BOKU - Universität für Bodenkultur Wien - Forschungsinformationssystem

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Gewählte Publikation:

Coulibaly, S., Schwihla, H., Abrahamson, M., Albini, A., Cerni, C., Clark, J.L., Ng, K.M., Katunuma, N., Schlappack, O., Glössl, J., Mach, L..
(1999): Modulation of invasive properties of murine squamous carcinoma cells by heterologous expression of cathepsin B and cystatin C.
Int. J. Cancer, 83, 526-531

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. Int. J. Cancer, 83:526-531, 1999. (C) 1999 Wiley-Liss, Inc.
Autor*innen der BOKU Wien:
Glößl Josef
Mach Lukas

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