INT171233

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Context Info
Confidence 0.07
First Reported 2002
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 25
Total Number 25
Disease Relevance 12.41
Pain Relevance 3.36

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

signal transduction (Ecm1) extracellular space (Ecm1) extracellular region (Ecm1)
proteinaceous extracellular matrix (Ecm1) enzyme binding (Ecm1) signal transducer activity (Ecm1)
Anatomy Link Frequency
extracellular matrix 3
neurons 2
lung 2
sensory neurons 1
hepatocyte 1
Ecm1 (Mus musculus)
Pain Link Frequency Relevance Heat
cytokine 64 100.00 Very High Very High Very High
chemokine 30 100.00 Very High Very High Very High
Bile 53 99.88 Very High Very High Very High
metalloproteinase 128 99.70 Very High Very High Very High
Mechanotransduction 106 98.60 Very High Very High Very High
Action potential 230 98.32 Very High Very High Very High
TRP channel 5 96.72 Very High Very High Very High
Central nervous system 12 89.52 High High
Inflammatory response 24 87.56 High High
dorsal root ganglion 90 87.04 High High
Disease Link Frequency Relevance Heat
Cancer 293 100.00 Very High Very High Very High
Glioma 113 100.00 Very High Very High Very High
Disease 34 99.96 Very High Very High Very High
Pulmonary Disease 234 98.98 Very High Very High Very High
Pulmonary Emphysema 6 98.72 Very High Very High Very High
Malignant Neoplastic Disease 19 98.48 Very High Very High Very High
Cholangiocarcinoma 1 98.12 Very High Very High Very High
Injury 164 98.06 Very High Very High Very High
Death 15 97.96 Very High Very High Very High
Adhesions 118 97.48 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Taken together, these data and our results confirm the critical role of aggrecanases in cartilage destruction and suggest that a controlled level of MMP-mediated aggrecanolysis may be needed for cartilage homeostasis, and possibly repair, as MMPs proteolysis can facilitate cell migration, regulate tissue architecture, release and activate ECM bound growth factors and signaling molecules49.
ECM Binding (bound) of in cartilage associated with metalloproteinase
1) Confidence 0.07 Published 2009 Journal Osteoarthritis Cartilage Section Body Doc Link PMC2706394 Disease Relevance 0.29 Pain Relevance 0.35
It has been shown that the transmission of forces between the skeletal muscle and tendon depends on the interaction of the muscle fibres with the surrounding ECM and also on the collagen fibrillar organization of the tendon (37).
ECM Binding (interaction) of in muscle
2) Confidence 0.07 Published 2010 Journal Human Molecular Genetics Section Body Doc Link PMC2792148 Disease Relevance 0.49 Pain Relevance 0
In contrast, the wound assay allows for cell movement to be assessed in the absence of disruption of cell-cell or cell-ECM interactions and thus allows migration of a connected population of cells to be measured.
ECM Binding (interactions) of associated with injury
3) Confidence 0.05 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2954173 Disease Relevance 1.24 Pain Relevance 0.03
In addition, in disorders such as Alzheimer's disease, alterations in the ECM may be related to diminished synaptic plasticity and therefore play a role in cognitive dysfunction.
ECM Binding (alterations) of associated with cognitive disorder and disease
4) Confidence 0.05 Published 2005 Journal BMC Neurosci Section Body Doc Link PMC1199600 Disease Relevance 0.20 Pain Relevance 0.19
Growth factor availability can also be regulated by binding to ECM components [36].
ECM Binding (binding) of
5) Confidence 0.04 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC535545 Disease Relevance 0.18 Pain Relevance 0
As well as providing a dynamic structural framework, the ECM of the endometrium interacts with its associated cells to mediate critical processes, including adhesion, migration and differentiation (reviewed in [35]).
ECM Binding (interacts) of in endometrium associated with adhesions
6) Confidence 0.04 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC535545 Disease Relevance 0.19 Pain Relevance 0
It associates with FN and a variety of other ECM proteins including laminin and fibrinogen [13].
ECM Binding (associates) of
7) Confidence 0.04 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2954173 Disease Relevance 0.58 Pain Relevance 0.04
Furthermore, interactions between integrins expressed by glioma cells and the ECM and the activity of MMPs form the basis for glioma cell migration and invasion [17].
ECM Binding (interactions) of associated with metalloproteinase and glioma
8) Confidence 0.04 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2904700 Disease Relevance 1.31 Pain Relevance 0.21
Integrins directly bind components of the ECM and provide the traction necessary for cell motility and invasion.
ECM Binding (bind) of
