INT176516

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Context Info
Confidence 0.76
First Reported 2004
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 28
Total Number 28
Disease Relevance 19.39
Pain Relevance 1.90

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

extracellular space (Spp1) extracellular region (Spp1) cell adhesion (Spp1)
cytoplasm (Spp1)
Anatomy Link Frequency
T cell 3
alveolar macrophages 2
stroma 1
plasma 1
epithelial cells 1
Spp1 (Mus musculus)
Pain Link Frequency Relevance Heat
chemokine 59 100.00 Very High Very High Very High
Inflammation 257 99.96 Very High Very High Very High
cytokine 186 99.16 Very High Very High Very High
fibrosis 149 97.32 Very High Very High Very High
Inflammatory marker 3 73.84 Quite High
rheumatoid arthritis 4 62.32 Quite High
imagery 28 36.84 Quite Low
metalloproteinase 37 26.92 Quite Low
agonist 4 20.72 Low Low
Inflammatory response 10 14.32 Low Low
Disease Link Frequency Relevance Heat
INFLAMMATION 227 99.96 Very High Very High Very High
Diabetes Mellitus 86 99.84 Very High Very High Very High
Atherosclerosis 10 99.52 Very High Very High Very High
Cancer 697 99.40 Very High Very High Very High
Sprains And Strains 53 99.04 Very High Very High Very High
Blister 72 98.84 Very High Very High Very High
Renal Disease 28 98.72 Very High Very High Very High
Insulin Resistance 38 98.60 Very High Very High Very High
Targeted Disruption 394 98.58 Very High Very High Very High
Cardiovascular Disorder Under Development 112 97.64 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Osteopontin (Opn), also known as early T cell activation gene-1, or eta-1, is a secreted, acidic glycoprotein with pleiotropic effects.
Localization (secreted) of Osteopontin in T cell
1) Confidence 0.76 Published 2010 Journal Cancer Cell Int Section Body Doc Link PMC2984396 Disease Relevance 0.31 Pain Relevance 0
Osteopontin (Opn), also known as early T cell activation gene-1, or eta-1, is a secreted, acidic glycoprotein with pleiotropic effects.
Localization (secreted) of eta-1 in T cell
2) Confidence 0.76 Published 2010 Journal Cancer Cell Int Section Body Doc Link PMC2984396 Disease Relevance 0.25 Pain Relevance 0
Osteopontin (Opn), also known as early T cell activation gene-1, or eta-1, is a secreted, acidic glycoprotein with pleiotropic effects.
Localization (secreted) of Opn in T cell
3) Confidence 0.76 Published 2010 Journal Cancer Cell Int Section Body Doc Link PMC2984396 Disease Relevance 0.31 Pain Relevance 0
We suggest that the potential mislocalization of OPN and potential reduction in secreted OPN in these cells may lead to protein complexes, which alter signaling pathways and increase the migratory behavior of the cells.
Localization (mislocalization) of OPN
4) Confidence 0.70 Published 2004 Journal Breast Cancer Res Section Body Doc Link PMC400667 Disease Relevance 0.41 Pain Relevance 0
We suggest that the potential mislocalization of OPN and potential reduction in secreted OPN in these cells may lead to protein complexes, which alter signaling pathways and increase the migratory behavior of the cells.
Localization (secreted) of OPN
5) Confidence 0.70 Published 2004 Journal Breast Cancer Res Section Body Doc Link PMC400667 Disease Relevance 0.40 Pain Relevance 0
This showed that OPN was localized in the lumen and at the luminal membrane of alveolar cells and ductal cells (data not shown).
Localization (localized) of OPN in lumen
6) Confidence 0.70 Published 2004 Journal Breast Cancer Res Section Body Doc Link PMC400667 Disease Relevance 1.42 Pain Relevance 0
To determine whether OPN is released by pulmonary cells upon stimulation with B. pseudomallei, we incubated murine alveolar macrophage MHS and lung epithelial MLE-15 cells with medium or heat-killed B. pseudomallei (MOI 1?
Localization (released) of OPN in lung
7) Confidence 0.69 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2930856 Disease Relevance 0.56 Pain Relevance 0
Using this model we confirmed increased release of OPN in the circulation and the lungs in mice and identified alveolar macrophages and respiratory epithelial cells as potential cellular sources for OPN upon infection with B. pseudomallei.
Localization (release) of OPN in alveolar macrophages associated with infection
8) Confidence 0.69 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2930856 Disease Relevance 1.03 Pain Relevance 0
These data support our immunohistochemistry observations that OPN may be mislocalized and preferentially sequestered in the cytoplasm.
Localization (sequestered) of OPN
