m en t w as d ow nl oa de d fo r pe rs on al u se o nl y. U na ut ho riz ed d is tr ib ut io n is s tr ic tly p ro hi bi te d.\",\"PeriodicalId\":296417,\"journal\":{\"name\":\"Words for War\",\"volume\":\"140 1\",\"pages\":\"0\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2019-12-31\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Words for War\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1515/9781618116673-009\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Words for War","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1515/9781618116673-009","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 0
摘要
s 921三个放射性峰(大约)。在随后的对照血小板SDS聚丙烯酰胺凝胶电泳中观察到mw9.7 000、i20.000和i50.000)。用凝血酶处理预先标记的血小板时,没有发现三个峰的“特异性”放射性有任何变化,这表明没有标记的碎片被分离。在发生释放反应的条件下,在碘化前用凝血酶治疗,导致放射性掺入的急剧减少。当抗霉素和2-脱氧葡萄糖在凝血酶治疗前和随后的碘化处理抑制释放反应时,对放射性的掺入几乎没有影响。这些血小板悬浮液与牛凝血因子VIII和利斯托斯汀加人利斯托斯汀辅因子的聚集表明,经历了释放反应的血小板与这些药物的聚集很差。因此,三种膜多肽碘化所必需的膜构象和血小板在因子VIII依赖系统中聚集的能力似乎在凝血酶诱导的释放反应中被改变,可能是由于膜结构的改变。菲利普斯博士,0岁。詹金斯博士。迈耶,m.j.。Lan·ieu和e.f. Luscher (Theodor Kocher Institute, Bern, Switzerland, and Institut de Pathologic cellaire, h6ital de Bicetre, 94270 Le Kremlin-Bicetre, France):血小板jumembrane糖蛋白及其与血小板聚集ADP机制的可能关系。(451)从Glanzmann血栓减少症患者分离的血小板在凝血酶和其他刺激下释放,但对ADP没有反应。由于血小板和ADP之间的初始相互作用是在膜表面,因此表面似乎缺乏ADP所需的受体。采用乳酸过氧化物酶碘化技术对正常血小板和巨噬细胞血小板的表面结构进行了比较。正常血小板的碘化导致四种糖蛋白标记,I, II, a, IIb和III,其相对比例为1:1:1:1:3加上其他非特征多肽。类似处理的血栓性血小板显示膜上糖蛋白的表达急剧改变。相对比值(1.5:1:0.4:0.5)显示糖蛋白IIb降低,糖蛋白III明显降低。将提出的论据和数据表明,糖蛋白IIb可能参与adp诱导的聚集。S. Levy-Toledano, R. Bredoux, F。Rendu, G. Tobelem, L. Degas和J。P。Oaen (h6ital Saint-Louis, 2, pl. du Dr. Fournier, F 75475 Paris Cedex 10, France):获得性抗血小板抗体在多次输血血栓减少患者中的特异性。(452)在多次输血的血栓患者中产生的IgG抗体与350名正常人的血小板互补固定反应,但与其他8名血栓患者的血小板不反应。它能凝集PRP中的人血小板,但不能凝集血栓性血小板。如果在37°C预孵育PRP >,或者在添加抗体之前分离血小板,则这种凝集会增加。狗的血小板可被患者血浆凝集,而不是兔的。腺苷和pge1都不能抑制这种凝集,这种凝集被乙酰水杨酸轻微减少,并与EDTA和EGTA一起消失(3,8 mM)。与对照血小板膜孵育后,其活性降低或消失,但与从血栓性血小板或兔血小板获得的膜孵育后,其活性不会降低或消失。对ADP诱导的正常血小板形态改变无抑制作用,对ADP介导的血小板聚集均有抑制作用,但对牛因子VIII和雷斯托霉素诱导的血小板聚集无抑制作用。该抗体似乎针对血栓性血小板中缺失或结构修饰的分子,该分子可能参与血小板聚集,特别是ADP介导的血小板聚集。这是一种很好的方法,它可以使你的身体变得更健康,你可以使你的身体变得更健康,你可以使你的身体变得更健康。
s 921 Three radioactive peaks ( approx. MW 97.000, I 20.000 and I 50 .000) were seen on subsequent SDS polyacrylamide gel electrophoresis of control platelets. Treatment of prelabeled platelets with thrombin did not reveal any changes in the " specific" radioactivity of the three peaks, indicating that no labeled fragments had been split off. Treatment with thrombin before iodination under conditions where the release reaction occurred, resulted in a. drastic reduction in the incorporation of radioactivity. When the release reaction was inhibited by antimycin and 2-deoxyglucose before thrombin treatment and subsequent iodination, very little or no effect could be observed on the incorporation of radioactivity. Aggregation of these platelet suspensions with bovine factor VIII, and ristocetin plus human ristocetin cofactor indicate that platelets which have undergone the release reaction aggregate poorly with these agents. The membrane conformation necessary for iodination of the three membrane polypeptides and the ability of the platelets to aggregate in the facbor VIII -dependant systems thus seem to be altered during thrombin-induced release reaction, possibly because of alterations in the membrane structure. D. R. Phillips, 0 . S. P. Jenkins, D . Meyer, M .