INT35864

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Context Info
Confidence 0.61
First Reported 1984
Last Reported 2010
Negated 4
Speculated 0
Reported most in Abstract
Documents 19
Total Number 19
Disease Relevance 8.14
Pain Relevance 3.63

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 (PRSS1) extracellular space (PRSS1) extracellular region (PRSS1)
Anatomy Link Frequency
cleavage 2
exocrine pancreas 1
pancreas 1
platelet 1
urine 1
PRSS1 (Homo sapiens)
PRSS1 - E79K (1)
Pain Link Frequency Relevance Heat
Chronic pancreatitis 383 99.62 Very High Very High Very High
Lasting pain 4 94.12 High High
Cholecystokinin 4 93.00 High High
Inflammation 24 89.64 High High
agonist 6 88.08 High High
fibrosis 51 87.44 High High
alcohol 21 87.44 High High
Clonidine 4 87.04 High High
Opioid 2 75.00 Quite High
Bile 19 73.32 Quite High
Disease Link Frequency Relevance Heat
Pancreatic Cancer 69 100.00 Very High Very High Very High
Pancreatitis 535 99.62 Very High Very High Very High
Disease 81 99.00 Very High Very High Very High
Injury 10 98.40 Very High Very High Very High
Cancer 35 97.24 Very High Very High Very High
Sprains And Strains 40 96.64 Very High Very High Very High
Malaria 15 96.48 Very High Very High Very High
Diabetes Mellitus 26 95.00 High High
Pain 29 94.12 High High
INFLAMMATION 22 89.64 High High

Sentences Mentioned In

Key: Protein Mutation Event Anatomy Negation Speculation Pain term Disease term
Because increased autoactivation was observed with the R122H, N29I and N29T mutations, whereas N29I had no effect on trypsin stability, the logical conclusion was put forth that enhanced autoactivation is the common pathogenic mechanism of hereditary pancreatitis associated PRSS1 mutations [62].


Neg (no) Regulation (effect) of trypsin associated with pancreatitis
1) Confidence 0.61 Published 2007 Journal Orphanet J Rare Dis Section Body Doc Link PMC1774562 Disease Relevance 0.44 Pain Relevance 0
More importantly, the model fails to explain how the other pancreatitis associated PRSS1 mutations might work, as the majority of these do not affect trypsin stability.


