脑梗死血浆F1+2水平与低分子肝素和噻氯匹定治疗的关系

目的　研究急性脑梗死治疗过程中凝血酶原片段 1+ 2 (F1+ 2 )的变化。方法　连续收集 39例急性脑梗死病例 ,17例用低分子肝素 (LMWH) ,12例用噻氯匹定 ,10例为其他治疗。以酶联免疫吸附双抗夹心法 (ELISA) ,测定发病 2 4h内以及治疗 10～14d时F1+ 2的血浆水平。结果　病例组治疗前、后与对照组比较 ,血浆F1+ 2 (2 80± 1 2 3,3 0 9± 1 80～ 1 0 2± 0 35mol/L ,均为P =0 0 0 0 )水平显著增高。二因素方差分析发现时间因素主效应 (P =0 0 0 0 0 )、治疗因素主效应 (P =0 0 0 9)、时间与治疗因素交互作用(P =0 0 0 2 )对F1+ 2水平均有显著影响。结论　急性脑梗死凝血功能的变化 ,以及LMWH和噻氯匹定治疗对凝血功能的干预 ,通过检测F1+ 2可以得到反映。     

围手术期卒中患者外周血vWF及ADAMTS13检测及临床意义

目的探讨v WF(血管性血友病因子)、ADAMTS13(血管性血友病因子裂解酶)在围手术期卒中的发生发展中所起的作用。方法收集围手术期内发生缺血性卒中的患者31例做为实验组,将实验组分为腔隙性梗死组、小面积梗死组以及大面积梗死组3个亚组。同时收集48例健康体检者做为对照组。采用酶联免疫吸附法(ELISA)检测v WF抗原、ADAMTS13抗原含量,应用残余胶原结合试验检测ADAMTS13的活性。结果 (1)实验组患者血浆中v WF抗原水平明显高于对照组(P<0.05),ADAMTS13活性水平及ADAMTS13抗原含量均明显低于对照组(P<0.05)。(2)实验组3个亚组的v WF抗原水平在大面积梗死组最高,腔隙性梗死组最低,大面积梗死组与腔隙性梗死组间差异有显著性(P<0.05)。(3)ADAMTS13抗原含量在大面积梗死组最低,腔隙性梗死组最高,3组间差异均具有显著性(均P<0.05),ADAMTS13活性水平在3组间差异无显著性(均P>0.05)。结论v WF及ADAMTS13参与了围手术期卒中的发生发展,ADAMTS13水平降低及v WF水平升高可能是围手术期卒中发生的危险因素。     

65例妇科恶性肿瘤合并2型糖尿病患者的围手术期护理

糖尿病患者接受盆扫根治性手术,容易加重糖尿病的各种并发症,也会大大增加盆扫术后的并发症.据统计,糖尿病患者接受外科手术,其手术并发症较非糖尿病患者高5倍左右[1].因此,做好围手术期护理,预防术后并发症是保证糖尿病患者行盆扫根治性手术成功的关键.2003-01～2008-01,我院为65例妇科恶性肿瘤合并2型糖尿病患者实施了盆扫根治术,现将有关护理报告如下.     

血栓弹力图在重型颅脑损伤患者围手术期的应用

目的 探讨血栓弹力图（TEG）在重型颅脑损伤患者围手术期的应用价值。方法 2014年10月1日~2015年8月1日急诊开颅血肿清除术治疗重症颅脑损伤患者78例,根据围手术期凝血功能监测方法分为TEG组（n=39）和经验治疗组（n=39）。TEG组测量反应时间（R值）、凝血形成时间（K值）、血栓最大幅度（Ma值）和凝固角（α值）等项参数,根据测量结果输注血液制品。经验治疗组则根据出血量及血气分析结果,按照经验疗法进行围手术期管理。结果 两组患者的手术时间无显著差异（P>0.05）;TEG组的出血量以及红细胞、新鲜冰冻血浆、冷沉淀、血小板输注量均较经验治疗组明显减少（P<0.01）;术后6、24 h引流量,teg组较经验治疗组均显著下降（P<0.01）;两组二次开颅手术率和30 d死亡率无明显差异（P>0.05）。结论 TEG可监测凝血功能,指导输血,减少血液制品输注量,减少术后颅内出血发生几率,在重型颅脑损伤患者围手术期具有重要的意义。     

