Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin B activity by neutrophil elastase
(1995) In Archives of Biochemistry and Biophysics 317(1). p.305-310- Abstract
- Procathepsin B and cystatin C are found in human lung secretions. We investigated the capacity of human bronchial epithelial cells to synthesize and secrete these proteins. Immunoprecipitation of [35S]methionine-labeled proteins from cultured bronchial epithelial cell lysates, followed by denaturing gel electrophoresis and autoradiography, showed the presence of newly synthesized procathepsin B of M(r) 42,000; no mature form was detected. Cathepsin B in conditioned medium from epithelial cells was tagged with benzyloxycarbonyl-125I-tyrosyl-alanine-diazomethane before and after treatment of the medium with neutrophil elastase. Control medium again showed a predominant form of cathepsin B with a M(r) of 42,000, but upon treatment with... (More)
- Procathepsin B and cystatin C are found in human lung secretions. We investigated the capacity of human bronchial epithelial cells to synthesize and secrete these proteins. Immunoprecipitation of [35S]methionine-labeled proteins from cultured bronchial epithelial cell lysates, followed by denaturing gel electrophoresis and autoradiography, showed the presence of newly synthesized procathepsin B of M(r) 42,000; no mature form was detected. Cathepsin B in conditioned medium from epithelial cells was tagged with benzyloxycarbonyl-125I-tyrosyl-alanine-diazomethane before and after treatment of the medium with neutrophil elastase. Control medium again showed a predominant form of cathepsin B with a M(r) of 42,000, but upon treatment with neutrophil elastase this protein was converted to a M(r) of 38,000, similar to the active form previously found in lung secretions, and cathepsin B activity was generated. The medium also contained the cathepsin B inhibitor, cystatin C, but cystatins A, B, S, SN, SA, and kininogen were not detected. After removal of cystatin C from the medium, elastase was still required to activate procathepsin B. These results suggest that bronchial epithelial cells are a source of procathepsin B and cystatin C in lung secretions. Cleavage both of cystatin C and procathepsin B by neutrophil elastase is essential for the generation of cathepsin B activity in the medium. (Less)
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https://lup.lub.lu.se/record/1108943
- author
- Burnett, D ; Abrahamson, Magnus LU ; Devalia, J L ; Sapsford, R J ; Davies, R J and Buttle, D J
- organization
- publishing date
- 1995
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Archives of Biochemistry and Biophysics
- volume
- 317
- issue
- 1
- pages
- 305 - 310
- publisher
- Academic Press
- external identifiers
-
- pmid:7872798
- scopus:0028939165
- pmid:7872798
- ISSN
- 0003-9861
- DOI
- 10.1006/abbi.1995.1167
- language
- English
- LU publication?
- yes
- id
- df68ca40-2e6f-4786-937f-0190212b50e1 (old id 1108943)
- date added to LUP
- 2016-04-01 11:40:01
- date last changed
- 2021-01-03 05:00:46
@article{df68ca40-2e6f-4786-937f-0190212b50e1,
abstract = {{Procathepsin B and cystatin C are found in human lung secretions. We investigated the capacity of human bronchial epithelial cells to synthesize and secrete these proteins. Immunoprecipitation of [35S]methionine-labeled proteins from cultured bronchial epithelial cell lysates, followed by denaturing gel electrophoresis and autoradiography, showed the presence of newly synthesized procathepsin B of M(r) 42,000; no mature form was detected. Cathepsin B in conditioned medium from epithelial cells was tagged with benzyloxycarbonyl-125I-tyrosyl-alanine-diazomethane before and after treatment of the medium with neutrophil elastase. Control medium again showed a predominant form of cathepsin B with a M(r) of 42,000, but upon treatment with neutrophil elastase this protein was converted to a M(r) of 38,000, similar to the active form previously found in lung secretions, and cathepsin B activity was generated. The medium also contained the cathepsin B inhibitor, cystatin C, but cystatins A, B, S, SN, SA, and kininogen were not detected. After removal of cystatin C from the medium, elastase was still required to activate procathepsin B. These results suggest that bronchial epithelial cells are a source of procathepsin B and cystatin C in lung secretions. Cleavage both of cystatin C and procathepsin B by neutrophil elastase is essential for the generation of cathepsin B activity in the medium.}},
author = {{Burnett, D and Abrahamson, Magnus and Devalia, J L and Sapsford, R J and Davies, R J and Buttle, D J}},
issn = {{0003-9861}},
language = {{eng}},
number = {{1}},
pages = {{305--310}},
publisher = {{Academic Press}},
series = {{Archives of Biochemistry and Biophysics}},
title = {{Synthesis and secretion of procathepsin B and cystatin C by human bronchial epithelial cells in vitro: modulation of cathepsin B activity by neutrophil elastase}},
url = {{http://dx.doi.org/10.1006/abbi.1995.1167}},
doi = {{10.1006/abbi.1995.1167}},
volume = {{317}},
year = {{1995}},
}