Exploring antithrombin: insights into its physiological features, clinical implications and analytical techniques.
Blood Coagul Fibrinolysis
; 35(2): 43-48, 2024 Mar 01.
Article
en En
| MEDLINE
| ID: mdl-38179715
ABSTRACT
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 58â200âD. 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.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Antitrombinas
/
Deficiencia de Antitrombina III
Tipo de estudio:
Qualitative_research
Límite:
Humans
Idioma:
En
Revista:
Blood Coagul Fibrinolysis
Asunto de la revista:
ANGIOLOGIA
/
HEMATOLOGIA
Año:
2024
Tipo del documento:
Article
País de afiliación:
Emiratos Árabes Unidos
Pais de publicación:
Reino Unido