INT234952

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Context Info
Confidence 0.96
First Reported 2008
Last Reported 2008
Negated 1
Speculated 0
Reported most in Body
Documents 3
Total Number 9
Disease Relevance 5.86
Pain Relevance 0.98

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

cytosol (DSG1) plasma membrane (DSG1)
Anatomy Link Frequency
cleavage 2
DSG1 (Homo sapiens)
Pain Link Frequency Relevance Heat
Chronic pancreatitis 105 90.20 High High
metalloproteinase 12 86.84 High High
Inflammatory mediators 2 48.76 Quite Low
Kinase C 26 5.00 Very Low Very Low Very Low
agonist 10 5.00 Very Low Very Low Very Low
corticosteroid 4 5.00 Very Low Very Low Very Low
addiction 4 5.00 Very Low Very Low Very Low
Pain 2 5.00 Very Low Very Low Very Low
imagery 2 5.00 Very Low Very Low Very Low
antagonist 2 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Pancreatitis 119 99.40 Very High Very High Very High
Streptococcus Infection 4 98.00 Very High Very High Very High
Adenocarcinoma 98 97.60 Very High Very High Very High
Pancreatic Cancer 266 96.20 Very High Very High Very High
Bullous Skin Disease 608 95.76 Very High Very High Very High
Acantholysis 130 92.28 High High
Erythema 2 92.28 High High
Fever 2 91.88 High High
Disease 50 88.28 High High
Skin Infection 8 82.84 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Proteolysis of Dsg1 resulted in a rapid degradation of recombinant Dsg1 into fragments undetectable by western blot.
Protein_catabolism (degradation) of Dsg1
1) Confidence 0.96 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2628383 Disease Relevance 0.23 Pain Relevance 0
Proteolysis of Dsg1 resulted in a rapid degradation of recombinant Dsg1 into fragments undetectable by western blot.
Protein_catabolism (Proteolysis) of Dsg1
2) Confidence 0.96 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2628383 Disease Relevance 0.23 Pain Relevance 0
Recombinant Dsg2 was also cleaved by hK7 in a time-dependent manner, however, in contrast to the complete proteolysis of Dsg1, the cleavage of Dsg2 resulted in distinct proteolytic fragments (Fig. 3B, left).
Protein_catabolism (proteolysis) of Dsg1 in cleavage
3) Confidence 0.96 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2628383 Disease Relevance 0.59 Pain Relevance 0.18
In support of an association between hK7 and the desmogleins, hK7 was able to proteolyze both Dsg1 and Dsg2.
Protein_catabolism (proteolyze) of Dsg1
4) Confidence 0.96 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2628383 Disease Relevance 0.23 Pain Relevance 0
Upon incubation with thermolysin-activated hK7, recombinant Dsg1 was rapidly degraded with little detectable protein remaining after 60 minutes (Fig. 3A, left).
Neg (little) Protein_catabolism (degraded) of Dsg1
5) Confidence 0.96 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2628383 Disease Relevance 0.77 Pain Relevance 0.26
The ability of hK7 to degrade Dsg1 and Dsg2 was investigated using in vitro degradation assays.
Protein_catabolism (degrade) of Dsg1
6) Confidence 0.63 Published 2008 Journal BMC Cancer Section Abstract Doc Link PMC2628383 Disease Relevance 0.49 Pain Relevance 0.07
hK7 cleaves both recombinant Dsg1 and Dsg2 in vitro
Protein_catabolism (cleaves) of Dsg1
7) Confidence 0.63 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2628383 Disease Relevance 0.91 Pain Relevance 0.31
Nevertheless, the fact that specific cleavage of Dsg 1 by staphylococcal exfoliative toxin in bullous impetigo is sufficient to cause a histologic phenotype comparable to PF (Amagai et al. 2000a; Hanakawa et al. 2002) indicates that, in principle, specific proteolysis could be an effective mechanism in pemphigus.


Protein_catabolism (cleavage) of Dsg in cleavage associated with streptococcus infection and bullous skin disease
8) Confidence 0.32 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 1.23 Pain Relevance 0.16
Most cases are caused by staphylococcal exfoliative toxin (ET), a serine protease, which has been shown to selectively cleave Dsg 1 between EC 3 and 4 in conformation-dependent manner, but not Dsg 3 or E-cadherin (TableĀ 1) (Amagai et al. 2000a, 2002; Hanakawa et al. 2002; Melish and Glasgow 1970).
Protein_catabolism (cleave) of Dsg
9) Confidence 0.32 Published 2008 Journal Histochem Cell Biol Section Body Doc Link PMC2413110 Disease Relevance 1.18 Pain Relevance 0

General Comments

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