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Cathepsin B activates human trypsinogen 1 but not proelastase 2 or procarboxypeptidase B

Lindkvist, Björn LU ; Fajardo, Ignacio ; Pejler, Gunnar and Borgström, Anders LU (2006) In Pancreatology 6(3). p.224-231
Abstract
Background/Aims: Activation of trypsinogen to trypsin is a crucial step in the development of acute pancreatitis. The cause of this activation is not known although suggested explanations include autoactivation, cathepsin B-mediated activation and activation by mast cell tryptase. The aim of this study was to investigate cathepsin B and tryptase activation of pancreatic zymogens. Methods: Trypsinogen-1, proelastase, and procarboxypeptidase B were purified from human pancreatic juice. Human cathepsin B and beta I- tryptase are commercial products. Activation and degradation of zymogens were measured by activity towards specific substrates for trypsin and pancreatic elastase, ELISAs for procarboxypeptidase B and its activation peptide, and a... (More)
Background/Aims: Activation of trypsinogen to trypsin is a crucial step in the development of acute pancreatitis. The cause of this activation is not known although suggested explanations include autoactivation, cathepsin B-mediated activation and activation by mast cell tryptase. The aim of this study was to investigate cathepsin B and tryptase activation of pancreatic zymogens. Methods: Trypsinogen-1, proelastase, and procarboxypeptidase B were purified from human pancreatic juice. Human cathepsin B and beta I- tryptase are commercial products. Activation and degradation of zymogens were measured by activity towards specific substrates for trypsin and pancreatic elastase, ELISAs for procarboxypeptidase B and its activation peptide, and a radioimmunoassay for the trypsinogen activation peptide. Results: Cathepsin B caused activation of trypsinogen-1 with a trypsin yield of about 30% of that produced by enterokinase. Proelastase and procarboxypeptidase B was not activated by cathepsin B. None of the zymogens were inactivated by cathepsin B. Neither monomeric nor tetrameric tryptase could activate any of the examined zymogens. Conclusion: Cathepsin B is a competent activator of trypsinogen-1, although not as efficient as enterokinase. If cathepsin B is to play a role in protease activation in acute pancreatitis, this most probably occurs by activation of trypsinogen. (Less)
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author
; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
procarboxypeptidase B, proelastase, trypsinogen, cathepsin B, acute pancreatitis, tryptase
in
Pancreatology
volume
6
issue
3
pages
224 - 231
publisher
Karger
external identifiers
  • wos:000244257000012
  • scopus:33746355218
  • pmid:16534247
ISSN
1424-3903
DOI
10.1159/000091961
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Emergency medicine/Medicine/Surgery (013240200), Surgery Research Unit (013242220)
id
f096c31d-e4b1-450f-a71f-5f84b31e092f (old id 674455)
date added to LUP
2016-04-01 12:03:38
date last changed
2021-08-11 05:20:25
@article{f096c31d-e4b1-450f-a71f-5f84b31e092f,
  abstract     = {Background/Aims: Activation of trypsinogen to trypsin is a crucial step in the development of acute pancreatitis. The cause of this activation is not known although suggested explanations include autoactivation, cathepsin B-mediated activation and activation by mast cell tryptase. The aim of this study was to investigate cathepsin B and tryptase activation of pancreatic zymogens. Methods: Trypsinogen-1, proelastase, and procarboxypeptidase B were purified from human pancreatic juice. Human cathepsin B and beta I- tryptase are commercial products. Activation and degradation of zymogens were measured by activity towards specific substrates for trypsin and pancreatic elastase, ELISAs for procarboxypeptidase B and its activation peptide, and a radioimmunoassay for the trypsinogen activation peptide. Results: Cathepsin B caused activation of trypsinogen-1 with a trypsin yield of about 30% of that produced by enterokinase. Proelastase and procarboxypeptidase B was not activated by cathepsin B. None of the zymogens were inactivated by cathepsin B. Neither monomeric nor tetrameric tryptase could activate any of the examined zymogens. Conclusion: Cathepsin B is a competent activator of trypsinogen-1, although not as efficient as enterokinase. If cathepsin B is to play a role in protease activation in acute pancreatitis, this most probably occurs by activation of trypsinogen.},
  author       = {Lindkvist, Björn and Fajardo, Ignacio and Pejler, Gunnar and Borgström, Anders},
  issn         = {1424-3903},
  language     = {eng},
  number       = {3},
  pages        = {224--231},
  publisher    = {Karger},
  series       = {Pancreatology},
  title        = {Cathepsin B activates human trypsinogen 1 but not proelastase 2 or procarboxypeptidase B},
  url          = {http://dx.doi.org/10.1159/000091961},
  doi          = {10.1159/000091961},
  volume       = {6},
  year         = {2006},
}