ArticleMolecular pathology : MP1999
Proteolysis in colorectal cancer.
Article in Molecular pathology : MP, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 32 citations in OpenAlex.
- Newly characterised ex vivo colospheres as a three-dimensional colon cancer cell model of tumour aggressiveness.British journal of cancer · 2009Article
- Peroxisome proliferator-activated receptor gamma agonists inhibit the proliferation and invasion of human colon cancer cells.Postgraduate medical journal · 2007Article
- Clinicopathological significance of stromal variables: angiogenesis, lymphangiogenesis, inflammatory infiltration, MMP and PINCH in colorectal carcinomas.Molecular cancer · 2006Review
- Identification of serum proteins discriminating colorectal cancer patients and healthy controls using surface-enhanced laser desorption ionisation-time of flight mass spectrometry.World journal of gastroenterology · 2006Article
- Significance and prognostic value of lysosomal enzyme activities measured in surgically operated adenocarcinomas of the gastroesophageal junction and squamous cell carcinomas of the lower third of esophagus.World journal of gastroenterology · 2005Article
- Balance between activation and inhibition of matrix metalloproteinase-2 (MMP-2) is altered in colorectal tumors compared to normal colonic epithelium.Digestive diseases and sciences · 2002Article
- Tissue levels of active matrix metalloproteinase-2 and -9 in colorectal cancer.British journal of cancer · 2002Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe process of metastasis is complex, involving many interrelated stages, including proteolysis. Proteolysis occurs in both normal and pathological processes and involves the breakdown of the extracellular matrix and/or basement membrane by proteolytic enzymes. Normally, proteolysis is tightly controlled by specific endogenous proteinase inhibitors. However, in certain disease processes, including cancer, controlled but abnormal proteolysis seems to occur. Proteinases involved in tumour invasion and metastasis include the matrix metalloproteinases (MMPs) and the serine proteinases.
aimsTo gain a greater understanding of the proteolytic process occurring in colorectal cancer and to determine which, if any, proteinases are upregulated.
methodsThe synthesis of proteinases and their inhibitors was compared in paired tumour and normal tissue samples from patients with colorectal cancer (n = 24). Substrate zymography was used to determine the synthesis of MMPs (MMP-2, MMP-9, and MMP-3) and the plasminogen activators (urokinase and tissue-type plasminogen activators); enzyme linked immunosorbent assays (ELISAs) were used to determine the concentrations of MMP-1 and tissue inhibitor of metalloproteinase 1 (TIMP-1); and the technique of quenched fluorescence substrate hydrolysis was performed to determine the total MMP activity of each sample.
resultsIn general, both proteinase and inhibitor expression was greater in the tumour tissue when compared with the corresponding normal colorectal tissue. The amount of active MMPs was greater in the tumour tissue.
conclusionsThe increased extracellular proteinase concentrations and activity may encourage tumour invasion and metastasis. This study points to MMP-9 as being of potential major importance in the development of this form of cancer.
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