Unique activation of matrix metalloproteinase-9 within human liver metastasis from colorectal cancer Journal Article


Authors: Zeng, Z. S.; Guillem, J. G.
Article Title: Unique activation of matrix metalloproteinase-9 within human liver metastasis from colorectal cancer
Abstract: Experimental in vitro and animal data support an important role for matrix metalloproteinases (MMPs) in cancer invasion and metastasis via proteolytic degradation of the extracellular matrix (ECM). Our previous data have shown that MMP-9 mRNA is localized to the interface between liver metastasis and normal liver tissue, indicating that MMP-9 may play an important role in liver metastasis formation. In the present study, we analysed the cellular enzymatic expression of MMP-9 in 18 human colorectal cancer (CRC) liver metastasis specimens by enzyme-linked immunosorbent assay (ELISA) and zymography. ELISA analysis reveals that the latent form of MMP-9 is present in both liver metastasis and paired adjacent normal liver tissue. The mean level of the latent form of MMP-9 is 580 ± 270 ng per mg total tissue protein (mean ± s.e.) in liver metastasis vs 220 ± 90 in normal liver tissue. However, this difference is not significantly different (P = 0.26). Using gelatin zymography, the 92-kDa band representative of the latent form is present in both liver metastasis and normal liver tissue. However, the 82 kDa band, representive of the active form of MMP-9, was seen only in liver metastasis. This was confirmed by Western blot analysis. Our observation of the unique presence of the active form of MMP-9 within liver metastasis suggests that proMMP-9 activation may be a pivotal event during CRC liver metastasis formation.
Keywords: clinical article; controlled study; human tissue; liver neoplasms; colorectal cancer; gelatinase b; enzyme activation; enzyme linked immunosorbent assay; colorectal neoplasms; liver metastasis; blotting, western; matrix metalloproteinase; immunoblotting; enzyme-linked immunosorbent assay; collagenases; enzyme precursors; metalloproteinase; activation; matrix metalloproteinase 9; gelatin; zymography; humans; human; priority journal; article; 92 kda type iv collagenase (mmp-9)
Journal Title: British Journal of Cancer
Volume: 78
Issue: 3
ISSN: 0007-0920
Publisher: Nature Publishing Group  
Date Published: 1998-08-01
Start Page: 349
End Page: 353
Language: English
PUBMED: 9703281
PROVIDER: scopus
PMCID: PMC2063024
DOI: 10.1038/bjc.1998.497
DOI/URL:
Notes: Article -- Export Date: 12 December 2016 -- Source: Scopus
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  1. Jose Guillem
    414 Guillem
  2. Zhaoshi Zeng
    87 Zeng