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Extrapancreatic trypsin-2 cleaves proteinase-activated receptor-2.

Alm, Anna-Karin; Gagnemo Persson, Rebecca LU ; Sorsa, Timo and Sundelin, Johan (1999) In Biochemical and Biophysical Research Communications 275(1). p.77-83
Abstract
Proteinase-activated receptors (PARs) are activated by proteolytic removal of a short amino terminal peptide, thus exposing a new amino terminus that functions as a tethered ligand that activates the receptor. With the aim to identify and study potential activators of PAR-2 we have developed a new method to measure proteolytic cleavage of PARs. PAR-2 was tagged with the insulin C-peptide that upon receptor cleavage is released and quantified using an ELISA. The modified receptor, shown to be functional in mouse 3T3 cells, was expressed in an insect cell line and the ability of different proteinases to cleave PAR-2 was studied. Two different mast cell tryptases cleaved PAR-2 in a concentration dependent manner, but were much less potent... (More)
Proteinase-activated receptors (PARs) are activated by proteolytic removal of a short amino terminal peptide, thus exposing a new amino terminus that functions as a tethered ligand that activates the receptor. With the aim to identify and study potential activators of PAR-2 we have developed a new method to measure proteolytic cleavage of PARs. PAR-2 was tagged with the insulin C-peptide that upon receptor cleavage is released and quantified using an ELISA. The modified receptor, shown to be functional in mouse 3T3 cells, was expressed in an insect cell line and the ability of different proteinases to cleave PAR-2 was studied. Two different mast cell tryptases cleaved PAR-2 in a concentration dependent manner, but were much less potent than pancreatic trypsin and trypsin-2 isolated from a carcinoma cell line. Pancreatic trypsin and trypsin-2 were almost equally effective at cleaving PAR-2 suggesting that extrapancreatic trypsins are potential in vivo activators of PAR-2. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
proteinase-activated receptor-2; mast cell tryptase; trypsin-2
in
Biochemical and Biophysical Research Communications
volume
275
issue
1
pages
6 pages
publisher
Elsevier
external identifiers
  • Scopus:0034682915
ISSN
1090-2104
DOI
10.1006/bbrc.2000.3267
language
English
LU publication?
yes
id
165eef61-7487-48ff-8229-c0ec23ee6f58
date added to LUP
2016-08-19 14:31:22
date last changed
2016-10-13 05:12:39
@misc{165eef61-7487-48ff-8229-c0ec23ee6f58,
  abstract     = {Proteinase-activated receptors (PARs) are activated by proteolytic removal of a short amino terminal peptide, thus exposing a new amino terminus that functions as a tethered ligand that activates the receptor. With the aim to identify and study potential activators of PAR-2 we have developed a new method to measure proteolytic cleavage of PARs. PAR-2 was tagged with the insulin C-peptide that upon receptor cleavage is released and quantified using an ELISA. The modified receptor, shown to be functional in mouse 3T3 cells, was expressed in an insect cell line and the ability of different proteinases to cleave PAR-2 was studied. Two different mast cell tryptases cleaved PAR-2 in a concentration dependent manner, but were much less potent than pancreatic trypsin and trypsin-2 isolated from a carcinoma cell line. Pancreatic trypsin and trypsin-2 were almost equally effective at cleaving PAR-2 suggesting that extrapancreatic trypsins are potential in vivo activators of PAR-2.},
  author       = {Alm, Anna-Karin and Gagnemo Persson, Rebecca and Sorsa, Timo and Sundelin, Johan},
  issn         = {1090-2104},
  keyword      = {proteinase-activated receptor-2;  mast cell tryptase;  trypsin-2  },
  language     = {eng},
  number       = {1},
  pages        = {77--83},
  publisher    = {ARRAY(0x5708270)},
  series       = {Biochemical and Biophysical Research Communications},
  title        = {Extrapancreatic trypsin-2 cleaves proteinase-activated receptor-2.},
  url          = {http://dx.doi.org/10.1006/bbrc.2000.3267 },
  volume       = {275},
  year         = {1999},
}