对年轻的乳腺癌患者在围手术期的心理护理

目的探讨年轻的乳腺癌患者围手术期的最佳心理护理措施。方法把32例年轻的乳腺癌患者随机分成2组,对照组和实验组各16例。采用Zung氏焦虑自评量表(SAS)和抑郁自评量表(SDS)评估患者的心理状况。结果 2组患者入院时SAS和SDS测量评分差异无统计学意义(P>0.05)。经治疗后SAS和SDS测量评分有明显差异(P<0.01),试验组心理状况改善明显优于对照组。结论年轻的乳腺癌患者在围手术期表现出焦虑忧郁等不良心理,对其采取相应的心理护理,改善焦虑忧郁等不良心理,有助于使病人更加轻松地面对手术,给手术治疗及术后恢复带来更多的希望,并且病人出院后,敢于面对现实,以积极的心态迎接生活。     

重症肌无力患者围手术期的心理状态分析及护理

重症肌无力是一种依赖T细胞的乙酰胆碱受体抗体介导的自身免疫性疾病,严重威胁患者的健康,而且也给患者的心理产生严重的影响.加强围术期护理是保证手术安全,提高疗效和降低病死率的重要措施[1].2000-05～2006-10,我科对198例重症肌无力患者围手术期进行积极的心理护理,收到了满意的效果.     

心理和疼痛护理对宫颈癌患者围手术期睡眠质量的效果

目的探讨心理、疼痛联合护理干预模式对宫颈癌患者围手术期睡眠质量及预后影响。方法选取我院于2018年2月～2019年2月期间收治的98例宫颈癌患者作为研究对象,应用随机数字表抽取法分组,分别采取心理、疼痛联合护理干预模式方案(观察组,n=49)与采用常规护理方案(对照组,n=49)比较两组的疼痛控制满意度、自我护理能力评分、睡眠质量评分、细胞免疫相关指标。结果观察组疼痛控制满意度经评估为93.88%,高于对照组79.59%(P0.05);两组干预前,自我护理能力各维度即自我概念、自我护理技能、自护责任感、健康知识水平评分无差异(P0.05);干预后,各项评分经评定较前均有升高,观察组较对照组升高程度更为显著(P0.05);两组干预前,匹兹堡睡眠质量指数量表评分无差异(P0.05),干预后评分较前均有降低,观察组较对照组降低程度更为显著(P0.05);两组干预前,免疫指标NK细胞活性水平无差异(P0.05),干预后观察组无明显变化,对照组明显降低(P0.05)。结论宫颈癌患者围手术期重视心理、疼痛联合护理干预模式的实施,可提高患者疼痛控制满意度,增强自我护理水平,改善睡眠质量,调节机体免疫功能。     

急性缺血性脑卒中患者的血清UCP2,HIF-1α水平变化及其临床意义

目的 探讨急性缺血性脑卒中(Acute ischemic stroke, AIS)患者血清解偶联蛋白2(Uncoupling protein 2,UCP2)、缺氧诱导因子-1α(Hypoxia-inducible factor-1α,HIF-1α)水平变化及其临床意义。方法 选取123例AIS患者为研究对象(AIS组),以同期61例体检健康的人群为对照组;采用酶联免疫吸附法检测血清UCP2,HIF-1α水平;分析血清UCP2,HIF-1α水平与梗死面积、美国国立卫生研究院卒中量表(National institutes of health stroke scale, NIHSS)评分的关系;多因素Logistic回归分析影响AIS患者预后的因素;受试者工作曲线(Receiver operating curve, ROC)分析血清UCP2,HIF-1α水平单独及联合检测对AIS预后的预测价值。结果 AIS组血清UCP2水平明显低于对照组(P<0.05);AIS组血清HIF-1α水平明显高于对照组(P<0.05);不同梗死面积、NIHSS评分AIS患者血清UCP2、HIF-1α...     

