Title
The cofactor role of protein S in the acceleration of whole blood clot lysis by activated protein C in vitro
Author
de Fouw, N.J.
Haverkate, F.
Bertina, R.M.
Gaubius Instituut TNO
Publication year
1986
Abstract
The effect of purified human activated protein C (APC) and protein S on fibrinolysis was studied by using an in vitro blood clot lysis technique. Blood clots were formed from citrated blood (supplemented with 125I-fibrinogen) by adding thrombin and Ca2+-ions; lysis of the clots was achieved by adding tissue-type plasminogen activator. The release of labeled fibrin degradation products from the clots into the supernatant was followed in time. We clearly demonstrated that APC accelerates whole blood clot lysis in vitro. The effect of APC was completely quenched by antiprotein C IgG, pretreatment of APC with diisopropylfluorophosphate, and preincubation of the blood with antiprotein S IgG. This demonstrates that both the active site of APC and the presence of the cofactor, protein S, are essential for the expression of the profibrinolytic properties. At present, the substrate of APC involved in the regulation of fibrinolysis is not yet known. Analysis of the radiolabeled fibrin degradation products demonstrated that APC had no effect on the fibrin cross-linking capacity of factor XIII. Chemicals/CAS: Cross-Linking Reagents; Fibrin Fibrinogen Degradation Products; Glycoproteins; Immunoglobulin G; Protein C; Protein S
Subject
Activated protein c
Protein s
Blood and hemopoietic system
Fibrinogen i 125
In vitro study
Cross-Linking Reagents
Fibrin Fibrinogen Degradation Products
Fibrinolysis
Glycoproteins
Human
Immunoglobulin G
In Vitro
Protein C
Protein S
Support, Non-U.S. Gov't
Time Factors
To reference this document use:
http://resolver.tudelft.nl/uuid:14a832ba-cc29-4b2d-995c-5d6e2db0392e
TNO identifier
230079
ISSN
0006-4971
Source
Blood, 67 (4), 1189-1192
Document type
article