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Modulation of invasive properties of murine squamous carcinoma cells by heterologous expression of cathepsin B and cystatin C

Coulibaly, S; Schwihla, H; Abrahamson, Magnus LU ; Albini, A; Cerni, C; Clark, JL; Ng, KM; Katunuma, N; Schlappack, O and Glossl, J, et al. (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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type
Contribution to journal
publication status
published
subject
in
International Journal of Cancer
volume
83
issue
4
pages
526 - 531
publisher
John Wiley & Sons
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
2008-07-09 12:56:26
date last changed
2017-10-01 03:51:34
@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},
  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},
  volume       = {83},
  year         = {1999},
}