Coagulation factors

Author:Prof. Dr. med. Peter Altmeyer

All authors of this article

Last updated on: 29.10.2020

Dieser Artikel auf Deutsch

Requires free registration (medical professionals only)

Please login to access all articles, images, and functions.

Our content is available exclusively to medical professionals. If you have already registered, please login. If you haven't, you can register for free (medical professionals only).


Requires free registration (medical professionals only)

Please complete your registration to access all articles and images.

To gain access, you must complete your registration. You either haven't confirmed your e-mail address or we still need proof that you are a member of the medical profession.

Finish your registration now

DefinitionThis section has been translated automatically.

The clotting factors are mainly enzymes, but also coenzymes that accelerate the reaction. For historical reasons, the individual coagulation factors have several names, which often led to confusion. Therefore, the "International Committee for the Standardization of the Nomenclature of the Blood Clotting Factors" was founded in 1954 and the clotting factors were numbered consecutively, if possible in the order of their discovery.

The factors II, VII, IX, X, XI and XII are serine proteases. Factors II, VII, IX and X are vitamin K-dependent and are synthesized ribosomally in hepatocytes. Postribosomally, they are coenzyme co-synthesized with vitamin K to the activating factors y-carboxylated. The y-carboxyl group enables the factors to bind to the calcium-phospholipid matrix, especially in the thrombocinase complex.
The activation of the factors takes place by splitting the reactive centre. At the same time, they become accessible for inhibitors.

Common to all serine proteases are the catalytic targets serine 195, histidine 57 and asparagine 102. All serine kinases act by reversible hydrolysis and water binding. In contrast to other enzymes, the catalytic action of serine proteases is not reversible. The reason for this is on the one hand a fast separation of enzyme and substrate and a stretching of the protein chain after binding of the substrate to the serine, histidine and aspartic acid.
The serine kinases become particularly active when they come into contact with injured membranes. Due to regulatory subunits the serine kinases have a high specificity in contrast to unspecific proteases, e.g. trypsin.

Activation leads to a considerable reduction in the half-lives of the enzymes, e.g. factor II, prothrombin, has a half-life of 48 hours, factor IIa, thrombin, has a half-life of only a few seconds.

The factors at a glance

Factors Effect Plasma concentration (mg/dl) Molecular weight (MD) Half-life Place of education
F-I Fibrinogen Substrate 200-400 341.000 5-6 days Liver
F-II Prothrombin enzyme 6-10 72.000 48 hours Liver, vitamin K-dependent
F-III Thrombokinase enzyme Depending on polymer: 53.000-425.000 29.000 very brief Intermediary product
F-IV Ca++ Catalyst Ionized and bound effective
F-V Proakzelerin Accelerator approx. 3 300.000 12-15 hours Liver
F-VII Proconvertin enzyme approx. 0,1 56.000 2-5 hours
(VIIa < 2 hours)
Liver, vitamin K dependent
F-VIII antihemophilic factor Accelerator 0,5-1,0 approx. 2 x 106 5-12 hours Liver and megakaryocytes
F-IX Christmas Factor enzyme 0,5-0,7 72.000 12-30 hours
(IXa < 12 hours)
Liver, vitamin K dependent
F-X Stuart factor enzyme approx. 0,8 72.000 32 hours
(Xa 4 hours)
Liver, vitamin K dependent
F-XI enzyme approx. 0,6 180.000 < 12 hours Liver
F-XII Hageman factor enzyme 1,4-4,7 80.000 < 12 hours Liver
F-XIII enzyme 2-3 d Liver
F-XIV enzyme 1,0-4,0 300.000
HMWK 0,5-2,0 180.000
F-XV 1,4-4,5 88.000
protein Z Cofactor for binding thrombin to lipid surface 2,9 62.000 2,5 d Liver, vitamin K-dependent

LiteratureThis section has been translated automatically.

  1. HA Neumann (2014) The coagulation system. ABW-Wissenschaftsverlag GmbH Berlin S. 48f.
  2. HA Neumann (2014) The coagulation system. ABW-Wissenschaftsverlag GmbH Berlin S. 72f.

Authors

Last updated on: 29.10.2020