加速康复外科在颅神经血管压迫综合征患者围手术期的应用

目的 探讨加速康复外科（ERAS）方案在颅神经血管压迫综合征（NVCS）患者围手术期应用的有效性和安全性。方法 将78例NVCS患者随机分为ERAS组（39例）和对照组（39例）,ERAS组采用ERAS管理方案,对照组采用神经外科常规围手术期管理方案。比较两组患者术后首次进食、首次下床活动、准备出院时间,疼痛、头晕、恶心呕吐、焦虑抑郁状况,术后并发症的发生率及术后恢复质量。结果 ERAS组术后恢复质量、术后疼痛、头晕、恶心呕吐、焦虑抑郁情况均优于对照组（P＜0.05);ERAS组术后首次进食、首次下床活动及准备出院时间均比对照组短（P＜0.05）;两组患者并发症的发生率比较,差异无统计学意义（P＞0.05）。结论 ERAS方案可以改善患者术后康复质量,加快其术后康复进程,同时不会增加术后并发症的发生率。国际神经病学神经外科学杂志, 2023, 50(3): 21-25]     

The effects of bovine prothrombin fragment 1 and fragment 1.2 on prothrombin activation

In this paper we describe the effects of the activation peptides prothrombin fragment 1 and fragment 1.2 on factor Xa-catalyzed prothrombin activation. Prothrombin activation in free solution by either factor Xa or factor Xa together with factor Va is unaffected by the activation fragments. When negatively charged phospholipids are present we observed considerable inhibition of prothrombin activation by both fragment 1 and fragment 1.2. For the activation of 0.25 microM prothrombin by factor Xa in the presence of 50 microM phospholipid (phosphatidylserine/phosphatidylcholine, 25/75; mol/mol) and 5 mM CaCl2 50% inhibition was obtained at 0.28 microM fragment 1 or fragment 1.2. Much higher fragment concentrations were required for 50% inhibition of a prothrombinase complex consisting of factor Xa, factor Va, Ca2+ and phospholipid. This shows that factor Va protects prothrombin activation against inhibition by its own activation peptides. Less inhibition by activation fragments was also observed at higher phospholipid and prothrombin concentrations or when the mole fraction phosphatidylserine in the phospholipid vesicles was decreased. The effects of fragment 1 and fragment 1.2 on prothrombin activation were identical throughout all experiments, indicating that the inhibition is due to the gamma-carboxyglutamic acid containing region of the activation peptides. Our observations suggest that the activation fragments inhibit prothrombin activation by competing with prothrombin and factor Xa for binding sites at the phospholipid surface. In such a model factor Va will protect against the inhibition since it is known to promote the assembly of the prothrombinase complex through interactions with factor Xa and prothrombin that are independent of the gla-residues. The kinetic properties of fragment inhibition also suggest that in vivo prothrombin activation will not be affected by the generation of activation peptides.     

Multicentric evaluation of a new assay for prothrombin fragment F1+2 determination.

A multicenter study of a recently developed ELISA for the determination of prothrombin fragment F1+2 was performed in order to evaluate analytical and clinical aspects. Mean intra-assay and inter-assay reproducibility were found to be 11.0 and 12.6%, respectively. The measuring range covered by the calibration curve reaches from 0.04 to 10.0 nM/l F1+2. Testing 133 healthy subjects a reference range of 0.37 to 1.11 nM/l F1+2 (2.5-97.5 percentile) with a median of 0.66 nM/l F1+2 was calculated. Minor difficulties with blood sampling (venous occlusion for 2 min) did not affect F1+2 plasma concentrations. Significantly increased F1+2 levels were measured in patients with leukemia (p < 0.0001), severe liver disease (p < 0.005) and after myocardial infarction (p < 0.01). Elevated F1+2 concentration before the beginning of heparin therapy (1.25 nM/l) decreased to 0.77 nM/l (p < 0.0001) after 1 day of therapy. For patients in the stable phase of oral anticoagulant therapy decreasing F1+2 concentrations were measured with increasing INR. F1+2 levels were already significantly reduced in patients with INR < 2.0 (0.56 nM/l; p = 0.0005). Thus F1+2 determination may be helpful in identifying activation processes as well as in monitoring anticoagulant therapy.     

