China
Africa
Explore chapters and articles related to this topic
Critical Care and Anaesthesia
Published in Tjun Tang, Elizabeth O'Riordan, Stewart Walsh, Cracking the Intercollegiate General Surgery FRCS Viva, 2020
Rajkumar Rajendram, Alex Joseph, John Davidson, Avinash Gobindram, Prit Anand Singh, Animesh JK Patel
What are the natural anticoagulant mechanisms?Antithrombin inhibits thrombin, factor Xa and other activated clotting factors.Protein C pathway degrades and inactivates factors Va and VIIIa, thereby blocking thrombin generation.Tissue factor pathway inhibitor inactivates Xa and VIIa.Plasmin causes fibrinolysis by degrading fibrin into fibrin degradation products. It also inactivates Va and VIIIa and disrupts platelet function. Plasminogen activators tPA and uPA activate plasminogen to produce plasmin. Vascular endothelium produces prostacyclin (prostaglandin I2); it is a potent vasodilator that inhibits platelet activation.
Disorders in tHemostasis System and Changes in the Rheological Properties of the Blood in Ischemic Heart Disease and Diabetes Mellitus Patients
Published in E.I. Sokolov, Obesity and Diabetes Mellitus, 2020
The activity of antithrombin III fluctuated from 20.1 to 37.2 s (the norm is 25–35 s), while the fibrinolytic activity of the blood fluctuated within 13–22% (the norm is 15–17%). The intravascular aggregation of thrombocytes was absent in most of the healthy persons, as was the spontaneous aggregation of thrombocytes.
Coagulation Theory, Principles, and Concepts
Published in Harold R. Schumacher, William A. Rock, Sanford A. Stass, Handbook of Hematologic Pathology, 2019
Antithrombin III is the classic inhibitor of thrombin. Functionally it appears to be the most important inhibitor of not only thrombin, but also several other serine proteases of coagulation. The structure of antithrombin III is that of standard serine protease inhibitors which are lumped together under the term serpins (SERine Protease INhibitor). Antithrombin III is a single-chain glycoprotein having a molecular weight of 58,200. In the inhibition of thrombin by antithrombin III, a covalent bond is established between the reactive site on antithrombin III and the active site serine in thrombin (86,87).
Combined proteomics and transcriptomics identifies serpin family C member 1 associated protein as a biomarker of endometriosis
Published in Annals of Medicine, 2023
Xiao-yan Li, Xi Wang, Zhi-yue Gu, Ting-ting Sun, Jin-hua Leng, Qi Yu
As Table 2 indicates, SERPINC1 exhibited significant variances in the EM vs. control group on both the transcript and protein level, and these differences were supported by ELISA in the validation set. Validation using ELISA in an independent sample set (n = 44) showed a similar and statistically important trend (p < 0.05). The SERPINC1 gene is located on chromosome 1q23-25 and comprises 6 introns and 7 exons and spans 13.4 kbp of genomic deoxyribonucleic acid [29]. The SERPINC1 gene has a wide range of mutations, according to prior studies. To date, there have been more than 250 reports linking antithrombin deficiency with mutations in the SERPINC1 gene [30]. Mutations in SERPINC1 were discovered via direct sequencing of all seven exons and regulatory areas, as well as multiplex ligation-dependent probe amplification, in 21 families studied by Mulder et al. They found that nearly half of the SERPINC1 mutations were linked to type I antithrombin deficiency. The most common cause of antithrombin deficiency is a mutation in the SERPINC1 gene [30]. Because EM has long been considered a disease characterized by haemorrhage, the down-regulation of SERPINC1 may be associated with the aetiology of EM through the antithrombin pathway, which could lead to dysfunctional anticoagulation.
The antithrombosis effect of dehydroandrographolide succinate: in vitro and in vivo studies
Published in Pharmaceutical Biology, 2022
Bowen Yin, Shuhua Zhang, Yuxi Huang, Yuanzhu Long, Yiguo Chen, Shiyun Zhao, Aiqun Zhou, Minghua Cao, Xiaoming Yin, Daya Luo
In both the in vitro and in vivo experiments, AT-III activity increased by approximately 30–45%, suggesting that DAS effectively prevented the cascade reaction of the intrinsic and extrinsic pathways by enhancing AT-III activity. These results support previous research suggesting that andrographolide derivatives inhibit thrombin-induced platelet aggregation (Thisoda et al. 2006). Based on these findings, we indicated its exact antithrombin mechanism. This enables DAS to consolidate its anticoagulant effect by preventing secondary hemostasis through the inhibition of platelet aggregation. However, this enhancement is limited. On the one hand, antithrombin is responsible for inhibiting 60–70% of thrombin in vivo, and it mainly acts on FII, FIX, FX, FXI, and FXII. On the other hand, with increasing doses, the total amount of partially activated coagulation factors will gradually exceed the inhibitory capacity of AT-III. Therefore, with the increase in AT-III activity, coagulation factors with enhanced activity are still detected with an increasing dose, but the inhibitory effect of AT-III on FII effectively prevented the increase in the prothrombin complex and further inhibited thrombin-induced platelet aggregation. This process directly weakened the effect of secondary hemostasis on reinforcing platelet aggregation, and thus the final effect of DAS on secondary hemostasis was still attributed to the inhibition of platelet aggregation.
First Report of an α Chain Variant [Hb Coombe Park (HBA2: c.382A>G)] from India, Coinherited with a Novel SERPINC1 Gene Mutation: A Double Whammy?
Published in Hemoglobin, 2022
Sona B. Nair, Arundhati S. Athalye, Madhavi Panphalia, Firuza R. Parikh
Hereditary antithrombin (AT) deficiency, an important physiological inhibitor of blood coagulation proteases such as thrombin and factor Xa, are associated with high risk of a pro-thrombotic tendency is caused by mutations/variants in the SERPINC1 gene [4]. It is an autosomal disorder with a dominant inheritance pattern and affects about 1/2000 to 1/3000 individuals [5]. Antithrombin deficiency can be classified as a type I (quantitative) and type II (qualitative or functional) deficiency [6]. To date, several mutations have been reported in the SERPINC1 gene affecting the AT structure and function [7]. Antithrombin deficiency is mainly due to heterozygous mutations, as homozygous mutations are very rare and incompatible with life, though there have been reports of few homozygous cases [5].