9) Confidence 0.65 Published 2004 Journal Breast Cancer Res Section Body Doc Link PMC400667 Disease Relevance 0.43 Pain Relevance 0
These data support our immunohistochemistry observations that OPN may be mislocalized and preferentially sequestered in the cytoplasm.
Localization (mislocalized) of OPN
10) Confidence 0.65 Published 2004 Journal Breast Cancer Res Section Body Doc Link PMC400667 Disease Relevance 0.43 Pain Relevance 0
With regard to its role in cancer, previous studies have shown OPN to be a secreted, integrin-binding glycophosphoprotein whose plasma concentrations are elevated in metastatic breast cancer and are associated with increased tumor burden and decreased survival [39].
Localization (secreted) of OPN in plasma associated with cancer and advanced or metastatic breast cancer
11) Confidence 0.65 Published 2004 Journal Breast Cancer Res Section Body Doc Link PMC400667 Disease Relevance 0.82 Pain Relevance 0
Clinical relevance of OPN in diabetes
Localization (relevance) of OPN associated with diabetes mellitus
12) Confidence 0.65 Published 2010 Journal Cardiovasc Diabetol Section Body Doc Link PMC2988001 Disease Relevance 1.83 Pain Relevance 0.17
OPN release by both alveolar macrophages and epithelial cells was significantly enhanced upon B. pseudomallei stimulation in a dose dependent manner compared to the medium control (MHS: P<0.05 for both MOI, MLE-15: P?
Localization (release) of OPN in epithelial cells
13) Confidence 0.65 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2930856 Disease Relevance 0.66 Pain Relevance 0
We have shown that osteopontin (OPN), a secreted inflammatory glycophosphoprotein, plays a pivotal role in cardiac fibrosis (11) and is often increased in the tissues of diabetic mouse models (11–13).
Localization (secreted) of osteopontin associated with fibrosis, inflammation, diabetes mellitus and cardiovascular disorder under development
14) Confidence 0.56 Published 2008 Journal Diabetes Section Body Doc Link PMC2518499 Disease Relevance 1.73 Pain Relevance 0.29
Cells over-expressing 12/15LO secreted two potent chemokines, MCP-1 and osteopontin, implicated in the development of insulin resistance.
Localization (secreted) of osteopontin associated with chemokine and insulin resistance
15) Confidence 0.52 Published 2009 Journal PLoS ONE Section Abstract Doc Link PMC2746280 Disease Relevance 1.62 Pain Relevance 0.37
We have shown that osteopontin (OPN), a secreted inflammatory glycophosphoprotein, plays a pivotal role in cardiac fibrosis (11) and is often increased in the tissues of diabetic mouse models (11–13).
Localization (secreted) of OPN associated with fibrosis, inflammation, diabetes mellitus and cardiovascular disorder under development
16) Confidence 0.49 Published 2008 Journal Diabetes Section Body Doc Link PMC2518499 Disease Relevance 1.72 Pain Relevance 0.29
Furthermore, our ability to reverse the enhancement of implant size by treatment with the cleaved form of OPN that is released upon treatment with thrombin, strongly indicates that thrombin likely exerts its regulatory activity through interaction with OPN on stroma cells, as previously shown for maintenance of the blood tissue size under normal steady state hoemostasis[9], [10].


Localization (released) of OPN in stroma
17) Confidence 0.29 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2791444 Disease Relevance 0.19 Pain Relevance 0
Thrombin can also affect cells indirectly by cleaving OPN which is a secreted, multifunctional glycoprotein that exists either as a full-length molecule or as proteolytically cleaved fragments.
Localization (secreted) of OPN
18) Confidence 0.27 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2791444 Disease Relevance 0 Pain Relevance 0
Using this model we confirmed increased release of OPN in the circulation and the lungs in mice and identified alveolar macrophages and respiratory epithelial cells as potential cellular sources for OPN upon infection with B. pseudomallei.
Localization (release) of OPN in respiratory associated with infection
19) Confidence 0.24 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2930856 Disease Relevance 1.03 Pain Relevance 0
OPN release by both alveolar macrophages and epithelial cells was significantly enhanced upon B. pseudomallei stimulation in a dose dependent manner compared to the medium control (MHS: P<0.05 for both MOI, MLE-15: P?
Localization (release) of OPN in alveolar macrophages
20) Confidence 0.22 Published 2010 Journal PLoS Neglected Tropical Diseases Section Body Doc Link PMC2930856 Disease Relevance 0.66 Pain Relevance 0

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