INT171651

Context Info Confidence 0.60 First Reported 2002 Last Reported 2002 Negated 1 Speculated 0 Reported most in Body Documents 1 Total Number 4 Disease Relevance 1.07 Pain Relevance 0.16

peptidase activity (PRSS1) extracellular space (PRSS1) extracellular region (PRSS1)

Anatomy Link Frequency D22 4 cleavage 2 PRSS1 (Homo sapiens)

Pain Link Frequency Relevance Heat Chronic pancreatitis 12 87.36

Disease Link Frequency Relevance Heat Pancreatitis 92 92.84 Disease 4 31.28

Sentences Mentioned In

Key:

Protein

Mutation

Event

Anatomy

Negation

Speculation

Pain term

Disease term

This indicates a high control of cathepsin B action on trypsinogen activation by the amino acid structure of TAP and highlights the particular functional importance of the D22 residue within the tetraaspartic group D19-D20-D21-D22.

Regulation (control) of Positive_regulation (activation) of trypsinogen in D22

1) Confidence 0.60 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.18 Pain Relevance 0

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 (affect) of Positive_regulation (activation) of trypsinogen in cleavage

2) Confidence 0.60 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.29 Pain Relevance 0.07

This indicates a high control of cathepsin B action on trypsinogen activation by the amino acid structure of TAP and highlights the particular functional importance of the D22 residue within the tetraaspartic group D19-D20-D21-D22.

Regulation (action) of Positive_regulation (activation) of trypsinogen in D22

3) Confidence 0.26 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.18 Pain Relevance 0

The investigation of the wild type trypsinogen molecule and three distinct mutants (i.e., N29I, N29T and R122H) found that cathepsin B mediated trypsinogen activation was not influenced by the respective mutants [8].

Neg (not) Regulation (influenced) of Positive_regulation (activation) of trypsinogen

4) Confidence 0.26 Published 2002 Journal BMC Gastroenterol Section Body Doc Link PMC117221 Disease Relevance 0.42 Pain Relevance 0.09

General Comments

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