INT72127

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Context Info
Confidence 0.52
First Reported 1997
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 68
Total Number 70
Disease Relevance 56.00
Pain Relevance 14.13

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

extracellular region (MMRN1) cell adhesion (MMRN1)
Anatomy Link Frequency
ECM 22
macrophages 2
brain 2
stroma 1
chondrocytes 1
MMRN1 (Homo sapiens)
Pain Link Frequency Relevance Heat
metalloproteinase 1597 99.98 Very High Very High Very High
Inflammation 655 99.96 Very High Very High Very High
Osteoarthritis 237 99.84 Very High Very High Very High
cytokine 558 99.76 Very High Very High Very High
Pain 99 99.28 Very High Very High Very High
fibrosis 59 98.08 Very High Very High Very High
Central nervous system 202 97.00 Very High Very High Very High
ischemia 14 95.48 Very High Very High Very High
rheumatoid arthritis 183 94.00 High High
Arthritis 8 92.32 High High
Disease Link Frequency Relevance Heat
Cancer 2976 100.00 Very High Very High Very High
Apoptosis 476 100.00 Very High Very High Very High
Fibrosis 83 100.00 Very High Very High Very High
Breast Cancer 230 99.96 Very High Very High Very High
Arthritis 24 99.96 Very High Very High Very High
Airway Remodeling 43 99.92 Very High Very High Very High
Osteoarthritis 204 99.84 Very High Very High Very High
Metastasis 584 99.76 Very High Very High Very High
Aging 120 99.74 Very High Very High Very High
Adhesions 298 99.60 Very High Very High Very High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
These findings confirmed our expectations of the brain's ECM undergoing degradation following HIV infection, and these changes may well underlie the neurological disturbances manifested in AIDS patients.
Protein_catabolism (degradation) of ECM in ECM associated with acquired immune deficiency syndrome or hiv infection and infection
1) Confidence 0.52 Published 1997 Journal Neurobiol. Dis. Section Abstract Doc Link 9361307 Disease Relevance 1.35 Pain Relevance 0
High levels of proteases facilitate ECM degrading, thereby creating a path for the migration of cancer cells.
Protein_catabolism (degrading) of ECM associated with cancer
2) Confidence 0.43 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 1.58 Pain Relevance 0.08
This progress would rely on invadopodia which are membrane protrusions that localize enzymes required for ECM degradation, and MMP9 would be required in the initial steps of invadopodia formation [20].
Protein_catabolism (degradation) of ECM
3) Confidence 0.43 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 1.69 Pain Relevance 0.07
Thus, we supposed that MMPs-mediated degradation of BM and ECM can act as both positive and negative regulators of tumor progression which resulted in the unexpected results predicted in the traditional view because of the change of the tumor stroma during the cancer progression.
Protein_catabolism (degradation) of ECM in stroma associated with cancer and metalloproteinase
4) Confidence 0.43 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 1.06 Pain Relevance 0.18
Nevertheless, the roles of proteases in cancer are now known to be much broader than simply degradation of ECM during tumor invasion and metastasis.
Protein_catabolism (degradation) of ECM associated with cancer and metastasis
5) Confidence 0.43 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 1.23 Pain Relevance 0.13
The proteolysis of ECM by MMPs may reveal cryptic matrix binding sites, MMPs can act as tumor suppressor by revealing cryptic matrix binding sites, releasing matrix-bound growth factors and activating a variety of cell surface molecules [22].
Protein_catabolism (proteolysis) of ECM associated with cancer and metalloproteinase
6) Confidence 0.33 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 1.26 Pain Relevance 0.13
Urokinase-type plasminogen activator (uPA), a serine protease, has similarly been implicated in the degradation of ECM.
Protein_catabolism (degradation) of ECM in ECM
7) Confidence 0.29 Published 2009 Journal Journal of Proteome Research Section Body Doc Link PMC2652408 Disease Relevance 1.14 Pain Relevance 0
Further more, the process of pericellular proteolysis leads to ECM degradation and realignment during cell movement and integrate it into established steps of cell migration [11].
Protein_catabolism (degradation) of ECM
8) Confidence 0.29 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 0.67 Pain Relevance 0.08
Cancer cells erase ECM everywhere without foci degraded matrix, like wave breaking the dike on the beach (Figure 4A &4B). 2.
Protein_catabolism (degraded) of ECM associated with cancer
