Neutrophil elastase sorting involves plasma membrane trafficking requiring the C-terminal propeptide.
Tapper, Hans LU ; Källquist, Linda LU ; Johnsson, Ellinor LU ; Persson, Ann-Maj LU ; Hansson, Markus LU
and Olsson, Inge
LU
(2006)
In Experimental Cell Research
312(18).
p.3471-3484
- Abstract
- The primary granules/secretory lysosomes of neutrophils store mature neutrophil elastase (NE) as a luminal protein after proteolytic removal of N-terminal and C-terminal pro-peptides from a proform of NE. The N-terminal pro-peptide prevents premature activation that might be toxic to the cell, but the C-terminal pro-peptide has no defined function. In this study, we investigated the role of the C-terminal pro-peptide in trafficking of NE by expressing, in rat basophilic leukemia (RBL) cells, both wild-type NE and the mutant NE/Delta 248-267, which lacks the C-terminal pro-peptide. Both transfected proteins were found to be targeted to secretory lysosomes. in addition, results from antibody ligation and cell-surface biotinylation indicated... (More)
- The primary granules/secretory lysosomes of neutrophils store mature neutrophil elastase (NE) as a luminal protein after proteolytic removal of N-terminal and C-terminal pro-peptides from a proform of NE. The N-terminal pro-peptide prevents premature activation that might be toxic to the cell, but the C-terminal pro-peptide has no defined function. In this study, we investigated the role of the C-terminal pro-peptide in trafficking of NE by expressing, in rat basophilic leukemia (RBL) cells, both wild-type NE and the mutant NE/Delta 248-267, which lacks the C-terminal pro-peptide. Both transfected proteins were found to be targeted to secretory lysosomes. in addition, results from antibody ligation and cell-surface biotinylation indicated that proform of NE was targeted to the plasma membrane, and then subjected to endocytosis. The results were supported by the detection of targeting of the proform to the plasma membrane followed by internalization both in RBL cells and normal granulopoietic precursor cells. Targeting of NE to the plasma membrane required the C-terminal pro-peptide as NE/ Delta 248-267 expressed in RBL cells bypassed plasma membrane trafficking. our results indicate targeting of a population of NE to the plasma membrane and internalization dependent on the C-terminal NE pro-peptide. (c) 2006 Elsevier Inc. All rights reserved. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/161285
- author
- Tapper, Hans
LU
; Källquist, Linda
LU
; Johnsson, Ellinor
LU
; Persson, Ann-Maj
LU
; Hansson, Markus
LU
and Olsson, Inge
LU
- organization
- publishing date
- 2006
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- neutrophil elastase, sorting, pro-peptide, secretory lysosome, membrane, trafficking
- in
- Experimental Cell Research
- volume
- 312
- issue
- 18
- pages
- 3471 - 3484
- publisher
- Academic Press
- external identifiers
-
- wos:000241250900002
- scopus:33749365563
- ISSN
- 1090-2422
- DOI
- 10.1016/j.yexcr.2006.07.011
- language
- English
- LU publication?
- yes
- id
- ba6a66a3-3420-4a9f-a791-010364fbbf02 (old id 161285)
- alternative location
- http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=16950244&dopt=Abstract
- date added to LUP
- 2016-04-01 12:37:07
- date last changed
- 2024-10-09 16:53:32
@article{ba6a66a3-3420-4a9f-a791-010364fbbf02,
abstract = {{The primary granules/secretory lysosomes of neutrophils store mature neutrophil elastase (NE) as a luminal protein after proteolytic removal of N-terminal and C-terminal pro-peptides from a proform of NE. The N-terminal pro-peptide prevents premature activation that might be toxic to the cell, but the C-terminal pro-peptide has no defined function. In this study, we investigated the role of the C-terminal pro-peptide in trafficking of NE by expressing, in rat basophilic leukemia (RBL) cells, both wild-type NE and the mutant NE/Delta 248-267, which lacks the C-terminal pro-peptide. Both transfected proteins were found to be targeted to secretory lysosomes. in addition, results from antibody ligation and cell-surface biotinylation indicated that proform of NE was targeted to the plasma membrane, and then subjected to endocytosis. The results were supported by the detection of targeting of the proform to the plasma membrane followed by internalization both in RBL cells and normal granulopoietic precursor cells. Targeting of NE to the plasma membrane required the C-terminal pro-peptide as NE/ Delta 248-267 expressed in RBL cells bypassed plasma membrane trafficking. our results indicate targeting of a population of NE to the plasma membrane and internalization dependent on the C-terminal NE pro-peptide. (c) 2006 Elsevier Inc. All rights reserved.}},
author = {{Tapper, Hans and Källquist, Linda and Johnsson, Ellinor and Persson, Ann-Maj and Hansson, Markus and Olsson, Inge}},
issn = {{1090-2422}},
keywords = {{neutrophil elastase; sorting; pro-peptide; secretory lysosome; membrane; trafficking}},
language = {{eng}},
number = {{18}},
pages = {{3471--3484}},
publisher = {{Academic Press}},
series = {{Experimental Cell Research}},
title = {{Neutrophil elastase sorting involves plasma membrane trafficking requiring the C-terminal propeptide.}},
url = {{http://dx.doi.org/10.1016/j.yexcr.2006.07.011}},
doi = {{10.1016/j.yexcr.2006.07.011}},
volume = {{312}},
year = {{2006}},
}