Modulation of invasive properties of murine squamous carcinoma cells by heterologous expression of cathepsin B and cystatin C
(1999) In International Journal of Cancer 83(4). p.526-531- Abstract
- Murine SCC-VII squamous carcinoma cells have the capacity
to penetrate reconstituted basement membranes (Matrigel)
in vitro. The invasion of Matrigel layers by SCC-VII cells
was significantly reduced by E-64, a specific inhibitor of
lysosomal cysteine proteinases. The cathepsin-B-selective
E-64 derivative, CA-074, inhibited penetration of Matrigel by SCC-VII cells to the same extent, indicating a major role for this particular lysosomal enzyme in extracellular-matrix degradation during squamous-carcinoma-cell invasion. SCC-VII cells were stably transfected with a cDNA encoding human procathepsin B, in an attempt to modulate the invasive properties of the cell line. The transfected cells... (More) - Murine SCC-VII squamous carcinoma cells have the capacity
to penetrate reconstituted basement membranes (Matrigel)
in vitro. The invasion of Matrigel layers by SCC-VII cells
was significantly reduced by E-64, a specific inhibitor of
lysosomal cysteine proteinases. The cathepsin-B-selective
E-64 derivative, CA-074, inhibited penetration of Matrigel by SCC-VII cells to the same extent, indicating a major role for this particular lysosomal enzyme in extracellular-matrix degradation during squamous-carcinoma-cell invasion. SCC-VII cells were stably transfected with a cDNA encoding human procathepsin B, in an attempt to modulate the invasive properties of the cell line. The transfected cells expressed the heterologous gene, secreted increased amounts of procathepsin B and displayed enhanced invasive potential. In vivo, the
activity of cathepsin B is strictly regulated by endogenous
inhibitors. SCC-VII cells were therefore also stably transfected with a cDNA encoding human cystatin C, the most
potent cysteine-proteinase inhibitor in mammalian tissues.
The expression of this transgene resulted in the production of active recombinant cystatin C and a pronounced reduction in Matrigel invasion. These studies demonstrate that the invasive properties of squamous-cell carcinomas can be changed by modulation of the balance between cathepsin B and its endogenous inhibitors, and provide further evidence for the involvement of this lysosomal cysteine proteinase in tumour invasion and metastasis. (Less)
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- author
- organization
- publishing date
- 1999
- type
- Contribution to journal
- publication status
- published
- subject
- in
- International Journal of Cancer
- volume
- 83
- issue
- 4
- pages
- 526 - 531
- publisher
- John Wiley & Sons Inc.
- external identifiers
-
- scopus:0032834905
- ISSN
- 0020-7136
- DOI
- 10.1002/(SICI)1097-0215(19991112)83:4<526::AID-IJC15>3.0.CO;2-M
- language
- English
- LU publication?
- yes
- id
- f702494b-5d17-4617-ade9-dd8806b033bb (old id 1115924)
- date added to LUP
- 2016-04-01 12:16:57
- date last changed
- 2022-02-03 20:07:00
@article{f702494b-5d17-4617-ade9-dd8806b033bb,
abstract = {{Murine SCC-VII squamous carcinoma cells have the capacity<br/><br>
to penetrate reconstituted basement membranes (Matrigel)<br/><br>
in vitro. The invasion of Matrigel layers by SCC-VII cells<br/><br>
was significantly reduced by E-64, a specific inhibitor of<br/><br>
lysosomal cysteine proteinases. The cathepsin-B-selective<br/><br>
E-64 derivative, CA-074, inhibited penetration of Matrigel by SCC-VII cells to the same extent, indicating a major role for this particular lysosomal enzyme in extracellular-matrix degradation during squamous-carcinoma-cell invasion. SCC-VII cells were stably transfected with a cDNA encoding human procathepsin B, in an attempt to modulate the invasive properties of the cell line. The transfected cells expressed the heterologous gene, secreted increased amounts of procathepsin B and displayed enhanced invasive potential. In vivo, the<br/><br>
activity of cathepsin B is strictly regulated by endogenous<br/><br>
inhibitors. SCC-VII cells were therefore also stably transfected with a cDNA encoding human cystatin C, the most<br/><br>
potent cysteine-proteinase inhibitor in mammalian tissues.<br/><br>
The expression of this transgene resulted in the production of active recombinant cystatin C and a pronounced reduction in Matrigel invasion. These studies demonstrate that the invasive properties of squamous-cell carcinomas can be changed by modulation of the balance between cathepsin B and its endogenous inhibitors, and provide further evidence for the involvement of this lysosomal cysteine proteinase in tumour invasion and metastasis.}},
author = {{Coulibaly, S and Schwihla, H and Abrahamson, Magnus and Albini, A and Cerni, C and Clark, JL and Ng, KM and Katunuma, N and Schlappack, O and Glossl, J and Mach, L}},
issn = {{0020-7136}},
language = {{eng}},
number = {{4}},
pages = {{526--531}},
publisher = {{John Wiley & Sons Inc.}},
series = {{International Journal of Cancer}},
title = {{Modulation of invasive properties of murine squamous carcinoma cells by heterologous expression of cathepsin B and cystatin C}},
url = {{http://dx.doi.org/10.1002/(SICI)1097-0215(19991112)83:4<526::AID-IJC15>3.0.CO;2-M}},
doi = {{10.1002/(SICI)1097-0215(19991112)83:4<526::AID-IJC15>3.0.CO;2-M}},
volume = {{83}},
year = {{1999}},
}