Determination of human prothrombin activation fragment 1 + 2 in plasma with an antibody against a synthetic peptide

The present investigation describes a novel approach to prepare a specific antibody against prothrombin activation fragment 1 + 2 (F 1 + 2). The antibody discriminates between native prothrombin and F 1 + 2 in plasma. A synthetic peptide from the negatively charged region of F 1 + 2, which becomes the carboxy-terminal sequence after cleavage of prothrombin by factor Xa, was used for immunization of rabbits. Obtained antiserum was immunopurified and an enzyme-linked immunosorbent assay (ELISA) was constructed for determination of F 1 + 2. The test system follows the sandwich principle and uses two different antibodies directed against F 1 + 2 and prothrombin, respectively. The ELISA was calibrated with purified F 1 + 2 added to F 1 + 2-poor plasma. The lower limit of sensitivity of the assay was 0.02 nmol/l. Coefficients of variation of 6.9 to 10.4% (intraassay) and 6.7 to 11% (interassay) were found for F 1 + 2 concentrations between 0.08 and 4.9 nmol/l. A reference range from 0.32 to 1.2 nmol/l was calculated from 95 healthy donors (mean value +/- SD: 0.67 +/- 0.19 nmol/l). In patients with deep vein thrombosis (n = 7) confirmed by phlebography and in patients with pulmonary embolism (n = 8) confirmed by lung scan, F 1 + 2 levels were found up to 1.5 to 9.5 nmol/l. In plasma samples of patients under oral anticoagulant therapy in the stable state F 1 + 2 concentrations were found to be in the range of 0.08 to 0.5 nmol/l.(ABSTRACT TRUNCATED AT 250 WORDS)     

Influence of anticoagulants used for blood collection on plasma prothrombin fragment F1 + 2 measurements.

The levels of prothrombin fragment F₁₊₂ were measured by a double antibody radioimmunoassay in blood samples collected into different anticoagulant solutions. We evaluated healthy males between the ages of 42 and 77, asymptomatic patients with hereditary deficiencies of protein C or protein S, and persons receiving tumor necrosis factor infusions. The results in specimens collected in an anticoagulant containing ACD, EDTA, adenosine, and 25 U/ml of heparin (a) were highly correlated with those collected in an anticoagulant containing a synthetic thrombin inhibitor, EDTA, and aprotinin (b). However, in asymptomatic patients with congenital antithrombin III deficiency, we found that the plasma levels of F₁₊₂ in blood collected in anticoagulant (a) were usually substantially higher than those collected in anticoagulant (b). We determined that this phenomenon was not attributable to the venipuncture procedure itself, but rather appears to be due to the action of low concentrations of heparin in the presence of reduced blood levels of antithrombin III. Our data show that the previously documented elevations in plasma F₁₊₂ levels in patients with congenital antithrombin III deficiency appear to be caused by the above in vitro anticoagulant effect, and that this population does not exhibit evidence of a prethrombotic state as defined by the F₁₊₂ assay.     

