INT195092

Context Info Confidence 0.26 First Reported 2006 Last Reported 2010 Negated 0 Speculated 0 Reported most in Body Documents 4 Total Number 4 Disease Relevance 2.75 Pain Relevance 0.47

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

Anatomy Link Frequency cleavage 2 covering 1 F2 (Mus musculus)

Pain Link Frequency Relevance Heat metalloproteinase 2 99.52 Glutamate 24 91.92 cva 1 91.12 Inflammation 17 90.20 cytokine 15 79.48 rheumatoid arthritis 3 76.96 Angina 1 71.08 Inflammatory mediators 3 54.80 antagonist 9 20.72 anesthesia 5 5.00

Disease Link Frequency Relevance Heat Thrombosis 25 97.96 Adhesions 7 97.56 Diabetes Mellitus 67 96.52 Coronary Artery Disease 36 96.04 Renal Disease 27 95.72 Cv General 3 Under Development 2 91.12 INFLAMMATION 21 90.20 Brain Injury 10 87.52 Hypertrophy 3 84.96 Penetrating Head Injuries 5 81.16

Sentences Mentioned In

Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

Thrombin, a serine protease generated by cleaving pro-thrombin, is an essential component of the coagulation cascade.

Protein_catabolism (cleaving) of thrombin

1) Confidence 0.26 Published 2006 Journal J Neuroinflammation Section Body Doc Link PMC1533808 Disease Relevance 0.85 Pain Relevance 0.12

A unique N-terminal fragment of OPN (trOPN), produced by thrombin cleavage has previously been shown to be present in plasma and milk and may have physiologically distinct roles[17]-[19].

Protein_catabolism (cleavage) of thrombin in cleavage

2) Confidence 0.26 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2791444 Disease Relevance 0 Pain Relevance 0

However, once cleaved, (pro)thrombin was observed on fibrin fibers, covering the whole thrombus.

Protein_catabolism (cleaved) of thrombin in covering associated with thrombosis

3) Confidence 0.14 Published 2010 Journal PLoS ONE Section Abstract Doc Link PMC2861630 Disease Relevance 0.24 Pain Relevance 0

In vitro studies have reported that the N-terminal fragments of OPN generated by both thrombin cleavage and matrix metalloproteinase (MMP) cleavage induce enhanced adhesion compared with the effects of full-length OPN.

Protein_catabolism (cleavage) of thrombin in cleavage associated with metalloproteinase and adhesions

4) Confidence 0.06 Published 2010 Journal Cardiovasc Diabetol Section Body Doc Link PMC2988001 Disease Relevance 1.66 Pain Relevance 0.35

General Comments

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