Morphological features of tumors and the matrix metalloproteinases in the blood plasma of patients with gastric cancer

A.A. Ivannikov; V.L. Chang; E.S. Gershtein; N.A. Ognerubov; M.M. Dav-idov; I.S. Stilidi; N.E. Kushlinskii

Morphological features of tumors and the matrix metalloproteinases in the blood plasma of patients with gastric cancer

A.A. Ivannikov¹, V.L. Chang², E.S. Gershtein³, N.A. Ognerubov⁴, M.M. Dav-idov⁵, I.S. Stilidi⁶, N.E. Kushlinskii⁷

research article Pages: 42-48

¹ Ph.D. (Med.), Tambov Regional Cancer Clinical Dispensary, Tambov
² Assistant, Department of Oncology, Topographic Anatomy and Operative Surgery, G.A. Derzhavin Tambov State University, Tambov
³ Dr.Sc. (Biol.), Professor, Moscow State University of Medicine and Dentistry Named After A.I. Evdokimov
⁴ Dr.Sc. (Med.), Professor, Head, Department of Oncology, Topographic Anatomy and Operative surgery, G.A. Derzhavin Tambov State University, Tambov
⁵ Ph.D. (Med.), N.N. Blokhin Russian Cancer Research Center, Moscow
⁶ Dr.Sc. (Med.), Professor, Corresponding Member of the RAS, N.N. Blokhin Russian Cancer Research Center, Moscow
⁷ Dr.Sc. (Med.), Professor, Corresponding Member of the RAS, Head, of the Department of Clinical Biochemistry and Laboratory Diagnosis, Moscow State University of Medicine and Dentistry Named After A.I. Evdokimov

Keywords: primary gastric cancer histology MMP-2 MMP-7 MMP-9 TIMP-2

Abstract

The study was conducted in 91 primary gastric cancer patients stage I-IV, aged 16 to 84 years. All patients prior to treatment in the plasma was determined content of matrix metalloproteinases (MMP-2, MMP-7, MMP-9) and tissue inhibitor type 2 (TIMP-2). 73 (80.2 %) patients underwent surgical procedures in different volumes. The interrelation of the above markers with some morphological features of the structure of the tumor. MMP-7 levels in patients with LVI was significantly higher, when its median perstnevidnokletochnoy adenocarcinoma was, conversely, significantly smaller. The content of MMP-9 was significantly lower in tumor invasion of the submucosal layer, and the level of MMP-2 was also significantly decreased with increasing depth of tumor invasion from 300±17.5 ng/ml at the mucosal invasion to 243±23.2 ng/ml during the invasion in other organs.

How to cite

Иванников А.А., Чанг В.Л., Герштейн Е.С., Огнерубов Н.А., Давыдов М.М., Стилиди И.С., Кушлинский Н.Е. Морфологические особенности опухоли и матриксные металлопро-теиназы в плазме крови больных раком желудка // Вопросы биологической, медицинской и фармацевтической химии. 2015. № 6. С. 42–48.

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[1] Alexander C.M., Selvarajan S., Mudgett J., Werb Z. Stromelysin-1 regulates adipogenesis during mammary gland involution // J. Cell Biology. 2001. V. 152. № 4. P. 693-703.

[2] Brand K., Baker A.H., Perez-Canto A. et al. Treatment of colorectal liver metastases by adenoviral transfer of tissue inhibitor of metalloproteinases-2 into the liver tissue // Cancer Res. 2000. V. 60. № 20. P. 5723-5730.

[3] Celiker M.Y., Wang M., Atsidaftos E. et al. Inhibition of Wilms\' tumor growth by intramuscular administration of tissue inhibitor of metalloproteinases-4 plasmid DNA // Oncogene. 2001. V. 20. № 32. P. 4337-4343.

[4] Deryugina E.I., Quigley J.P. Pleiotropic roles of matrix metalloproteinases in tumor angiogenesis: contrasting, overlapping and compensatory functions // Biochim. Biophys. Acta. 2010. V. 1803. № 1. P. 103-120.

[5] Hanahan D., Weinberg R.A. The hallmarks of cancer. The next generation // Cell. 2011. V. 144. № 4. P. 646-674.

[6] Kemik O., Kemik A.S., Sumer A. et al. Levels of matrix metalloproteinase-1 and tissue inhibitors of metalloproteinase-1 in gastric cancer // World J. Gastroenterol. 2011. V. 17. № 16. P. 2109-2112.

[7] Kim J.S., Kim M.A., Kim T.M. et al. Biomarker analysis in stage III-IV (M0) gastric cancer patients who received curative surgery followed by adjuvant 5-fluorouracil and cisplatin chemotherapy: epidermal growth factor receptor (EGFR) associated with favourable survival // Br. J. Cancer. 2009. V. 100. № 5. P. 732-738.

[8] Kim M., Kim H.J., Choi B.Y. et al. Identification of potential serum biomarkers for gastric cancer by a novel computational method, multiple normal tissues corrected differential analysis // Clin. Chim. Acta. 2012. V. 413. № 3-4. P. 428-433.

[9] Malemud C.J. Matrix metalloproteinases (MMPs) in health and disease: an overview // Front Biosci. 2006. V. 11. P. 1696-1701.

[10] Murphy G., Nagase H. Progress in matrix metalloproteinase research // Mol. Aspects. Med. 2008. V. 29. № 5. P. 290-308.

[11] Nelson A.R., Fingleton B., Rothenberg M.L., Matrisian L.M. Matrix metalloproteinases: biologic activity and clinical implications // J. Clin. Oncol. 2000. V. 18. № 5. P. 1135-1149.

[12] Ramnath N., Creaven P.J. Matrix metalloproteinase inhibitors // Curr. Oncol. Rep. 2004. V. 6. № 2. P. 96-102.

[13] Visse R., Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry // Circ. Res. 2003. V. 92. № 8. P. 827-839.

[14] Westermarck J., Kahari V.M. Regulation of matrix metalloproteinase expression in tumor invasion // FASEB J. 1999. V. 13. № 8. P. 781-792.

[15] Woessne J.F., Nagase Jr., Anonymous H.Matrix Metalloproteinases and TIMPs. 1. New York: Oxford University Press. 2000.

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