Serum levels of TIMP-1 and MMP-7 as potential biomarkers in patients with metastatic colorectal cancer

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Abstract

Objective:

Tissue inhibitor of metalloproteinases 1 (TIMP-1) and matrix metalloproteinase 7 (MMP-7) were reported to have potent growth promoting activity. Lack of balance between MMPs and TIMPs is an important factor in the development of gastrointestinal malignancies.

Methods:

We collected serum samples from 97 patients with metastatic colorectal cancer and 79 samples from healthy controls. Serum levels of TIMP-1 and MMP-7 were measured immunochemically and compared with standard tumor markers carcinoembryonic antigen and CA19-9.

Results:

Serum levels of TIMP-1 and MMP-7 were significantly higher in patients with colorectal cancer compared to healthy controls (both, P < 0.001). TIMP-1 and MMP-7 correlate with the presence of colon involvement (P = 0.001; P = 0.012) and the presence of liver metastases (P = 0.002; P = 0.037), and negatively correlate with pulmonary metastases (P = 0.014; P = 0.005). MMP-7 had similar sensitivity and the same specificity as carcinoembryonic antigen. TIMP-1 and MMP-7 had better sensitivity than CA19-9. TIMP-1 and MMP-7 level correlate with worse outcome (P = 0.002).

Conclusion:

The results indicate that TIMP-1 and MMP-7 are effective biomarkers in patients with metastatic colorectal cancer with good sensitivity. TIMP-1 and MMP-7 levels strongly correlate with the extent of liver disease and have prognostic value.

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Most cited references 31

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Matrix metalloproteinases (MMPs) have long been associated with cancer-cell invasion and metastasis. This provided the rationale for clinical trials of MMP inhibitors, unfortunately with disappointing results. We now know, however, that the MMPs have functions other than promotion of invasion, have substrates other than components of the extracellular matrix, and that they function before invasion in the development of cancer. With this knowledge in hand, can we rethink the use of MMP inhibitors in the clinic?

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Matrix metalloproteinases (MMPs), also designated matrixins, hydrolyze components of the extracellular matrix. These proteinases play a central role in many biological processes, such as embryogenesis, normal tissue remodeling, wound healing, and angiogenesis, and in diseases such as atheroma, arthritis, cancer, and tissue ulceration. Currently 23 MMP genes have been identified in humans, and most are multidomain proteins. This review describes the members of the matrixin family and discusses substrate specificity, domain structure and function, the activation of proMMPs, the regulation of matrixin activity by tissue inhibitors of metalloproteinases, and their pathophysiological implication.

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Author and article information

Contributors

Michal Vočka: (View ORCID Profile)

Journal

Title: The International Journal of Biological Markers

Abbreviated Title: Int J Biol Markers

Publisher: SAGE Publications

ISSN (Print): 1724-6008

ISSN (Electronic): 1724-6008

Publication date Created: September 2019

Publication date (Electronic): September 04 2019

Publication date (Print): September 2019

Volume: 34

Issue: 3

Pages: 292-301

Affiliations

[1 ]Department of Oncology, First Faculty of Medicine, Charles University, and General University Hospital in Prague, Czech Republic

[2 ]Surgery Department, Second Faculty of Medicine, Charles University, and Military University Hospital in Prague, Prague, Czech Republic

[3 ]First Department of Surgery – Department of Abdominal, Thoracic Surgery and Traumatology, First Faculty of Medicine, Charles University, and General University Hospital in Prague, Czech Republic

[4 ]Fourth Department of Internal Medicine – Department of Gastroenterology and Hepatology, First Faculty of Medicine, Charles University, and General University Hospital in Prague, Czech Republic

[5 ]Department of Urology, First Faculty of Medicine, Charles University, and General University Hospital in Prague, Czech Republic

[6 ]Institute of Medical Biochemistry and Laboratory Diagnostics, First Faculty of Medicine, Charles University, and General University Hospital in Prague, Czech Republic