9) Confidence 0.29 Published 2010 Journal J Transl Med Section Body Doc Link PMC2965128 Disease Relevance 0.49 Pain Relevance 0
For example, degradation of the extracellular matrix (ECM) is a key biological process that promotes the invasion of pancreatic tumors into their surrounding tissue.
Protein_catabolism (degradation) of ECM in ECM associated with pancreatic cancer
10) Confidence 0.25 Published 2009 Journal Journal of Proteome Research Section Body Doc Link PMC2652408 Disease Relevance 0.71 Pain Relevance 0
The cysteine protease cathepsin C and the aspartic protease cathepsin D have been implicated in ECM degradation, facilitating tumor growth, invasion and metastasis.
Protein_catabolism (degradation) of ECM in ECM associated with cancer and metastasis
11) Confidence 0.25 Published 2009 Journal Journal of Proteome Research Section Body Doc Link PMC2652408 Disease Relevance 0.83 Pain Relevance 0
In addition, MMP-12 can activate other MMPs, for example, MMP-2 and -3, leading to subsequent degradation of other ECM proteins [10].
Protein_catabolism (degradation) of ECM associated with metalloproteinase
12) Confidence 0.18 Published 2005 Journal Respir Res Section Body Doc Link PMC1363355 Disease Relevance 0.86 Pain Relevance 0.83
In fact, some members of the MMP family of proteases may associate with cell membrane receptors able to drive an oriented degradation of ECM and display a disintegrin region that, by virtue of an RGD motif, play a role in cell-cell adhesion and cell migration (ADAM proteinases: A Disintegrin And Metallo proteinase) [101].
Protein_catabolism (degradation) of ECM associated with metalloproteinase and adhesions
13) Confidence 0.18 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC320496 Disease Relevance 0.73 Pain Relevance 0.16
Plasmin is the main protease involved in (pro)-u-PA activation, which gives origin to the initiation of the classical protease cascade (plasmin, interstitial MMPs, MT1-MMP, Gelatinase A) leading to ECM degradation.
Protein_catabolism (degradation) of ECM associated with metalloproteinase
14) Confidence 0.18 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC320496 Disease Relevance 0.15 Pain Relevance 0.05
Three extracellular protein ligands involved in ECM degradation and cell adhesion have been identified for u-PAR, namely u-PA, vitronectin (VN), and kininogen.
Protein_catabolism (degradation) of ECM associated with adhesions
15) Confidence 0.18 Published 2004 Journal Reprod Biol Endocrinol Section Body Doc Link PMC320496 Disease Relevance 0.15 Pain Relevance 0.05
MMP-12 degrades a broad range of ECM proteins, including elastin, type IV collagen, fibronectin, laminin and gelatin [8,9], and is involved in turnover of the matrix, cell migration, tissue repairing and remodeling.
Protein_catabolism (degrades) of ECM associated with metalloproteinase
16) Confidence 0.16 Published 2005 Journal Respir Res Section Body Doc Link PMC1363355 Disease Relevance 0.59 Pain Relevance 0.76
Recovery from either acute or chronic liver injury in animal models is characterized by apoptosis of HSC/MFs, reduction of TIMP (tissue inhibitor of metalloproteinases) levels and progressive degradation of fibrillar fibrotic ECM.
Protein_catabolism (degradation) of ECM in liver associated with fibrosis, injury, metalloproteinase and apoptosis
17) Confidence 0.15 Published 2008 Journal Fibrogenesis Tissue Repair Section Body Doc Link PMC2584013 Disease Relevance 1.30 Pain Relevance 0.13
MMP degrade ECM, disengage integrins, and stimulate reparative fibrosis.
Protein_catabolism (degrade) of ECM in ECM associated with fibrosis and metalloproteinase
18) Confidence 0.15 Published 2010 Journal Stem Cells International Section Body Doc Link PMC2975079 Disease Relevance 1.03 Pain Relevance 0.60
Secretion of active MMP-9 by PC3 cells may offer a potential mechanistic explanation for the processes of ECM degradation and cell migration.
Protein_catabolism (degradation) of ECM
19) Confidence 0.15 Published 2007 Journal Mol Cancer Section Body Doc Link PMC1828067 Disease Relevance 0 Pain Relevance 0
MMP-12 may facilitate airway inflammation by stimulating migration of inflammatory cells such as monocytes and macrophages to inflammatory sites, and mediate airway remodeling by degrading ECM proteins through its enzymatic activity or through mediating inflammatory cytokines to induce other MMPs, including MMP-2, -9, -13 and -14, in lung [11].
Protein_catabolism (degrading) of ECM in monocytes associated with inflammation, metalloproteinase, airway remodeling and cytokine
20) Confidence 0.13 Published 2005 Journal Respir Res Section Body Doc Link PMC1363355 Disease Relevance 1.07 Pain Relevance 0.93

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