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Cystatin C and cathepsin B in human colon carcinoma: Expression in cell lines and matrix degradation

Corticchiato, Olivier ; Cajot, Jean-Franqois ; Abrahamson, Magnus LU ; Chan, Shu Jin ; Keppler, Daniel and Sordat, Bernard (1992) In International Journal of Cancer 52. p.645-645
Abstract
Expression of the cysteine proteinase cathepsin B and its physiological inhibitor cystatin C was analyzed in vitro in I human fibrosarcoma and 4 human colon carcinoma cell lines. Cystatin C antigen as well as cathepsin B activity were detected in the conditioned media of the 5 cell lines. The corresponding cell extracts expressed high levels of cathepsin B activity, whereas only trace amounts of cystatin C antigen could be found. Northern-blot analysis revealed the presence in the 5 cell lines of a 0.8-kb cystatin C mRNA transcript and 2 cathepsin B transcripts of 2.3 and 4.3 kb. Pepsin treatment of tumor-cell-released cathepsin B induced an average 7.3-fold increase in activity, indicating that the enzyme was mainly present as a latent... (More)
Expression of the cysteine proteinase cathepsin B and its physiological inhibitor cystatin C was analyzed in vitro in I human fibrosarcoma and 4 human colon carcinoma cell lines. Cystatin C antigen as well as cathepsin B activity were detected in the conditioned media of the 5 cell lines. The corresponding cell extracts expressed high levels of cathepsin B activity, whereas only trace amounts of cystatin C antigen could be found. Northern-blot analysis revealed the presence in the 5 cell lines of a 0.8-kb cystatin C mRNA transcript and 2 cathepsin B transcripts of 2.3 and 4.3 kb. Pepsin treatment of tumor-cell-released cathepsin B induced an average 7.3-fold increase in activity, indicating that the enzyme was mainly present as a latent form in conditioned medium. The pepsin-activated cathepsin B from one colon carcinoma cell line was further characterized using the cysteine proteinase inhibitors E-64, recombinant cystatin C, a cystatin-C-derived peptidyl inhibitor (Z-LVG-CHN2), and cathepsin-B-specific diazomethyl ketone inhibitors (Z-FT(OBzl)-CHN2, Z-FS(OBzl)-CHN2). This activity was totally neutralized by recombinant cystatin C, suggesting a potential for interaction between released extracellular cathepsin B and cystatin C. In vitro assays of degradation of extracellular matrix showed that cyrteine proteinase inhibitors could decrease matrix degradation induced by pepsin-activated conditioned media. With colon cells, this inhibition was not observed, indicating a requirement for an extracellular activation of latent cathepsin B. Our data provide evidence that cystatin C and latent cathepsin B are both released extracellularly by colon carcinoma cells in vitro. They suggest that cystatin C and cathepsin B interactions may participate, in an as yet unelucidated way, in the modulation of the invasive phenotype of human colonic tumors. (Less)
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organization
publishing date
type
Contribution to journal
publication status
published
subject
in
International Journal of Cancer
volume
52
pages
645 - 645
publisher
John Wiley & Sons Inc.
external identifiers
  • scopus:0026779586
ISSN
0020-7136
DOI
10.1002/ijc.2910520425
language
English
LU publication?
yes
id
cb42e284-9462-4d42-8fc8-adf4faeab85d (old id 1106884)
date added to LUP
2016-04-04 13:56:20
date last changed
2021-01-03 06:03:30
@article{cb42e284-9462-4d42-8fc8-adf4faeab85d,
  abstract     = {{Expression of the cysteine proteinase cathepsin B and its physiological inhibitor cystatin C was analyzed in vitro in I human fibrosarcoma and 4 human colon carcinoma cell lines. Cystatin C antigen as well as cathepsin B activity were detected in the conditioned media of the 5 cell lines. The corresponding cell extracts expressed high levels of cathepsin B activity, whereas only trace amounts of cystatin C antigen could be found. Northern-blot analysis revealed the presence in the 5 cell lines of a 0.8-kb cystatin C mRNA transcript and 2 cathepsin B transcripts of 2.3 and 4.3 kb. Pepsin treatment of tumor-cell-released cathepsin B induced an average 7.3-fold increase in activity, indicating that the enzyme was mainly present as a latent form in conditioned medium. The pepsin-activated cathepsin B from one colon carcinoma cell line was further characterized using the cysteine proteinase inhibitors E-64, recombinant cystatin C, a cystatin-C-derived peptidyl inhibitor (Z-LVG-CHN2), and cathepsin-B-specific diazomethyl ketone inhibitors (Z-FT(OBzl)-CHN2, Z-FS(OBzl)-CHN2). This activity was totally neutralized by recombinant cystatin C, suggesting a potential for interaction between released extracellular cathepsin B and cystatin C. In vitro assays of degradation of extracellular matrix showed that cyrteine proteinase inhibitors could decrease matrix degradation induced by pepsin-activated conditioned media. With colon cells, this inhibition was not observed, indicating a requirement for an extracellular activation of latent cathepsin B. Our data provide evidence that cystatin C and latent cathepsin B are both released extracellularly by colon carcinoma cells in vitro. They suggest that cystatin C and cathepsin B interactions may participate, in an as yet unelucidated way, in the modulation of the invasive phenotype of human colonic tumors.}},
  author       = {{Corticchiato, Olivier and Cajot, Jean-Franqois and Abrahamson, Magnus and Chan, Shu Jin and Keppler, Daniel and Sordat, Bernard}},
  issn         = {{0020-7136}},
  language     = {{eng}},
  pages        = {{645--645}},
  publisher    = {{John Wiley & Sons Inc.}},
  series       = {{International Journal of Cancer}},
  title        = {{Cystatin C and cathepsin B in human colon carcinoma: Expression in cell lines and matrix degradation}},
  url          = {{http://dx.doi.org/10.1002/ijc.2910520425}},
  doi          = {{10.1002/ijc.2910520425}},
  volume       = {{52}},
  year         = {{1992}},
}