9) Confidence 0.03 Published 2010 Journal PLoS ONE Section Body Doc Link PMC2904700 Disease Relevance 1.38 Pain Relevance 0.15
Many of these steps involve dynamic interactions between tumor cells, stromal cells, and the extracellular matrix (ECM) [7].
ECM Binding (interactions) of in ECM associated with cancer
10) Confidence 0.03 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2680032 Disease Relevance 0.92 Pain Relevance 0
Thus the high levels of HA in COPD subjects would be a consequence of degradation of ECM, which in turn can bind to lung elastic fibers, thereby adaptively preventing their further degradation by protease (Cantor et al 1997, 2000).
ECM Binding (bind) of in lung associated with pulmonary disease
11) Confidence 0.03 Published 2007 Journal International Journal of Chronic Obstructive Pulmonary Disease Section Body Doc Link PMC2695202 Disease Relevance 0.85 Pain Relevance 0.12
Integrins are transmembrane receptor molecules that are responsible for the interaction of endothelial and tumor cells with the ECM.
ECM Binding (interaction) of associated with cancer
12) Confidence 0.03 Published 2010 Journal Aging (Albany NY) Section Body Doc Link PMC3006022 Disease Relevance 1.41 Pain Relevance 0
The thrombospondins (TSPs) are multifunctional matricellular proteins; TSP-1 and TSP-2 have strong anti-angiogenic properties, are present in a number of tissues where they bind to the extracellular matrix (ECM) and, in turn, are themselves able to bind receptors, enzymes, cytokines, proteases, and other ECM proteins [1-6].
ECM Binding (bind) of in extracellular matrix associated with cytokine
13) Confidence 0.03 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2575610 Disease Relevance 0.08 Pain Relevance 0.14
The thrombospondins (TSPs) are multifunctional matricellular proteins; TSP-1 and TSP-2 have strong anti-angiogenic properties, are present in a number of tissues where they bind to the extracellular matrix (ECM) and, in turn, are themselves able to bind receptors, enzymes, cytokines, proteases, and other ECM proteins [1-6].
ECM Binding (bind) of in extracellular matrix associated with cytokine
14) Confidence 0.03 Published 2008 Journal Arthritis Res Ther Section Body Doc Link PMC2575610 Disease Relevance 0.08 Pain Relevance 0.13
BDL: bile duct ligation; ECM: extracellular matrix; ERK: extracellular signal-regulated kinase; GAG: glycosaminoglycans; HGF: hepatocyte growth factor; HSC: hepatic stellate cell; HDL: high-density lipoprotein; HIF: hypoxia-inducible factor; IGF: insulin-like growth factor; IL: interleukin; iNOS: inducible nitric oxide synthase; IFN?
ECM Binding (ligation) of in hepatocyte associated with bile, cirrhosis, hypoxia and disorder of lipid metabolism
15) Confidence 0.02 Published 2008 Journal Fibrogenesis Tissue Repair Section Body Doc Link PMC2637833 Disease Relevance 0.99 Pain Relevance 0.26
GnRH neuronal migration is cell autonomous but modulated by composition of the ECM
ECM Binding (composition) of in neuronal
16) Confidence 0.02 Published 2002 Journal BMC Dev Biol Section Body Doc Link PMC65692 Disease Relevance 0 Pain Relevance 0
We hypothesize that the serine protease/inhibitor pair act by altering the ECM through which GnRH neurons migrate.
ECM Binding (altering) of in neurons
17) Confidence 0.02 Published 2002 Journal BMC Dev Biol Section Body Doc Link PMC65692 Disease Relevance 0 Pain Relevance 0
Gene expression analysis revealed an association of several secreted factors including colony stimulatory factors, cytokines and chemokines, acute phase proteins, angiogenesis factors and ECM modifying proteins with the 4T1 metastatic phenotype.
ECM Binding (association) of in 4T1 associated with chemokine and cytokine
18) Confidence 0.02 Published 2008 Journal BMC Cancer Section Abstract Doc Link PMC2529338 Disease Relevance 1.22 Pain Relevance 0.13
MMPs-1, -2, and -9 bind to various ECM proteins, which may increase the retention, stability, and bioactivity of proteinases in the lung and facilitate their roles in extracellular proteolysis (Murphy et al 1992; Allan et al 1995).


ECM Binding (bind) of in lung associated with metalloproteinase
19) Confidence 0.01 Published 2008 Journal International Journal of Chronic Obstructive Pulmonary Disease Section Body Doc Link PMC2629972 Disease Relevance 0.23 Pain Relevance 0.11
The neurons in these cultures also exhibited a lower threshold of stretch-activated action potentials when compared to neurons cultured upon a poly-L-lysine coating, implying that cell-ECM interactions are extremely important in neural mechanotransduction.
ECM Binding (interactions) of in neurons associated with action potential and mechanotransduction
20) Confidence 0.01 Published 2009 Journal PLoS ONE Section Body Doc Link PMC2627935 Disease Relevance 0 Pain Relevance 0.20

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