The expression and clinical correlations of matrix metalloproteinase-2, -7, -9, and -12 in colorectal cancer

Eun Jung Ahn, Soon Sup Chung, Ryung Ah Lee, Kwang Ho Kim

Research output: Contribution to journalArticlepeer-review

1 Scopus citations


Purpose: Tumor invasion and metastasis are multistep phenomina, involving proteolytic degradation of extracellular matrix (ECM) and alteration of cell adhesion. It is another oncologic therapeutic strategy to block tumor invasion and metastasis through analyzing the molecules which are involved in these processes. We examined the expressions of some of matrix metalloproteinases (MMPs) in colorectal cancer and analyze the correlation with clinical factors and survival. Methods: Fifty-five patients with colorectal cancer who underwent surgical resection were included. The expressions of the MMP-2, -7, -9, and -12 in tumor tissue and normal mucosa using RT-PCR technique was carried out. We evaluated and analyzed the correlation among these molecules, clinical characteristics, and survival. Results: Expressions of MMP-7, -9, and -12 were significantly higher in tumor tissue than in normal mucosa (P=0.00). The expressions of MMP-2 between cancer and normal mucosa had no significant difference but it had a significant difference according to the lymph node (LN) invasion (P=0.03) in tumor tissues. Three-year overall survival was worse in patient with high expression of MMP-2 compared to low expression. Conclusion: The expressions of MMP-7, -9, -12 in tumor tissue were higher than in normal mucosa and MMP-2 expression of tumor tissues had a significant difference according to LN invasion. MMP-2 overexpression seems to be a prognostic factor for 3-yr overall survival. But, large scale study with long term survival analysis will be needed for the prognostic significance of MMPs.

Original languageEnglish
Pages (from-to)26-33
Number of pages8
JournalJournal of the Korean Society of Coloproctology
Issue number1
StatePublished - Feb 2009


  • Colorectal cancer
  • Matrix metalloproteinase


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