INT4560

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Context Info
Confidence 0.96
First Reported 1975
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 18
Total Number 18
Disease Relevance 11.64
Pain Relevance 2.32

This is a graph with borders and nodes. Maybe there is an Imagemap used so the nodes may be linking to some Pages.

peptidase activity (PLG) extracellular space (PLG) extracellular region (PLG)
plasma membrane (PLG)
Anatomy Link Frequency
extracellular matrix 4
blood 2
macrophages 1
plasma 1
liver 1
PLG (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 240 100.00 Very High Very High Very High
Pain 6 99.64 Very High Very High Very High
Angina 10 98.40 Very High Very High Very High
Inflammation 126 85.76 High High
Central nervous system 73 85.24 High High
depression 1 78.32 Quite High
Inflammatory response 10 77.88 Quite High
cytokine 32 62.32 Quite High
rheumatoid arthritis 38 57.28 Quite High
Neuropeptide 2 29.84 Quite Low
Disease Link Frequency Relevance Heat
Viral Meningitis 168 99.82 Very High Very High Very High
Adhesions 18 99.32 Very High Very High Very High
Metastasis 26 99.30 Very High Very High Very High
Cancer 418 98.82 Very High Very High Very High
Wound Healing 1 98.44 Very High Very High Very High
Angina 10 98.40 Very High Very High Very High
Disease 112 98.20 Very High Very High Very High
Breast Cancer 185 97.76 Very High Very High Very High
Pressure Volume 2 Under Development 28 96.48 Very High Very High Very High
Burns 2 95.60 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Plasmin degrades the ECM, directly by removing glycoproteins from the ECM [43] and it releases axonal guidance molecules from the extracellular matrix [19]. tPA has multifaceted effects on tissue; it interacts with parenchymal cells through proteolytic plasminogen or non-plasminogen pathways [44]–[47].
Protein_catabolism (degrades) of Plasmin in extracellular matrix
1) Confidence 0.96 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2815778 Disease Relevance 0.05 Pain Relevance 0
Plasminogen and fibrinogen/fibrin degradation product (FDP) levels were normal in all patients.
Protein_catabolism (degradation) of Plasminogen
2) Confidence 0.86 Published 1975 Journal Blut Section Abstract Doc Link 1203541 Disease Relevance 0.55 Pain Relevance 0.19
For example, the urokinase-type plasminogen activator (uPA) and tissue-type plasminogen activator play a critical role in several processes, including clot dissolution, extracellular matrix (ECM) remodelling, angiogenesis and wound healing, as well as tumour invasion and metastasis [15]. uPA converts plasminogen to plasmin, which is a broad-spectrum enzyme that can degrade not only fibrin but also proteins of the joint ECM and cartilage.
Protein_catabolism (degrade) of plasmin in extracellular matrix associated with cancer, wound healing and metastasis
3) Confidence 0.86 Published 2007 Journal Arthritis Res Ther Section Body Doc Link PMC2212555 Disease Relevance 0.64 Pain Relevance 0.27
The fibrillar integrity of the collagen layer was confirmed by incubation with collagenase that degraded the film whilst the collagen fibres were resistant to degradation by both trypsin and plasmin (data not shown).
Protein_catabolism (degradation) of plasmin
4) Confidence 0.86 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.71 Pain Relevance 0.10
Thrombin and plasmin cleave, thereby activating protease-activated receptor -1 (PAR-1) on macrophages.
Protein_catabolism (cleave) of plasmin in macrophages
5) Confidence 0.64 Published 2008 Journal International Journal of Chronic Obstructive Pulmonary Disease Section Body Doc Link PMC2629972 Disease Relevance 0.69 Pain Relevance 0
Plasmin triggers protease cascades that degrade plasma and extracellular matrix proteins.
Protein_catabolism (degrade) of Plasmin in extracellular matrix
6) Confidence 0.64 Published 2006 Journal J Transl Med Section Body Doc Link PMC1479838 Disease Relevance 1.57 Pain Relevance 0.09
The contribution of these proteins in cancer progression relies on their capacity to control various biological processes such as (i) cell proliferation [5]; (ii) cell invasion through plasmin-mediated extracellular matrix degradation [6]; (iii) cell adhesion and migration through the interaction of uPA/uPAR/PAI-1 complex with vitronectin and integrins [7]; and (iv) cell apoptosis through the control of pro-apoptotic factor release [8].
Protein_catabolism (degradation) of plasmin in extracellular matrix associated with cancer, apoptosis and adhesions
7) Confidence 0.64 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2836381 Disease Relevance 1.19 Pain Relevance 0.07
It has recently been demonstrated that binding of u-PA to its receptor increases pro-MMP-2,-9 [23] and -13 [16] activation, and that in the absence of cells, plasmin not only fails to activate pro-MMPs, but rapidly degrades them [23].
Protein_catabolism (degrades) of plasmin associated with metalloproteinase
8) Confidence 0.64 Published 2005 Journal Cancer Cell Int Section Body Doc Link PMC548674 Disease Relevance 0.56 Pain Relevance 0.19
Inhibitors of both the PAS (aprotinin and PA inhibitor-1) and MMPs (CT1166 and tisue inhibitor of metalloproteinase) blocked collagen degradation, demonstrating the requirement of both plasminogen activation and MMP activity for degradation.
Protein_catabolism (degradation) of plasminogen associated with metalloproteinase
9) Confidence 0.50 Published 2005 Journal Cancer Cell Int Section Abstract Doc Link PMC548674 Disease Relevance 0.46 Pain Relevance 0.27
The impact of 6-week strenuous exercise training (SET) on blood coagulative and fibrinolytic parameters (levels of fibrinogen, soluble fibrin, fibrinogen-fibrin degradation products, activities of plasminogen and plasmin) was studied in 28 patients with first angina pectoris, in 16 of whom in the first 3 months of onset of the disease, but angina pectoris lasting 3-4 prior to SET.
Protein_catabolism (degradation) of plasmin in blood associated with angina and disease
10) Confidence 0.28 Published 1991 Journal Kardiologiia Section Abstract Doc Link 1895656 Disease Relevance 0.45 Pain Relevance 0.42
Plasmin triggers protease cascades that degrade plasma and extracellular matrix proteins.
Protein_catabolism (degrade) of Plasmin in plasma
11) Confidence 0.22 Published 2006 Journal J Transl Med Section Body Doc Link PMC1479838 Disease Relevance 1.57 Pain Relevance 0.09
Plasmin degrades fibrin leading to the premature breakdown of hemostatic clots and subsequent increased blood loss and transfusion requirements.[2] Kang reported that 82.5% of patients showed signs of hyperfibrinolytic activity in at least one blood sample during OLT.[5] Identification of hyperfibrinolysis as one of the underlying mechanisms of increased blood loss during liver transplantation has provided support for a more goal-directed therapy, using antifibrinolytic drugs.[2] Antifibrinolytic drugs are available as direct inhibitors of plasminogen (lysine analogs eg.
Protein_catabolism (degrades) of Plasmin in liver associated with pressure volume 2 under development
12) Confidence 0.12 Published 2008 Journal Asian Journal of Transfusion Science Section Body Doc Link PMC2798768 Disease Relevance 0.63 Pain Relevance 0
Both serine (130 KD) and metalloproteases (150 KD) of AGE isolate degrade plasminogen
Protein_catabolism (degrade) of plasminogen associated with viral meningitis
13) Confidence 0.09 Published 2006 Journal BMC Microbiol Section Body Doc Link PMC1464133 Disease Relevance 0.32 Pain Relevance 0
In this study, the zymographic assays revealed that both serine and metalloproteases from AGE isolate degraded plasminogen at neutral pH (Fig. 5).