Neg (not) Regulation (affect) of trypsin associated with pancreatitis
2) Confidence 0.61 Published 2007 Journal Orphanet J Rare Dis Section Body Doc Link PMC1774562 Disease Relevance 0.21 Pain Relevance 0
Several recent human genetic studies have provided insight into components of the pathogenic mechanisms leading to human CP, all of which are related to failure to regulate intrapancreatic trypsin activity and the associated pancreatic injury.
Regulation (regulate) of trypsin associated with injury and chronic pancreatitis
3) Confidence 0.61 Published 2008 Journal PLoS ONE Section Body Doc Link PMC2289874 Disease Relevance 1.67 Pain Relevance 1.18
To challenge this notion, here we describe the unique properties of the E79K cationic trypsinogen mutation (c.235G>A), which was identified in three European families affected by sporadic or familial pancreatitis cases.
Regulation (affected) of cationic trypsinogen (E79K) associated with pancreatitis
4) Confidence 0.45 Published 2004 Journal Hum. Mutat. Section Abstract Doc Link 14695529 Disease Relevance 0.58 Pain Relevance 0.08
In contrast to the mutations N29I, N29T and R122H, which are located away from this cleavage site, trypsinogen mutations affecting the K23-I24 bond could potentially affect the cathepsin B action on trypsinogen activation.
Regulation (affecting) of trypsinogen in cleavage
5) Confidence 0.44 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.29 Pain Relevance 0.07
A novel A121T mutation in human cationic trypsinogen associated with hereditary pancreatitis: functional data indicating a loss-of-function mutation influencing the R122 trypsin cleavage site.
Regulation (influencing) of trypsin in cleavage associated with pancreatitis
6) Confidence 0.40 Published 2008 Journal J. Med. Genet. Section Title Doc Link 18511571 Disease Relevance 0.20 Pain Relevance 0.10
The recent discovery that mutations in the trypsinogen gene are responsible for acute and chronic pancreatitis, and that patients with hereditary pancreatitis are at great risk for pancreatic cancer, has opened the door to understanding many aspects of pancreatic disease.
Regulation (responsible) of trypsinogen gene associated with pancreatic cancer, pancreatitis and chronic pancreatitis
7) Confidence 0.39 Published 1999 Journal Curr Gastroenterol Rep Section Abstract Doc Link 10980943 Disease Relevance 0.69 Pain Relevance 0.17
Twenty microlitres of different pruritogenic substances [histamine, substance P, neurokinin A, neurokinin B, trypsin, platelet-activating factor (PAF) and serotonin] and saline as control were injected intradermally into the inflamed test sites and in corresponding non-treated sites on the opposite forearm.
Regulation (control) of trypsin in platelet
8) Confidence 0.27 Published 2002 Journal Br. J. Dermatol. Section Body Doc Link 12000375 Disease Relevance 0.08 Pain Relevance 0
Biochemical characterization of the N29I mutation using recombinant trypsinogen found no effect on trypsin or trypsinogen stability.
Neg (no) Regulation (effect) of trypsin
9) Confidence 0.27 Published 2007 Journal Orphanet J Rare Dis Section Body Doc Link PMC1774562 Disease Relevance 0.20 Pain Relevance 0
Effect of trypsin on the hormonal regulation of the fat-stimulated human exocrine pancreas.
Regulation (Effect) of trypsin in exocrine pancreas
10) Confidence 0.25 Published 1988 Journal Scand. J. Gastroenterol. Section Title Doc Link 3227303 Disease Relevance 0.15 Pain Relevance 0.26
BACKGROUND: Chronic pancreatitis shows alterations in the trypsinogen gene (protease serine 1, PRSS1) in some individuals.
Regulation (alterations) of PRSS1 associated with chronic pancreatitis
11) Confidence 0.18 Published 2008 Journal HBPD INT Section Abstract Doc Link 18522894 Disease Relevance 0.27 Pain Relevance 0.26
Mild variations in the glomerular function seem to be able to influence serum trypsinogen 1 levels.
Regulation (influence) of trypsinogen 1
12) Confidence 0.16 Published 1988 Journal Pancreas Section Abstract Doc Link 3362841 Disease Relevance 0.37 Pain Relevance 0.07
In order to investigate the role of renal factors in affecting trypsinogen 1 metabolism and excretion in chronic pancreatic disease, serum immunoreactive trypsin (IRT), urinary IRT, gamma-glutamyltransferase (GGT), alpha-glucosidase (AGL) and RNase outputs and the molecular size distribution of serum and urine IRT were studied in 8 control subjects, 18 cases with pancreatic cancer, and 23 cases with chronic pancreatitis.
Regulation (affecting) of trypsinogen 1 in urine associated with pancreatic cancer, pancreatitis and chronic pancreatitis
13) Confidence 0.08 Published 1988 Journal Pancreas Section Abstract Doc Link 3362841 Disease Relevance 0.35 Pain Relevance 0.09
In contrast to pancreatic trypsin, trypsin IV was completely resistant to inhibition by polypeptide inhibitors.
Regulation (resistant) of trypsin
14) Confidence 0.07 Published 2004 Journal J. Biol. Chem. Section Abstract Doc Link 14726524 Disease Relevance 0.11 Pain Relevance 0.27
In addition, five down-regulated proteins identified in pancreatic cancer juice (carboxypeptidase A2, chymotrypsinogen B, elastase-3A, elastase-3B and trypsin-1) was also down-regulated in pancreatic cancer tissues compared with pancreatitis and normal pancreas tissues as described by Shen et al. [9].
Regulation (regulated) of trypsin in pancreas associated with pancreatitis and pancreatic cancer
15) Confidence 0.05 Published 2008 Journal BMC Cancer Section Body Doc Link PMC2528014 Disease Relevance 1.38 Pain Relevance 0
Genetic factors determining susceptibility to chronic pancreatitis can be classified in two groups: 1. rare gene mutations affecting the cationic trypsinogen gene that directly cause the disease, and 2. genetic variants that increase the risk for chronic pancreatitis but require additional risk factors to precipitate the disease.
Regulation (affecting) of trypsinogen gene associated with disease and chronic pancreatitis
16) Confidence 0.03 Published 2008 Journal Orv Hetil Section Abstract Doc Link 18755660 Disease Relevance 0.90 Pain Relevance 0.57
Of the pure enzymes, the quickest hydrolysis of the peptides was observed for the pancreatic enzymes chymotrypsin, trypsin and carboxypeptidase A.
Regulation (hydrolysis) of trypsin
17) Confidence 0.02 Published 2000 Journal J. Pharm. Pharmacol. Section Abstract Doc Link 10933129 Disease Relevance 0 Pain Relevance 0.14
The new compound is thermostable, not affected by proteolytic enzymes, such as trypsin, chymotrypsin, pronase, papain and pyroglutamase, or by boiling in 0.2 M HCl for 5 min.
Neg (not) Regulation (affected) of trypsin
18) Confidence 0.02 Published 1984 Journal Eur. J. Biochem. Section Abstract Doc Link 6092070 Disease Relevance 0 Pain Relevance 0.36
However, some malaria strains exhibit sialic acid-independent invasion [6]–[8], which is not affected by the absence of glycophorin A or B [6] or by antibodies against glycophorin A [7], but it is trypsin sensitive [6], [9], [10].
Regulation (sensitive) of trypsin associated with malaria and sprains and strains
19) Confidence 0.00 Published 2010 Journal PLoS Pathogens Section Body Doc Link PMC2887475 Disease Relevance 0.26 Pain Relevance 0

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