Serpin family C member 1
Also known as antithrombin III isoform, antithrombin-III, serpin peptidase inhibitor clade C member 1, serpin peptidase inhibitor, clade C (antithrombin), member 1, SERPINC1, serine (or cysteine) proteinase inhibitor, clade C (antithrombin), member 1, Serpin C1
Antithrombin (AT) is a small glycoprotein that inactivates several enzymes of the coagulation system. It is a 464-amino-acid protein produced by the liver. It contains three disulfide bonds and a total of four possible glycosylation sites. α-Antithrombin is the dominant form of antithrombin found in blood plasma and has an oligosaccharide occupying each of its four glycosylation sites. A single glycosylation site remains consistently un-occupied in the minor form of antithrombin, β-antithrombin. Its activity is increased manyfold by the anticoagulant drug heparin, which enhances the binding of
Clinical Trials
55 registered- PHASE2ENROLLING_BY_INVITATIONAntithrombin to Improve Thromboprophylaxis and Reduce the Incidence of Trauma-Related Venous ThromboembolismBryan Cotton · NCT05794165
- PHASE2COMPLETEDSafety and Efficacy of Preoperative Antithrombin Supplementation in Patients Undergoing High-Risk Cardiopulmonary BypassGrifols Therapeutics LLC · NCT02037555
- PHASE4TERMINATEDResponse of Recombinant Antithrombin in Heparin Resistant Patients Undergoing Cardiac SurgeryMayo Clinic · NCT01547728
- PHASE3RECRUITING
~22 min read
Article
18 sectionsContents
- Structure
- Function
- Antithrombin and heparin
- Allosteric activation
- Non-allosteric activation
- Effect of glycosylation on activity
- Deficiencies
- Acquired antithrombin deficiency
- Inherited antithrombin deficiency
- Type I antithrombin deficiency
- Type II antithrombin deficiency
- Toponyms
- Medical uses
- Cleaved and latent antithrombin
- Antiangiogenic antithrombin
- References
- Further reading
- External links
Antithrombin (AT) is a small glycoprotein that inactivates several enzymes of the coagulation system. It is a 464-amino-acid protein produced by the liver. It contains three disulfide bonds and a total of four possible glycosylation sites. α-Antithrombin is the dominant form of antithrombin found in blood plasma and has an oligosaccharide occupying each of its four glycosylation sites. A single glycosylation site remains consistently un-occupied in the minor form of antithrombin, β-antithrombin. Its activity is increased manyfold by the anticoagulant drug heparin, which enhances the binding of antithrombin to factor IIa (thrombin) and factor Xa.
== Structure == Antithrombin is also termed antithrombin III (AT III). The designations antithrombin I through to antithrombin IV originate in early studies carried out in the 1950s by Seegers, Johnson and Fell.