Preview

Tumors of female reproductive system

Advanced search

Role of matrix metalloproteinase 7 in ovarian cancer (review of literature)

https://doi.org/10.17650/1994-4098-2015-11-3-67-71

Abstract

Ovarian carcinoma is one of the most aggressive cancer in women, and one of the leading causes of death from cancer of the reproductive system. Despite enhancement methods of prevention, early diagnosis, treatment, such as surgery, radiation, drugs, including targeted and hormone therapy, long-term results remain unsatisfactory. In this connection, much attention is paid to the search for molecular biological mechanisms involved in carcinogenesis and the development of laboratory tests for detecting patients at early stages of tumor process, to differentiate malignant and benign tumors, to determine the tactics of treatment of a particular patient, to assess the prognosis. One of the key aspects of the pathogenesis of ovarian cancer is the interaction of tumor tissue extracellular matrix, the protein degradation of which in most cases is controlled by proteolytic enzymes. Matrix metalloproteinase 7 (MMP-7), also known as matrilysin, like other members of the matrix metalloproteinase` family, demonstrates proteolytic activity against components of the extracellular matrix, the degradation of which is the basis of cancer invasion and metastasis. Matrilysin is also involved in the regulation of activities of bioactive molecules associated with cell physiology. The overview briefly highlights the role of MMP-7 in ovarian cancer. 

About the Authors

R. I. Knyazev
Russian Medical Academy of Postgraduate Education, Ministry of Health of Russia; 2/1 Barrikadnaya St., Moscow, 123995, Russia
Russian Federation


I. I. Bokin
Russian Medical Academy of Postgraduate Education, Ministry of Health of Russia; 2/1 Barrikadnaya St., Moscow, 123995, Russia
Russian Federation


V. V. Barinov
N.N. Blokhin Russian Cancer Research Center; 23 Kashirskoe Shosse, Moscow, 115478, Russia
Russian Federation


References

1. Злокачественные новообразования в России в 2013 г. (заболеваемость и смертность). Под ред. А.Д. Каприна, В.В. Старинского, Г.В. Петровой. М., 2015. 12 с. [Malignant tumors in Russia in 2013 (morbidity and mortality). Ed. by А.D. Kaprin, V.V. Starinsky, G.V. Petrova. Мoscow, 2015. 12 р. (In Russ.)].

2. International agency for research on cancer. GLOBOCAN 2012: estimated cancer incidence, mortality and prevalence worldwide in 2012. URL: http://globocan.iarc.fr/Pages/ fact_sheets_population.aspx.

3. Friedl P., Locker J., Sahai E., Segall J.E. Classifying collective cancer cell invasion. Nat Cell Biol 2012;14(8):777–83.

4. Friedl P., Alexander S. Cancer invasion and the microenvironment: plasticity and reciprocity. Cell 2011;147(5):992–1009.

5. Kessenbrock K., Plaks V., Werb Z. Matrix metalloproteinases: regulators of the tumor microenvironment. Cell 2010;141(1):52–67.

6. Кушлинский Н.Е., Герштейн Е.С. Исследование матриксных металлопротеиназ и их тканевых ингибиторов в опухолях и периферической крови онкологических больных. Клинические перспективы. Лабораторная служба 2013;1:25–38. [Kushlinsky N.Е., Gerstein Е.S. Research of matrix metalloprotease and its tissue inhibitors in tumors and peripheral blood of oncologic patients. Clinical prospects. Laboratornaya sluzhba = Laboratory Service 2013;1:25–38. (In Russ.)].

7. Nelson A.R., Fingleton B., Rothenberg M.L., Matrisian L.M. Matrix metalloproteinases: biologic activity and clinical implications. J Clin Oncol 2000;18(5):1135–49.

8. Moss L.A.S., Jensen-Taubman S., StetlerStevenson W.G. Matrix metalloproteinases: changing roles in tumor progression and metastasis. Am J Pathol 2012;181(6):1895–9.

9. Liotta L.A. Tumor invasion and metastases – role of the extracellular matrix: Rhoads Memorial Award lecture. Cancer Res 1986;46(1):1–7.

10. Герштейн Е.С., Кушлинский Н.Е. Клинические перспективы исследования ассоциированных с опухолью протеаз и их тканевых ингибиторов у онкологических больных. Вестник РАМН 2013;5:16–27. [Gerstein Е.S., Kushlinsky N.Е. Clinical prospects of the research, associated with protease tumors and its inhibitors at oncologic patients. Vestnik RAMN = RAMS Herald 2013;5:16–27. (In Russ.)].

11. Mantovani A. Molecular pathways linking inflammation and cancer. Curr Mol Med 2010;10(4):369–73.

12. Yu W.H., Woessner J.F. Jr, McNeish J.D., Stamenkovic I. CD44 anchors the assembly of matrilysin/MMP-7 with heparin-binding epidermal growth factor precursor and ErbB4 and regulates female reproductive organ remodeling. Genes Dev 2002;16(3):307–23.

13. Zhao H., Yang Z., Wang X. et al. Triptolide inhibits ovarian cancer cell invasion by repression of matrix metalloproteinase 7 and 19 and upregulation of E-cadherin. Exp Мol Мed 2012;44(11):633–41.

14. Rims C.R., McGuire J.K. Matrilysin (MMP-7) catalytic activity regulates β-catenin localization and signaling activation in lung epithelial cells. Exp Lung Res 2014;40(3): 126–36.

15. Mohan M.J., Seaton T., Mitchell J. et al. The tumor necrosis factor-α converting enzyme (TACE): a unique metalloproteinase with highly defined substrate selectivity. Biochemistry 2002;41(30):9462–9.

