INT226478

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Context Info
Confidence 0.85
First Reported 2008
Last Reported 2010
Negated 0
Speculated 0
Reported most in Body
Documents 11
Total Number 12
Disease Relevance 5.52
Pain Relevance 0.95

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

peptidase activity (DPP4) extracellular region (DPP4) cell adhesion (DPP4)
Golgi apparatus (DPP4) endoplasmic reticulum (DPP4) plasma membrane (DPP4)
Anatomy Link Frequency
stromal cell 1
monocytes 1
liver 1
cleavage 1
body 1
DPP4 (Homo sapiens)
Pain Link Frequency Relevance Heat
chemokine 31 98.64 Very High Very High Very High
agonist 107 96.20 Very High Very High Very High
Inflammation 132 86.52 High High
Central nervous system 7 85.48 High High
antagonist 44 63.16 Quite High
rheumatoid arthritis 8 30.16 Quite Low
Neurotransmitter 4 16.56 Low Low
cytokine 97 5.00 Very Low Very Low Very Low
Neuropeptide 20 5.00 Very Low Very Low Very Low
headache 18 5.00 Very Low Very Low Very Low
Disease Link Frequency Relevance Heat
Diabetes Mellitus 386 99.32 Very High Very High Very High
Myocardial Infarction 7 99.20 Very High Very High Very High
Coronary Artery Disease 5 95.96 Very High Very High Very High
Asthma 359 93.68 High High
Weight Loss 32 87.04 High High
INFLAMMATION 137 86.52 High High
Gastric Motility Disorder 2 82.72 Quite High
Hypoglycemia 41 78.00 Quite High
Apoptosis 13 77.40 Quite High
Disease 52 72.56 Quite High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
In April 2005, the US Food and Drug Administration (FDA) approved the first incretin mimetic, exenatide, a GLP-1 receptor analogue which is resistant to DPP-4 degradation.
Protein_catabolism (degradation) of DPP-4
1) Confidence 0.85 Published 2008 Journal Vascular Health and Risk Management Section Body Doc Link PMC2597770 Disease Relevance 0.50 Pain Relevance 0.04
GLP-1 is degraded rapidly by the ubiquitous enzyme dipeptidyl-peptidase IV (DPP-4).
Protein_catabolism (degraded) of DPP-4
2) Confidence 0.67 Published 2010 Journal Pediatr Nephrol Section Body Doc Link PMC2874027 Disease Relevance 0.68 Pain Relevance 0.09
GLP-1 is degraded rapidly by the ubiquitous enzyme dipeptidyl-peptidase IV (DPP-4).
Protein_catabolism (degraded) of dipeptidyl-peptidase IV
3) Confidence 0.67 Published 2010 Journal Pediatr Nephrol Section Body Doc Link PMC2874027 Disease Relevance 0.68 Pain Relevance 0.09
In contrast to naturally occurring CCL11, NNY-CCL14 is resistant to degradation by CD26/dipeptidyl peptidase IV (DP4).
Protein_catabolism (degradation) of CD26
4) Confidence 0.64 Published 2008 Journal J Occup Med Toxicol Section Body Doc Link PMC2259400 Disease Relevance 0.27 Pain Relevance 0.10
DPP IV degrades interferon (IFN) gamma - induced chemokines, CCL3, CCL5 (RANTES), CCL11, CCL22, and CXCL12 (stromal cell-derived factor-1 alpha; SDF-1?).
Protein_catabolism (degrades) of DPP IV in stromal cell associated with chemokine
5) Confidence 0.61 Published 2010 Journal Allergy Asthma Clin Immunol Section Body Doc Link PMC2877018 Disease Relevance 0.44 Pain Relevance 0.16
DPP IV cleavage of the N-terminal dipeptide from CCL5 enhanced chemotaxis of T cells, but not monocytes, in vitro [41].
Protein_catabolism (cleavage) of DPP IV in monocytes
6) Confidence 0.61 Published 2010 Journal Allergy Asthma Clin Immunol Section Body Doc Link PMC2877018 Disease Relevance 0.41 Pain Relevance 0.18
These comprise the injectable GLP-1 receptor agonists solely acting on the GLP-1 receptor on the one hand and orally active dipeptidyl-peptidase inhibitors (DPP-4 inhibitors) raising endogenous GLP-1 and other hormone levels by inhibiting the degrading enzyme DPP-4.
Protein_catabolism (degrading) of DPP-4 associated with agonist
7) Confidence 0.50 Published 2010 Journal Pediatr Nephrol Section Abstract Doc Link PMC2874027 Disease Relevance 0.32 Pain Relevance 0.09
This structural change results in slow release from the injection site and decreased susceptibility to degradation by DPP-IV when in the circulation.
Protein_catabolism (degradation) of DPP-IV
8) Confidence 0.46 Published 2010 Journal British Journal of Clinical Pharmacology Section Body Doc Link PMC2997321 Disease Relevance 0.80 Pain Relevance 0
Through preventing the rapid degradation of incretin hormones, DPP-4 inhibitors result in postprandial increases in levels of biologically active intact GLP-1 and reduce glucose production from the liver by inhibition of glucagon from the ?
Protein_catabolism (degradation) of DPP-4 in liver
9) Confidence 0.43 Published 2008 Journal Vascular Health and Risk Management Section Body Doc Link PMC2597770 Disease Relevance 0.07 Pain Relevance 0
Thereby liraglutide is fully metabolized in the body by sequential cleavage of small peptide fragments and amino acids, which involves DPP-IV and neutral endopeptidase (NEP), and clearance of liraglutide is suggested to take place by multiple organ/tissues (EMEA/379172/2009).
Protein_catabolism (cleavage) of DPP-IV in body
10) Confidence 0.34 Published 2010 Journal British Journal of Clinical Pharmacology Section Body Doc Link PMC2997321 Disease Relevance 0.52 Pain Relevance 0
Because of the rapid proteolysis of GLP-1 by DPP-4, the native peptide is not suitable for therapeutic use.
Protein_catabolism (proteolysis) of DPP-4
11) Confidence 0.32 Published 2010 Journal International Journal of Clinical Practice Section Body Doc Link PMC2904489 Disease Relevance 0.47 Pain Relevance 0.13
In addition to cleavage of GLP-1, DPP-4 has been shown to cleave multiple substrates in vitro, but few of these substrates have been validated as physiological substrates in humans.
Protein_catabolism (cleavage) of DPP-4 in cleavage
12) Confidence 0.32 Published 2010 Journal International Journal of Clinical Practice Section Body Doc Link PMC2904489 Disease Relevance 0.35 Pain Relevance 0.07

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