-J. Lan·ieu and E. F. Luscher (Theodor Kocher Institute, Bern, Switzerland, and Institut de Pathologic Cellulaire, H6pital de Bicetre, 94270 Le Kremlin-Bicetre, France): Platelet JUembrane Glycoproteins and their Possible Relationship to the ADP Mechanism of Platelet Aggregation. (451) Platelets isolated from patients with Glanzmann's Thrombasthenia release in the presence of thrombin and other stimuli but fail to respond to ADP. Since the intial interaction between the platelet and ADP is at the membrane surface, it would appear that this surface lacks the necessary receptor for ADP. The surface structure of normal and t,Juomhasthenic platelets was compared using the lactoperoxidase iodination technique. Iodination of normal platelets results in the labelling of four glycoproteins, I, II a IIb and III, with relative ratios of l : l : l : 3 plus other non-characterised polypeptides. Thrombasthenic platelets similarly treated revealed a drastically altered expression of the glycoproteins on the membrane. The relative ratios (1.5: l: 0.4 : 0.5) revealed the decrease of glycoprotein IIb and the marked reduction of glycoprotein III. Arguments and data will be presented which point to the possibility that glycoprotein IIb is involved in ADP-induced aggregation. S. Levy-Toledano, R. Bredoux, F . Rendu, G. Tobelem, L. Degas and J . P . Oaen (H6pital Saint-Louis, 2, pl. du Dr. Fournier, F 75475 Paris Cedex 10, France): Specificity of an Acquired Antiplatelet Antibody OccUl'ing in a Polytransfused Thrombasthenic Patient . ( 452) An IgG antibody which developed in a polytransfused thrombasthenic patient reacted in cumplement fixation with platelets from 350 normal individuals but not with platelets from 8 other thrombasthenic patients. It agglutinates human platelets in PRP but not thrombasthenic platelets. This agglutination increased if the PRP >vas preincubated at 37° C or if the platelets were isolated before the additi on of the antibody. Dog but not rabbit platelets are agglutinated by the patient plasma. Neither adenosine, nor PGE l inhibit this agglutination which is slightly reduced by acatylsalicilic acid and disappears with EDTA and EGTA (3,8 mM). Its activity is reduced or abolished after incubation with control platelet membranes but not with those obtained from thrombasthenic or rabbit platelets. It does not inhibit the ADP-induced shape change of normal platelets, and it prevents all the ADP mediated platelet aggregations but not those induced by bovine factor VIII and ristocetin. This antibody seemed to be directed against a molecule absent or structurally modified in thrombasthenic platelets which would be involved in platelet aggregation and more especiall y in ADP mediated platelet aggregation. T hi s do cu m en t w as d ow nl oa de d fo r pe rs on al u se o nl y. U na ut ho riz ed d is tr ib ut io n is s tr ic tly p ro hi bi te d.