Prothrombin fragment

Fig. 2. Generation of tenase and prothrombin complexes. PPL represents the anionic phospholipid surface provided by the platelets (platelet phospholipid). Cleavage of prothrombin by the prothrombinase complex results in the formation of thrombin and the release of a small fragment called prothrombin fragment 1.2 (PFI.2).

K. H. Pearce, R. G. Hiskey, and N. L. Thompson, Binding kinetics of fluorescently labeled bovine prothrombin fragment 1 at planar model membranes measured by total internal reflection fluorescence microscopy, Biophys. J. 59, 622a (1991). 

The a-thrombin dissociates from the prothrombin fragment 1-2 and diffuses to its substrates platelets (the platelet thrombin receptor), factor V, factor VIII,... 

Also see color figure.) Tissue factor-factor Vila complex. The three-dimensional structure of the complex of factor Vila and tissue factor (minus the transmembrane polypeptide domain of the tissue factor) in the absence of membrane surface. It is approximately 115 A in length and has a diameter of 40-50 A. Factor Vila shows its four distinct domains the Gla domain, two EGF-like domains, and the proteinase domain. Tissue factor contacts factor VHa via the interface between the two fibronectin type Ill-like domains. All four domains of factor Vila appear to be involved in the interaction between tissue factor and factor Vila. The Gla domain of factor Vila is folded very similarly to the Gla domain of prothrombin (Gla domain of prothrombin fragment 1). Activation of factor VII can be catalyzed by thrombin, factor Xa, factor Vila, and factor Xlla—all by cleavage at Arg -Ile . Secondary structures are shown in the center diagram two views of the close interactions between TF and factor Vila are shown in the two diagrams at each side. 

Elevated D-dimer Decreased antithrombin Decreased fibrinogen Thrombocytopenia Decreased protein C and protein S Increased fibrinopeptides A and B Elevated prothrombin fragments 1 and 2 Evidence of end-organ dysfunction or failure... 

L. Li, T. Darden, C. Foley, R. Hiskey, L. Pedersen. Homology modeling and molecular dynamics simulation of human prothrombin fragment 1. Protein Sci. 1995, 4, 2341-2348. 

Following the initial structure determination of D-Phe-Pro-Arg chloromethyl ketone-inhibited human a-fhrombin [25], the structures of more than 100 thrombin complexes have been solved and deposited in the Protein Data Bank. In addition, a number of prothrombin fragments and intermediates, the three-dimensional structure of the immediate precursor of a-thrombin, prethrombin-2 (pre-cleavage cat-... 

Compared to placebo patients, patients who received rhAT showed significant inhibition of the generation of two markers of thrombin activation - prothrombin fragment 1.2 and thrombin-antithrombin complex. 

This adverse effect is related to the abihty of OKT3 to activate the coagulation system as indicated by sequential determinations of plasma levels of prothrombin fragments 1+2 (F1+2). These molecules are released during conversion of prothrombin to thrombin and witness activation of the common pathway of the coagulation system [162]. All kidney transplant recipients tested in our center displayed increased plasma levels of prothrombin fragments, which peaked 4 hours after the first injection of OKT3 (mean + SEM 4.82 ... 

Similarly to prothrombin. Fragment 1 containing the Y carboxy-glutamic residues, increased the capacitance of PS-containing mono-layers, also givij rise to a pseudocapacitance peak. The effect increases with Ca and with Fragment 1 concentration and it is lar-... 

Marin et al. (M7) reported that patients with atrial fibrillation had lower levels of plasma MMP-1 but increased levels of TIMP-1 and prothrombin fragments FI 2 (an index of thrombogenesis) and higher ratios of TIMP-1 to MMP-1 as compared to control subjects. The authors proposed that MMP TIMP measurements in blood might be useful as markers of comorbidity that is associated with increased risk of stroke and thromboembolism in patients with atrial fibrillation. 

Desialylation destroys the protease activity of plasminogen. Functional prothrombin arises from its precursor by two post-translational modifications a vitamin K-dependent carboxylation of glutamic acid residues, followed by glycosylation in the carboxylated region (prothrombin fragment 1 AS 1-156). Deglycosylation of prothrombin in the presence of Ca " leads to greatly increased self-association this occurs at certain contact points on the molecule, which are probably concealed by carbohydrate chains in the intact molecule (Fletcher et al... 

Figure 1 The Ca(II) ion network in bovine prothrombin fragment 1. A similar network is present in all of the vitamin K-dependent coagulation proteins. Coordinates kindly provided by A1 Tulinsky. Moviemol was used to prepare the figure. Thanks to Lallth Perera for assistance...

Fig. 8 In vitro hemocompatibility of solution-cast P3HB films, compared to that of P3HB films modified with 30% each of at-P3HB, dg-P3HB, TEC (leached), and BTHC PLLA films for comparison. Activation of a cellular coagulation (release of /3-thromboglobulin, control = collagen), b plasmatic coagulation (release of prothrombin fragment Fl+2, control = kaolinite), and c complement system (release of C3a-desArg, control = inulin) [72]...

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