دورية أكاديمية

Exploring antithrombin: insights into its physiological features, clinical implications and analytical techniques.

التفاصيل البيبلوغرافية
العنوان: Exploring antithrombin: insights into its physiological features, clinical implications and analytical techniques.
المؤلفون: Saboor M; Department of Medical Laboratory Sciences, College of Health Sciences, University of Sharjah, Sharjah, United Arab Emirates., Hamali HA; Department of Medical Laboratory Technology, College of Applied Medical Sciences, Jazan University, Jazan, Saudi Arabia., Mobarki AA; Department of Medical Laboratory Technology, College of Applied Medical Sciences, Jazan University, Jazan, Saudi Arabia., Madkhali AM; Department of Medical Laboratory Technology, College of Applied Medical Sciences, Jazan University, Jazan, Saudi Arabia., Dboie G; Department of Medical Laboratory Technology, College of Applied Medical Sciences, Jazan University, Jazan, Saudi Arabia.
المصدر: Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis [Blood Coagul Fibrinolysis] 2024 Mar 01; Vol. 35 (2), pp. 43-48. Date of Electronic Publication: 2023 Dec 15.
نوع المنشور: Review; Journal Article
اللغة: English
بيانات الدورية: Publisher: Lippincott Williams And Wilkins Country of Publication: England NLM ID: 9102551 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1473-5733 (Electronic) Linking ISSN: 09575235 NLM ISO Abbreviation: Blood Coagul Fibrinolysis Subsets: MEDLINE
أسماء مطبوعة: Publication: London : Lippincott Williams And Wilkins
Original Publication: Oxford, UK : Rapid Communications of Oxford Ltd., c1990-
مواضيع طبية MeSH: Antithrombins*/therapeutic use , Antithrombins*/chemistry , Antithrombin III Deficiency*/drug therapy, Humans ; Antithrombin III ; Anticoagulants ; Heparin ; Blood Coagulation
مستخلص: Antithrombin is an essential protein that acts as a natural anticoagulant in the human body. It is synthesized by the liver and belongs to the serine protease inhibitors, which are commonly referred to as the SERPINS superfamily. The antithrombin molecule comprises 432 amino acids and has a molecular weight of approximately 58 200 D. It consists of three domains, including an amino-terminal domain, a carbohydrate-rich domain, and a carboxyl-terminal domain. The amino-terminal domain binds with heparin, whereas the carboxyl-terminal domain binds with serine protease. Antithrombin is a crucial natural anticoagulant that contributes approximately 60-80% of plasma anticoagulant activities in the human body. Moreover, antithrombin has anti-inflammatory effects that can be divided into coagulation-dependent and coagulation-independent effects. Furthermore, it exhibits antitumor activity and possesses a broad range of antiviral properties. Inherited type I antithrombin deficiency is a quantitative disorder that is characterized by low antithrombin activity due to low plasma levels. On the other hand, inherited type II antithrombin deficiency is a qualitative disorder that is characterized by defects in the antithrombin molecule. Acquired antithrombin deficiencies are more common than hereditary deficiencies and are associated with various clinical conditions due to reduced synthesis, increased loss, or enhanced consumption. The purpose of this review was to provide an update on the structure, functions, clinical implications, and methods of detection of antithrombin.
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المشرفين على المادة: 0 (Antithrombins)
9000-94-6 (Antithrombin III)
0 (Anticoagulants)
9005-49-6 (Heparin)
تواريخ الأحداث: Date Created: 20240105 Date Completed: 20240205 Latest Revision: 20240308
رمز التحديث: 20240308
DOI: 10.1097/MBC.0000000000001271
PMID: 38179715
قاعدة البيانات: MEDLINE
الوصف
تدمد:1473-5733
DOI:10.1097/MBC.0000000000001271