D-Dimers, thrombin antithrombin III complexes and prothrombin fragments 1+2: diagnostic value in clinically suspected deep vein thrombosis

This study was performed to determine the accuracy of D-Dimer fibrin derivatives, thrombin-antithrombin III (TAT) complexes and prothrombin fragments 1 + 2 (F 1 + 2) determinations for the diagnosis of deep vein thrombosis (DVT). One hundred and sixteen consecutive patients referred to the angiology unit of our hospital for a clinically suspected DVT were investigated. They were submitted to mercury strain gauge plethysmography and to ultrasonic duplex scanning examination; in cases of inconclusive results or of proximal DVT (n = 35), an ascending phlebography was performed. After these investigations were completed, the diagnosis of DVT was confirmed in 34 and excluded in 82. One half of the patients were already under anticoagulant therapy at the time of investigation. The 3 biological markers were assayed using commercially available ELISA techniques and the D-Dimer was also assayed with a fast latex method. The normal distribution of these markers was established in 40 healthy blood donors. The most accurate assay for the diagnosis of DVT was the D-Dimer ELISA which had both a high sensitivity (94%) and a high negative predictive value (95%). The D-Dimer latex, TAT complexes and F 1 + 2 were far less sensitive and provided negative predictive values which ranged between 78 and 85%. In spite of positive and significant correlations between the levels of the 3 markers, their association did not improve their overall accuracy for detecting DVT. Therefore, with the exception of the D-Dimer ELISA, these markers were of little value for the diagnosis of DVT in this specific population.     

Gemfibrozil reduces plasma prothrombin fragment F1 + 2 concentration, a marker of coagulability, in patients with coronary heart disease.

The effects of gemfibrozil on several indices of haemostatic activity were explored in male patients with coronary heart disease (CHD). Sixty-three of 71 patients completed a crossover study in which gemfibrozil 1,200 mg/day and matching placebo were each taken in randomised order for 2 months in a double-blind manner, separated by a 2-month washout period. Serum cholesterol decreased by an average (95% confidence interval) of 12 (9 to 15)% and non-fasting triglyceride concentration by 43 (34 to 51)% during active treatment. Plasma prothrombin fragment F1 + 2 concentration, a marker of the in vivo rate of generation of thrombin, was 25 (12 to 37)% lower on average while on gemfibrozil than during the placebo phase. Factor VII coagulant activity (VIIc) and antigen concentration, and fibrinopeptide A concentration were not influenced by gemfibrozil in the group overall. However, the VIIc response appeared to be dependent upon the untreated cholesterol level. Hypercholesterolaemic men (cholesterol greater than 6.5 mmol/l) experienced a significant reduction in VIIc averaging 6% of standard during active therapy. Other effects of gemfibrozil were a 5 (2 to 9)% increase in plasma fibrinogen by a gravimetric method, an 11 (8 to 13)% increase in platelet count, and a 6 (2 to 10)% reduction in white cell count. The reduced incidence of CHD following gemfibrozil therapy in hyperlipidaemic patients may arise in part through a reduction in procoagulant activity and thus the risk of an occlusive coronary thrombosis.     

Expression of prothrombin fragment 1+2 in cancer tissue as an indicator of local activation of blood coagulation

Immunohistochemistry was applied to AMeX-fixed tissue sections of 12 adenocarcinomas of the stomach (seven intestinal adenocarcinomas and five diffuse carcinomas), 12 adenocarcinomas of the pancreas (nine ductal adenocarcinomas and three signet ring carcinomas), and 12 squamous cell carcinomas of the larynx obtained at surgical resection to examine the possibility of extravascular activation of blood coagulation in cancer tissues by exploring the in loco patterns of distribution of fibrinogen, a final product of blood coagulation, fibrin, and a by-product of coagulation reactions (prothrombin fragment 1+2). Gastric, pancreatic, and laryngeal cancers exhibited fibrinogen antigen in abundance throughout the tumor stroma. Fibrin was detected along the edges of nests of carcinoma cells and at the host-tumor interface. Prothrombin fragment 1+2 was present in the blood vessels in areas of neoangiogenesis at the host-tumor interface (gastric and pancreatic cancer tissues) and on the tumor cell bodies (pancreatic and laryngeal cancer tissues). The presence of prothrombin fragment 1+2 in cancer tissues appears to be a good indicator of coagulation activation and thrombin generation at the tumor burden.