INT337008

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Context Info
Confidence 0.20
First Reported 2010
Last Reported 2010
Negated 0
Speculated 1
Reported most in Body
Documents 2
Total Number 10
Disease Relevance 4.91
Pain Relevance 0.81

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

unfolded protein binding (HSP90B1) protein folding (HSP90B1) cytosol (HSP90B1)
endoplasmic reticulum (HSP90B1) RNA binding (HSP90B1) response to stress (HSP90B1)
Anatomy Link Frequency
plasma 2
Caco-2 1
epithelial cells 1
gut 1
HSP90B1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Crohn's disease 459 98.22 Very High Very High Very High
Inflammation 45 97.36 Very High Very High Very High
cytokine 27 45.36 Quite Low
Opioid 1 44.88 Quite Low
rheumatoid arthritis 9 31.12 Quite Low
chemokine 2 31.04 Quite Low
Inflammatory response 9 5.00 Very Low Very Low Very Low
abdominal pain 9 5.00 Very Low Very Low Very Low
Dopamine 3 5.00 Very Low Very Low Very Low
agonist 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Sprains And Strains 243 99.00 Very High Very High Very High
Meningitis 27 98.96 Very High Very High Very High
Disease 495 98.22 Very High Very High Very High
INFLAMMATION 45 97.36 Very High Very High Very High
Targeted Disruption 18 94.34 High High
Infection 72 90.48 High High
Stress 153 87.44 High High
Lymphatic System Cancer 9 59.24 Quite High
Adhesions 36 58.80 Quite High
Inflammatory Bowel Disease 108 48.68 Quite Low

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Therefore, in light of our findings, strategies to inhibit the OmpA–Gp96 interaction would be helpful to develop new treatment options for preventing inflammation resulting from gut mucosa invasion by AIEC but also by virulent bacteria using Gp96 as a host cell receptor.



Gp96 Binding (interaction) of in gut associated with inflammation
1) Confidence 0.20 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.50 Pain Relevance 0.21
In addition, confocal images indicated a recruitment or accumulation of Gp96 at the cell surface at the sites where the OMVs were observed.
Gp96 Binding (recruitment) of
2) Confidence 0.16 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.19 Pain Relevance 0.03
Since OmpA plays a major role in the ability of meningitis-associated E coli K1 to invade human BMECs via its binding to the Gp96 receptor,19 20 we investigated the role of OmpA in the ability of AIEC strain LF82 to invade IECs.
Gp96 Binding (binding) of associated with meningitis and sprains and strains
3) Confidence 0.16 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.76 Pain Relevance 0
Such a co-localisation of Gp96 and CEACAM6 in patients with CD at the apical side of ileal epithelial cells is of great interest, since we previously reported that CEACAM6 acts as a receptor for E coli type 1 pili and therefore allows AIEC to colonise the ileal mucosa12 and promote gut inflammation as shown in transgenic CEABAC10 mice expressing the human CEACAM6 molecule.46 Increased expression of Gp96 at the same site as CEACAM6 should increase AIEC virulence, since the bacteria would be able to colonise the mucosa by binding to CEACAM6 and can better invade the ileal epithelium through AIEC OMV–Gp96 interaction.
Gp96 Binding (interaction) of in epithelial cells associated with targeted disruption, inflammation and crohn's disease
4) Confidence 0.16 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.62 Pain Relevance 0.23
Gp96 has already been reported to be a key mediator of the innate immune response due to its ability to bind pathogenic bacteria or their products.19–21 37 38 Indeed, Gp96 is a plasma membrane receptor for Vip, a Listeria monocytogenes virulence factor that is required for cell invasion and downstream signalling events.21 In addition, a Gp96 homologue, Ecgp96, the expression of which is increased during meningitis-associated E coli K1 infection of human BMECs, promotes invasion of these pathogenic bacteria.19 20 37
Gp96 Binding (membrane receptor) of in plasma associated with meningitis and infection
5) Confidence 0.16 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.78 Pain Relevance 0.09
To investigate whether OmpA expressed by LF82 bacteria binds Gp96 receptor expressed by Caco-2 IECs, we used pull-down and a ligand overlay approach.
Gp96 Spec (whether) Binding (binds) of in Caco-2
6) Confidence 0.15 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.57 Pain Relevance 0
OmpA binds Gp96 and is involved in AIEC strain LF82 invasion ability
Gp96 Binding (binds) of associated with sprains and strains
7) Confidence 0.15 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.66 Pain Relevance 0
In addition, we can speculate that increased expression of Gp96 in patients with CD could also contribute to an abnormal colonisation of the mucosa by other bacteria using Gp96 as a plasma membrane receptor allowing the bacteria to bind to or to enter inside host cells, as already reported for L monocytogenes.21
Gp96 Binding (bind) of in plasma associated with crohn's disease
8) Confidence 0.14 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.68 Pain Relevance 0.26
min with anti-Gp96 (diluted 1:500), and next for 1?
Gp96 Binding (min) of
9) Confidence 0.14 Published 2010 Journal Gut Section Body Doc Link PMC2976078 Disease Relevance 0.16 Pain Relevance 0
Although interactions with calreticulin, PDI and GRP94 appear to be conserved through all receptor pairs, differences in the interaction pattern can be observed in the case of Bip, which interacts only with the ?
GRP94 Binding (interactions) of
10) Confidence 0.14 Published 2010 Journal J Mol Signal Section Body Doc Link PMC2954983 Disease Relevance 0 Pain Relevance 0

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