Protein C: An Automated Activity Assay

Ødegaard, O.R.; K, Try; Andersson, Terje R.

doi:10.1159/000215567

Cited by 25 publications

(18 citation statements)

References 4 publications

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“…Values in patients on heparin were excluded from the analysis. PC was determined as previously described [37]. The normal reference interval was 70–130%.…”

Section: Methodsmentioning

confidence: 99%

Lipoprotein(a), Other Lipoproteins and Hemostatic Profiles in Patients with Ischemic Stroke: The Relation to Cardiogenic Embolism

Dahl

Kontny²,

Slagsvold³

et al. 2000

Cerebrovasc Dis

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Lipoprotein and hemostatic profiles including coagulation inhibitors were determined in 136 patients with acute ischemic stroke. Based on clinical examination, cerebral computed tomography, Doppler ultrasonography of precerebral arteries and transthoracic echocardiography, the strokes were classified as cardioembolic (n = 38), non-cardioembolic (n = 92), and mixed cardioembolic/hypertensive (n = 6). Patients with cardioembolic stroke were older than patients with non-cardioembolic stroke. Lipoprotein(a) was higher in the cardioembolic than in the non-cardioembolic group. Lipoprotein(a) was not significantly correlated to the other lipid levels and may represent an independent lipid risk factor. The non-cardioembolic group had higher levels of total cholesterol, triglycerides, total cholesterol/high-density lipoprotein cholesterol ratio, low-density lipoprotein cholesterol, apolipoprotein A1, and apolipoprotein B. The cardioembolic group had higher concentrations of fibrinogen and D-dimer, and lower levels of antithrombin, protein C, protein S and heparin cofactor 2 than the non-cardioembolic group. The differences in the hemostatic profile are consistent with thrombosis due to activated coagulation being more involved in the pathogenesis of cardioembolic than of non-cardioembolic stroke. Lipoprotein(a) seems to be more associated with coagulation markers of thrombosis than with atherosclerosis, whereas the other lipids mainly seem to be risk factors for atherosclerosis.

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“…Values in patients on heparin were excluded from the analysis. PC was determined as previously described [37]. The normal reference interval was 70–130%.…”

Section: Methodsmentioning

confidence: 99%

Lipoprotein(a), Other Lipoproteins and Hemostatic Profiles in Patients with Ischemic Stroke: The Relation to Cardiogenic Embolism

Dahl

Kontny²,

Slagsvold³

et al. 2000

Cerebrovasc Dis

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“…The P-prothrombin complex was analyzed with reagents front Stago, Asnières, France, and P-fibrinogen was determined with a polymerization method [5], Amidolytic methods, using chromogenic peptide substrates (from Chrontogenix, formerly Kabi Diagnostics, Mölndal, Sweden) were used to assay P-protein C [6], P-antithrombin [7] and P-F VII [8], respectively, with a centrifugal analyzer (Cobas Bio, Roche, Basel, Switzerland). A similar method was also employed to measure P-PAI-1 [9] using the substrate PAR/pl (Bio pool, Umeâ, Sweden) and P-soluble fibrin, previously called fibrin monomers [10], using a substrate from Chromogenix.…”

Section: Laboratory Methodsmentioning

confidence: 99%

Hemostatic Abnormalities May Predict Chronic Hypertension after Preeclampsia

Bremme

Blombäck

1996

Gynecol Obstet Invest

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Objectives: Preeclampsia is a pregnancy-induced hypertensive disease. About 25–30% of women suffering from this disease will later, while still fertile, develop essential hypertension. Study design: Various hemostatic variables known to increase the risk of cardiovascular complications were investigated in 28 women with severe preeclampsia and 14 with mild preeclampsia 6–15 months after delivery. Results: High levels of the coagulation inhibitors protein C and total protein S were found in the women with severe preeclampsia (p < 0.001). The levels of prothrombin complex, fibrinogen, plasminogen activator inhibitor-1 were increased in women who had previously had severe preeclampsia as compared to those who had had mild preeclampsia (p < 0.01). The levels of the four markers for thrombin activity (thrombin-antithrombin complex, prothrombin fragments 1+2, fibrin Z)-dimers and soluble fibrin) were higher in the severe preeclampsia group. In 12 women in this group (43%), the levels of three to four variables were higher than the reference ranges (mean ± 2 SD). In patients with earlier severe or mild preeclampsia, factor VII antigen was also found to be increased as compared to normal fertile women (p < 0.02). Conclusions: Women with earlier severe preeclampsia displayed increased levels of coagulation factors and the main fibrinolytic inhibitor, high levels of which are known to predict cardiovascular events. This was also reflected by increased levels of thrombin markers.

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“…The amidolytic activity of APC was determined by the hydrolysis of a tripeptide substrate Glu-Pro-Arg-p-nitroanilide (S-2366) (Kabi) at 2 mM concentration in 0.05 M Tris, pH 8.4 buffer, at 20~ (Odegaard et al, 1987). One unit of APC was defined as the amount of APC required to release 1 ~tmol of p-nitroanilide (pNA) at 20~ pH 8.4, using an extinction coefficient of 9620M -1 cm -1 for pNA at 405 nm.…”

Section: Determination Of the Functional Activities Of Rhpcmentioning

confidence: 99%

Inefficient processing of human protein C in the mouse mammary gland

Drohan

Zhang²,

Paleyanda

et al. 1994

Transgenic Research

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Vitamin K-dependent plasma protein, human Protein C (HPC) has been expressed in transgenic mice, using a 4.2 kb mouse whey acidic protein (WAP) promoter, 9.0 kb HPC gene and 0.4 kb 3' flanking sequences. Expression was mammary gland-specific and the recombinant human Protein C (rHPC) was detected in milk at concentrations of 0.1 to 0.7 mg ml-1. SDS-PAGE revealed that the single, heavy and light chains of rHPC migrated with increased electrophoretic mobility, as compared to HPC. Enzymatic deglycosylation showed that these molecular weight disparities are in part due to differential glycosylation. The substantial increase observed in the amount of single chain protein, as well as the presence of the propeptide attached to 20-30% of rHPC, suggest that mouse mammary epithelial cells are not capable of efficient proteolytic processing of rHPC. The Km of purified rHPC for the S-2366 synthetic substrate was similar to that of plasma-derived HPC, while the specific activity was about 42-77%. Amino acid sequence analyses and low anticoagulant activity of purified rHPC suggest that gamma-carboxylation of rHPC is insufficient. These results show that proteolytic processing and gamma-carboxylation can be limiting events in the overexpression of fully biologically active rHPC in the mouse mammary gland.

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Protein C: An Automated Activity Assay

Cited by 25 publications

References 4 publications

Lipoprotein(a), Other Lipoproteins and Hemostatic Profiles in Patients with Ischemic Stroke: The Relation to Cardiogenic Embolism

Lipoprotein(a), Other Lipoproteins and Hemostatic Profiles in Patients with Ischemic Stroke: The Relation to Cardiogenic Embolism

Hemostatic Abnormalities May Predict Chronic Hypertension after Preeclampsia

Inefficient processing of human protein C in the mouse mammary gland

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