INT168000

Context Info Confidence 0.63 First Reported 2006 Last Reported 2010 Negated 0 Speculated 0 Reported most in Body Documents 6 Total Number 6 Disease Relevance 2.19 Pain Relevance 0.63

peptidase activity (F2) extracellular space (F2) extracellular region (F2) plasma membrane (F2)

Anatomy Link Frequency endothelial cell 1 cleavage 1 platelet 1 F2 (Homo sapiens)

Pain Link Frequency Relevance Heat Inflammation 142 94.36 cva 5 91.92 Potency 2 87.24 anesthesia 5 83.68 cytokine 149 79.48 abdominal pain 4 51.84 tolerance 1 48.44 rheumatoid arthritis 2 17.72 Inflammatory response 10 5.00 addiction 3 5.00

Disease Link Frequency Relevance Heat Coagulation Disorder 2 99.50 Myocardial Infarction 1 98.96 Thrombosis 52 98.28 INFLAMMATION 154 94.36 Thromboembolism 3 92.28 Pressure Volume 2 Under Development 4 90.40 Death 16 81.40 Cv General 4 Under Development 3 76.96 Paroxysmal Nocturnal Hemoglobinuria 1 75.80 Thrombosis Related Under Development 3 74.08

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Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

This is possible because the variant prothrombin is resistant to degradation.

Protein_catabolism (degradation) of prothrombin

1) Confidence 0.63 Published 2010 Journal J Med Case Reports Section Body Doc Link PMC2868876 Disease Relevance 0.94 Pain Relevance 0.09

To design the efficient thrombin inhibitors we have synthesized and studied peptide-based inhibitors resistant to enzymatic degradation.

Protein_catabolism (degradation) of thrombin

2) Confidence 0.48 Published 2008 Journal The Open Biochemistry Journal Section Abstract Doc Link PMC2627521 Disease Relevance 0.29 Pain Relevance 0.09

As prothrombin can be enzymatically cleaved into thrombin in the presence of active proteases, labeling was performed in the presence of the serine protease inhibitor PPACK.

Protein_catabolism (cleaved) of prothrombin

3) Confidence 0.18 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2861630 Disease Relevance 0.06 Pain Relevance 0

When bound to thrombomodulin, a thrombin receptor on the endothelial cell surface, thrombin activates protein C, which can degrade Factor VIIIa and Factor Va, essential cofactors in the activation of Factor X and prothrombin respectively [164].

Protein_catabolism (degrade) of prothrombin in endothelial cell

4) Confidence 0.09 Published 2006 Journal Malar J Section Body Doc Link PMC1629020 Disease Relevance 0.51 Pain Relevance 0.22

Coagulation parameters such as hematocrit, activated clotting time (ACT), fibrinogen, prothrombin time (PT), international normalized ratio (INR), platelet count, and fibrin degradation products (FDP) were investigated before cardiopulmonary bypass (CPB), after protamine administration, and at four hours postoperatively in the ICU.

Protein_catabolism (degradation) of prothrombin in platelet associated with coagulation disorder

5) Confidence 0.08 Published 2010 Journal Ann Card Anaesth Section Abstract Doc Link 20442540 Disease Relevance 0.31 Pain Relevance 0.23

To address this issue, we analyzed the time course of human prothrombin cleavage by Bi-VSP and found that thrombin was the major cleavage product (Figure 4).

Protein_catabolism (cleavage) of prothrombin in cleavage

6) Confidence 0.07 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2862700 Disease Relevance 0.08 Pain Relevance 0

General Comments

This test has worked.