Effects of Protein S and Factor Xa on Peptide Bond Cleavages during Inactivation of Factor Va and Factor VaR506Qby Activated Protein C

1995 ◽  
Vol 270 (46) ◽  
pp. 27852-27858 ◽  
Author(s):  
Jan Rosing ◽  
Lico Hoekema ◽  
Gerry A. F. Nicolaes ◽  
M. Christella L. G. D. Thomassen ◽  
H. Coenraad Hemker ◽  
...  
1981 ◽  
Author(s):  
F J Walker

The anticoagulant activity of activated Protein C has been observed to be species specific. This could be due either to the inability of the bovine enzyme to recognize its substrate, Factor Va, in non-bovine plasmas, or the absence of cofactor-Protein S, a protein that has been shown to be necessary for the maximum expression of the anticoagulant activity of activated Protein C. Activated Protein C was found to be an effective inhibitor of Factor Xa-initiated clotting of bovine plasma, but without activity in either human or rabbit plasma. Human and rabbit plasma supplemented with bovine Protein S was sensitive to the anticoagulant activity of activated Protein C. Neither rabbit nor human plasma contained bovine activated Protein C cofactor activity as measured by the enhancement of bovine activated Protein C-catalyzed inactivation of Factor Va. However, bovine activated Protein C was able to inactivate both human and rabbit Factor Va. The inactivation of both of these proteins could be stimulated by the addition of bovine Protein S. These results indicate that the species specificity of bovine activated Protein C is due to the absence of a cofactor protein in non-bovine plasma that will interact with the bovine enzyme. Secondly, these findings further confirm that Protein S is required for the maximal expression of the anticoagulant activity of activated Protein C.


2006 ◽  
Vol 281 (42) ◽  
pp. 31486-31494 ◽  
Author(s):  
Eva A. Norstrøm ◽  
Sinh Tran ◽  
Mårten Steen ◽  
Björn Dahlbäck

2006 ◽  
Vol 281 (42) ◽  
pp. 31486-31494
Author(s):  
Eva A. Norstrøm ◽  
Sinh Tran ◽  
Mårten Steen ◽  
Bjo¨rn Dahlba¨ck

1992 ◽  
Vol 67 (01) ◽  
pp. 046-049 ◽  
Author(s):  
H A Guglielmone ◽  
M A Vides

SummaryA simple and fast method for the quantitative determination of protein C activity in plasma is here described. The first step consists in the conversion of protein C in the test sample into activated protein C by means of an activator isolated from Southern Copperhead venom. Subsequently, the degradation of factor Va, in presence of protein C-deficient plasma, is measured by the prolongation of the prothrombin time which is proportional to the amount of protein C in the sample. The dose-response curve showed a linear relationship from 6 to 150% protein C activity and the inter- and intra-assay reproducibility was 3.5% and 5.6% respectively. In normal subjects, a mean of protein C level of 98 ± 15% of normal pooled plasma was found. Comparison with the anticoagulant assay in samples of patients with oral anticoagulant, liver cirrhosis, disseminated intravascular coagulation and severe preeclampsia revealed an excellent correlation (r = 0.94, p <0.001). Also, a similar correlation (r = 0.93, p <0.001) existed between amidolytic assay and the method here proposed for all the samples studied without including the oral anticoagulant group. These results allowed us to infer that this method evaluates the ability of protein C to interact with protein S, phospholipids, calcium ions and factor Va.


1982 ◽  
Vol 257 (3) ◽  
pp. 1443-1447
Author(s):  
M.E. Nesheim ◽  
W.M. Canfield ◽  
W. Kisiel ◽  
K.G. Mann

1993 ◽  
Vol 268 (4) ◽  
pp. 2872-2877
Author(s):  
M.J. Heeb ◽  
R.M. Mesters ◽  
G. Tans ◽  
J. Rosing ◽  
J.H. Griffin

2003 ◽  
Vol 278 (27) ◽  
pp. 24904-24911 ◽  
Author(s):  
Eva A. Norstrøm ◽  
Mårten Steen ◽  
Sinh Tran ◽  
Björn Dahlbäck

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