Plasma MMP-13 Level in Patients with Invasive Ductal Breast Cancer

Authors

  • Nuntana Meesiripan Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University
  • Nonglucksanawan Ritthisunthorn epartment of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University
  • Anong Tepsuwan Biomarker Development Section, Research Division, National Cancer Institute
  • Wassana Tangthai Out Patient Department, National Cancer Institute
  • Thitiluck Swangsri Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University
  • Tipparat Thiangtrongjit Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University
  • Jaree Svedginda Out Patient Department, Hospital for Tropical Diseases, Faculty of Tropical Medicine, Mahidol University
  • Santi Maneewatchararangsri Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University
  • Porntip Chavalitchewinkoon-Petmitr Department of Protozoology, Faculty of Tropical Medicine, Mahidol University
  • Somchai Thanasitthichai Department of Surgery, National Cancer Institute
  • Songsak Petmitr Department of Molecular Tropical Medicine and Genetics, Faculty of Tropical Medicine, Mahidol University

Keywords:

invasive ductal breast cancer, MMP-13, plasma biomarker

Abstract

Matrix metalloproteinases (MMPs) are a family of zinc-proteolytic endopeptidase enzymes that play an important role in extracellular matrix (ECM) degradation in human cancer progression and may be new targets for cancer therapeutics. This study aimed to detect the plasma level of matrix metalloproteinases 13 (MMP-13) in 108 patients with invasive ductal carcinoma (IDC) and 131 healthy controls with commercial enzyme-linked immunosorbent assay (ELISA) kits. The correlations between these protein levels and the clinical characteristics of the patients were also analyzed to elucidate their role in breast-cancer development. The results showed a significantly lower median concentration of MMP-13 in patients compared with controls (89.58 and 289.15 pg/ml, respectively; P=0.000). Receiver-operator characteristic (ROC) curve analysis, to determine a cutoff value for plasma MMP-13 concentration in the patients, had an AUC of 0.98 (95% CI=0.97-0.99), with a sensitivity of 91.6% and specificity of 91.7% at cutoff point 169 pg/ml. The results underline the difference in plasma level MMP-13 concentration in IDC development, and may serve as a biomarker for patients.

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References

Ferlay J, Soerjomataram I, Ervik M, Dikshit R, Eser S, Mathers C, et al. GLOBALCAN 2012 v1.0, Cancer incidence and mortality worldwide: IARC Cancer Base No.11 [internet]. Lyon, France:International Agency for Research on Cancer; 2013. Available at: http://globocan.iarc.fr. Accessed January 16, 2016.

Makki J. Diversity of breast carcinoma: Histological subtypes and clinical relevance. Clin Med Insights Pathol 2015;8:23-3.

Yadav L, Puri N, Rastogi V, Satpute P, Ahmad R, Kaur G. Matrix metalloproteinases and cancer-role in threat and therapy. Asian Pac J Cancer Prev 2014; 15:1085-91.

Cathcart J, Pulkoski-Gross A, Cao J. Targeting matrix metalloproteinases in cancer: Bringing new life to old ideals. Genes Dis 2015;2:26-34.

Verma RP and Hansch C. Matrix metalloproteinases (MMPs): chemical-biological functions and (Q) SARs. Bioorg Med Chem 2007;15:2223-68.

Leeman MF, Curran S, Murray GI. The structure, regulation, and function of human matrix metalloproteinase-13. Crit Rev Biochem Mol Biol 2002; 37:149-66.

Vincent-Chong VK, Salahshourifar I, Karen-Ng LP, Siow MY, Kallarakkal TG, Ramanathan A, et al. Overexpression of MMP-13 is associated with clinical outcomes and poor prognosis on oral squamous cell carcinoma. Sci World J 2014;897523.

Yang B, Gao J, Rao Z, Shin Q. Clinicopathological significance and prognostic value of MMP-13 expression in colorectal cancer. Scan J Clin Lab Invest 2012;72:501-5.

Wang J, Li Y, Wang J, Li C, Yu K, Wang Q. Increased expression of matrix metalloproteinase-13 in glioma is associated with poor overall survival of patients. Med Oncol 2012;29:2432-37.

Chang HJ, Yang MJ, Yang YH, Hou MF, Hsueh EJ, Lin SR. MMP13 is potentially a new tumor marker for breast cancer diagnosis. Oncol Rep 2009;22:1119-27.

Bleyer A and Welch HG. Effect of three decades of screening mammography on breast cancer incidence. N Engl J Med 2012;367:1998-2005.

Leung J, Mckenzie S, Martin J, McLaughin D. Effect of rurality on screening for breast cancer: a systematic review and meta-analysis comparing mammography. Rural Remote Health 2014;14:2730.

Morgia G, Falsaperla M, Malaponte G, Madonia M, Indelicato M, Travali S, et al. Matrix metalloproteinases as diagnostic (MMP-13) and prognostic (MMP-2, MMP-9) markers of prostate cancer. Urol Res 2005; 33:44-50.

Bonald CM, Azzalis LA, Junqueira VBC, de Oliveira CG, Vilas Boas VA, Gáscon TM, et al. Plasma levels of E-cadherin and MMP-13 in prostate cancer patients: correlation with PSA, testosterone and pathological parameters. Tumori 2015;101:185-8.

Decock J, Hendrickx W, Vanleeuw U, Van Belle V, Van Huffel S, Christiaens MR, et al. Plasma MMP1 and MMP8 expression in breast cancer: protective role of MMP8 against lymph node metastasis. BMC Cancer 2008;8:77.

Groblewska M, Mroczko B, Gryko M, Pryczynicz A, Guzińska-Ustymowicz K, Kędra B, et al. Serum levels and tissue expression of matrix metalloproteinase 2 (MMP-2) and tissue inhibitor of metalloproteinases 2 (TIMP-2) in colorectal cancer patients. Tumor Biol 2014;35:3793-802.

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Published

2017-09-29

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