INT234872

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Context Info
Confidence 0.24
First Reported 2008
Last Reported 2009
Negated 0
Speculated 0
Reported most in Body
Documents 4
Total Number 4
Disease Relevance 3.12
Pain Relevance 0.49

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

nucleus (Hspb2) response to stress (Hspb2) cytoplasm (Hspb2)
Anatomy Link Frequency
filaments 2
monocyte 1
keratinocytes 1
Hspb2 (Mus musculus)
Pain Link Frequency Relevance Heat
Inflammatory response 3 96.08 Very High Very High Very High
cytokine 15 95.00 High High
rheumatoid arthritis 65 89.24 High High
Kinase C 39 75.48 Quite High
methotrexate 4 74.40 Quite High
Arthritis 64 70.76 Quite High
Inflammation 43 70.36 Quite High
metalloproteinase 19 5.00 Very Low Very Low Very Low
agonist 17 5.00 Very Low Very Low Very Low
corticosteroid 6 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Shock 7 100.00 Very High Very High Very High
Bullous Skin Disease 912 99.74 Very High Very High Very High
Mucocutaneous Lymph Node Syndrome 3 97.28 Very High Very High Very High
INFLAMMATION 20 96.08 Very High Very High Very High
Apoptosis 102 93.36 High High
Blister 36 91.20 High High
Rheumatoid Arthritis 65 89.24 High High
Acantholysis 195 81.60 Quite High
Adhesions 154 77.12 Quite High
Arthritis 62 70.76 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Once activated, MK5/PRAK was reported to directly phosphorylate heat shock protein 27 (Hsp27) [91, 92], the latter having been implicated in several physiologically relevant immune-mediated inflammatory responses such as CD8+ lymphocyte subset expansion and apoptosis resistance [93] as well as in the activation of the Toll-like receptor-4 in monocyte-derived RA DCs [94].
Phosphorylation (phosphorylate) of Hsp27 in monocyte associated with inflammatory response, shock, rheumatoid arthritis and apoptosis
1) Confidence 0.24 Published 2009 Journal Mediators of Inflammation Section Body Doc Link PMC2842969 Disease Relevance 0.63 Pain Relevance 0.39
However, because p38MAPK-mediated phosphorylation of HSP27 or HSP 25 promoted actin assembly and stabilized F-actin against depolymerization in response to cytochalasin D or heat shock (Benndorf et al. 1994; Geum et al. 2002; Guay et al. 1997), one would expect that PV-IgG-induced HSP27 phosphorylation also would stabilize actin filaments.
Phosphorylation (phosphorylation) of HSP27 in filaments associated with shock and bullous skin disease
2) Confidence 0.18 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.55 Pain Relevance 0
In cultured human keratinocytes, phosphorylation of p38MAPK and HSP27 occured after 30 min of exposure to PV-IgG (Berkowitz et al. 2005; Kawasaki et al. 2006).
Phosphorylation (phosphorylation) of HSP27 in keratinocytes associated with mucocutaneous lymph node syndrome and bullous skin disease
3) Confidence 0.18 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 1.43 Pain Relevance 0.10
However, because p38MAPK-mediated phosphorylation of HSP27 or HSP 25 promoted actin assembly and stabilized F-actin against depolymerization in response to cytochalasin D or heat shock (Benndorf et al. 1994; Geum et al. 2002; Guay et al. 1997), one would expect that PV-IgG-induced HSP27 phosphorylation also would stabilize actin filaments.
Phosphorylation (phosphorylation) of HSP27 in filaments associated with shock and bullous skin disease
4) Confidence 0.18 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 0.50 Pain Relevance 0

General Comments

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