Protein_catabolism (degraded) of plasminogen associated with viral meningitis
14) Confidence 0.09 Published 2006 Journal BMC Microbiol Section Body Doc Link PMC1464133 Disease Relevance 0.25 Pain Relevance 0
We observed that both serine and metalloproteases directly degraded pro-enzyme, plasminogen suggesting that pathogenesis of AGE may involve the uPA/tPA system.
Protein_catabolism (degraded) of plasminogen associated with viral meningitis
15) Confidence 0.07 Published 2006 Journal BMC Microbiol Section Body Doc Link PMC1464133 Disease Relevance 0.62 Pain Relevance 0.12
These proteases degrade extracellular matrix (ECM), which provide structural and functional support to the brain tissue, as shown by the degradation of collagen I and III (major components of collagenous ECM), elastin (elastic fibrils of ECM), plasminogen (involved in proteolytic degradation of ECM), as well as casein and haemoglobin.
Protein_catabolism (degradation) of plasminogen in brain
16) Confidence 0.07 Published 2006 Journal BMC Microbiol Section Abstract Doc Link PMC1464133 Disease Relevance 0.59 Pain Relevance 0.04
During fibrinolysis, plasminogen is cleaved by tissue plasminogen activator (TPA) or urokinase-type plasminogen activator to form plasmin that lyses the fibrin clot, releasing fibrin degradation products.
Protein_catabolism (cleaved) of plasminogen
17) Confidence 0.06 Published 2006 Journal Thromb J Section Body Doc Link PMC1533804 Disease Relevance 0.33 Pain Relevance 0.07
The impact of 6-week strenuous exercise training (SET) on blood coagulative and fibrinolytic parameters (levels of fibrinogen, soluble fibrin, fibrinogen-fibrin degradation products, activities of plasminogen and plasmin) was studied in 28 patients with first angina pectoris, in 16 of whom in the first 3 months of onset of the disease, but angina pectoris lasting 3-4 prior to SET.
Protein_catabolism (degradation) of plasminogen in blood associated with angina and disease
18) Confidence 0.03 Published 1991 Journal Kardiologiia Section Abstract Doc Link 1895656 Disease Relevance 0.44 Pain Relevance 0.41

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