16. Wang F., So J., Reierstad S., Fishman D.A. Matrilysin (MMP 7) promotes invasion of ovarian cancer cells by activation of progelatinase. Int J Cancer 2005;114(1): 19–31.

17. Bavi P.P., Bu R., Uddin S., Al-Kuraya K.S. MMP7 Polymorphisms-A new tool in molecular pathology to understand esophageal cancer. Saudi J Gastroenterol 2011;17(5):299–300.

18. Sentani K., Matsuda M., Oue N. et al. Clinicopathological significance of MMP-7, laminin γ2 and EGFR expression at the invasive front of gastric carcinoma. Gastric Cancer 2014;17(3):412–22.

19. Clapper M.L., Hensley H.H., Chang W.C. et al. Detection of colorectal adenomas using a bioactivatable probe specific for matrix metalloproteinase activity. Neoplasia 2011;13(8):685–91.

20. Pryczynicz A., Gryko M., Niewiarowska K. et al. Immunohistochemical expression of MMP-7 protein and its serum level in colorectal cancer. Folia Histochem Cytobiol 2013;51(3):206–12.

21. Xing X.J., Gu X.H., Ma T.F. Relationship of serum MMP-7 levels for colorectal cancer: a meta-analysis. Tumor Biol 2014;35(10): 10515–22.

22. Hirashita T., Iwashita Y., Ohta M. et al. Expression of matrix metalloproteinase-7 is an unfavorable prognostic factor in intrahepatic cholangiocarcinoma. Jo Gastrointest Surg 2012;16(4):842–8.

23. Fukuda A., Wang S.C., Morris J.P. et al. Stat3 and MMP7 contribute to pancreatic ductal adenocarcinoma initiation and progression. Cancer Cell 2011;19(4):441–55.

24. Кисарова Я.А. Активность матриксных металлопротеаз у мышей при развитии и метастазировании аденокарциномы легких Льюис. Бюллетень СО РАМН 2010;4: 154–8. [Kisarova Y.А. Аctivity of matrix metalloproteases at mice at the development and dissemination of Lewis lungs adenocarcinoma. Bulleten' SO RAMN = Bulletin of SB RAMS 2010;4:154–8. (In Russ.)].

25. Kivisaari A.K., Kallajoki M., Mirtti T. et al. Transformation specific matrix metalloproteinases (MMP) 7 and MMP 13 are expressed by tumour cells in epidermolysis bullosa associated squamous cell carcinomas. Br J Dermatol 2008;158(4):778–85.

26. Bucan V., Mandel K., Bertram C. et al. LEF 1 regulates proliferation and MMP 7 transcription in breast cancer cells. Genes Cells 2012;17(7):559–67.

27. Littlepage L.E., Sternlicht M.D., Rougier N. et al. Matrix metalloproteinases contribute distinct roles in neuroendocrine prostate carcinogenesis, metastasis, and angiogenesis progression. Cancer Res 2010;70(6):2224–34.

28. Yurkovetsky Z., Ta'asan S., Skates S. et al. Development of multimarker panel for early detection of endometrial cancer. High diagnostic power of prolactin. Gynecol Оncol 2007;107(1):58–65.

29. Stokes A., Joutsa J., Ala-Aho R. et al. Expression profiles and clinical correlations of degradome components in the tumor microenvironment of head and neck squamous cell carcinoma. Clin Cancer Res 2010;16(7):2022–35.

30. Левкина Н.В. Клиническое значение матриксных металлопротеиназ у больных раком яичников. Дис. ... канд. мед. наук. М., 2011. С. 103–10. [Levkina N.V. Clinical value of matrix metalloproteinases at patients with ovarian cancer. PhD thesis. Мoscow, 2011. Pp. 103–10. (In Russ.)].

31. Zohny S.F., Fayed S.T. Clinical utility of circulating matrix metalloproteinase-7 (MMP-7), CC chemokine ligand 18 (CCL18) and CC chemokine ligand 11 (CCL11) as markers for diagnosis of epithelial ovarian cancer. Med Oncol 2010;27(4):1246–53.

32. Acar A., Onan A., Coskun U. et al. Clinical significance of serum MMP-2 and MMP-7 in patients with ovarian cancer. Med Оncol 2008;25(3): 279–83.

33. Brun J.L., Cortez A., Commo F. et al. Serous and mucinous ovarian tumors express different profiles of MMP-2, -7, -9, MT1MMP, and TIMP-1 and -2. Int J Oncol 2008;33(6):1239–46.

34. Schummer M., Drescher C., Forrest R. et al. Evaluation of ovarian cancer remission markers HE4, MMP7 and Mesothelin by comparison to the established marker CA-125. Gynecol Oncol 2012;125(1):65–9.

35. Sillanpää S.M., Anttila M.A., Voutilainen K.A. et al. Prognostic significance of matrix metalloproteinase 7 in epithelial ovarian cancer and its relation to β-catenin expression. Int J Cancer 2006;119(8):1792–9.

36. Brun J.L., Cortez A., Lesieur B. et al. Expression of MMP-2, -7, -9, MT1-MMP and TIMP-1 and -2 has no prognostic relevance in patients with advanced epithelial ovarian cancer. Oncol Rep 2012;27(4): 1049–57.


Review

For citations:


Knyazev R.I., Bokin I.I., Barinov V.V. Role of matrix metalloproteinase 7 in ovarian cancer (review of literature). Tumors of female reproductive system. 2015;11(3):67-71. (In Russ.) https://doi.org/10.17650/1994-4098-2015-11-3-67-71

Views: 860


Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 License.


ISSN 1994-4098 (Print)
ISSN 1999-8627 (Online)