Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
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High Expression of Matrix Metalloproteinase-11 indicates Poor Prognosis in Human Cholangiocarcinoma

  • Tongtawee, Taweesak (Department of surgery, Institute of Medicine, Suranaree University of Technology) ;
  • Kaewpitoon, Soraya J (Department of Family and Community Medicine, Institute of Medicine, Suranaree University of Technology) ;
  • Loyd, Ryan (Department of Family and Community Medicine, Institute of Medicine, Suranaree University of Technology) ;
  • Chanvitan, Supachai (Department of Surgery, Rajvithi Hospital) ;
  • Leelawat, Kawin (Department of Surgery, Rajvithi Hospital) ;
  • Praditpol, Niphol (Immunohistochemistry Section, Rajvithi Hospital) ;
  • Jujinda, Supathip (Department of Surgery, Rajvithi Hospital) ;
  • Kaewpitoon, Natthawut (Parasitic Disease Research Unit, Institute of Medicine, Suranaree University of Technology)
  • Published : 2015.05.18
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Abstract

Background: Cholangiocarcinoma (CHCA) is serious public health problem in Thailand, especially in the northeastern and northern regions. CHCA is known as one of the most aggressive malignant tumors associated with local invasion and a high rate of metastasis. A crucial step in the invasion process is the proteolytic degradation of the extracellular matrix (ECM) and basal membranes, for which several studies have shown a critical role played by matrix metalloproteinase-11 (MMP-11). Objective: This study aim to detect MMP-11 expression in CHCA specimens and any correlation with survival time. Materials and Methods: A retrospective analysis was conducted of 30 patients with CHCA in Rajvithi hospital, who had undergone immunohistochemical staining of MMP-11. Relationships between clinicopathological data and MMP-11 expression in CHCA specimens were analyzed by the ${\chi}^2$ test or Fisher's exact test. The estimated survival and the survival differences were analyzed by the Kaplan-Meier method and the log-rank test, respectively. Results: MMP-11 expression was found in 15 specimens (50%). The overall mean survival time is 237.0 days (95% CI 135.4-338.5, SD 271.9). Specimens with a positive MMP-11 had an average survival time of 136.7 days (95%CI 50.3-223.1, SD 156.0). Survival differences was signficant for the positive and negative MMP-11(p=0.022), but not well differentiated tumor and moderate to poor differentiated tumor (p=0.755), CA19-9 level of >1,000 and <1,000 (p=0.488), and between advanced and non-advanced staging (p=0.388). Conclusions: The positive MMP-11 expression indicates poor prognosis in CHCA specimens.

Keywords

References

  1. Akamatsu N, Sugawara Y, Hashimoto D (2011). Surgical strategy for bile duct cancer: advances and current limitations. World J Clin Oncol, 10, 94-107.
  2. Amalinei C, Caruntu ID, Giusca SE, et al (2010). Matrix metalloproteinases involvement in pathologic conditions. Rom J Morphol Embryol, 51, 215-28.
  3. Basset P, Bellocq JP, Wolf C, et al (1990). A novel Metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. Nature, 348, 699-704. https://doi.org/10.1038/348699a0
  4. Basset P, Wolf C, Chambon P (1993). Expression of the stromelysin-3 gene in fibroblastic cells of invasive carcinomas of the breast and other human tissues: a review. Breast Cancer Res Treat, 24, 185-93. https://doi.org/10.1007/BF01833259
  5. Basset P, Wolf C, Rouyer N, et al (1994). Stromelysin-3 in stromal tissue as a control factor in breast cancer behavior. Cancer, 74, 1045-9. https://doi.org/10.1002/1097-0142(19940801)74:3+<1045::AID-CNCR2820741511>3.0.CO;2-7
  6. Bourboulia D, Stetler-Stevenson WG (2010). Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs): Positive and negative regulators in tumor cell adhesion. Semin Cancer Biol, 20, 161-8. https://doi.org/10.1016/j.semcancer.2010.05.002
  7. Brasse D, Mathelin C, Leroux K, et al (2010). Matrix metalloproteinase 11/stromelysin-3 exerts both activator and repressor functions during the hematogenous metastatic process in mice. Int J Cancer, 127, 1347-55. https://doi.org/10.1002/ijc.25309
  8. Curran S, Murray GI (1999). Matrix metalloproteinases in tumour invasion and metastasis. J Pathol, 189, 300-8. https://doi.org/10.1002/(SICI)1096-9896(199911)189:3<300::AID-PATH456>3.0.CO;2-C
  9. Delany AM, Canalis E (2001). The metastasis-associated metalloproteinase stromelysin-3 is induced by transforming growth factor-beta in osteoblasts and fibroblasts. Endocrinology, 142, 1561-6.
  10. Deng H, Guo RF, Li WM, et al (2005). Matrix metalloproteinase 11 depletion inhibits cell proliferation in gastric cancer cells. Biochem Biophys Res Commun, 326, 274-81. https://doi.org/10.1016/j.bbrc.2004.11.027
  11. Fromigue O, Louis K, Wu E, et al (2003). Active stromelysin-3 (MMP-11) increases MCF-7 survival in three-dimensional Matrigel culture via activation of p42/p44 MAP-kinase. Int J Cancer, 106, 355-63. https://doi.org/10.1002/ijc.11232
  12. Gialeli C, Theocharis AD, Karamanos NK (2011). Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J, 278, 16-27. https://doi.org/10.1111/j.1742-4658.2010.07919.x
  13. Green A, Uttaravichien T, Bhudhisawasdi V, et al (1991). Cholangiocarcinoma in north east Thailand. A hospital-based study. Trop Geogr Med, 43, 193-8.
  14. IARC (1994). Infection with liver flukes (Opisthorchis viverrini, Opisthorchis felineus and Clonrochis sinensis). IARC Monogr Eval Carcinog Risks of Hum, 61, 121-75.
  15. Kaewpitoon N, Kaewpitoon SJ, Pengsaa P, et al (2008). Opisthorchis viverrini: the carcinogenic human liver fluke. World J Gastroenterol, 7, 666-74.
  16. Keeratichamroen S, Leelawat K, Thongtawee T, et al (2011). Expression of CD24 in cholangiocarcinoma cells is associated with disease progression and reduced patient survival. Int J Oncol, 39, 873-81.
  17. Linder C, Engel G, Auer G, et al (1997). Distribution of stromelysin-3 mRNA transcripts and microvessels in human breast carcinomas. Breast Cancer Res Treat, 42, 207-13. https://doi.org/10.1023/A:1005769622570
  18. Noel AC, Lefebvre O, Maquoi E, Vet al (1996). Stromelysin-3 expression promotes tumor take in nude mice. J Clin Invest, 97, 1924-30. https://doi.org/10.1172/JCI118624
  19. Nonsrijun N, Mitchai J, Brown K, et al (2013). Expression of MMP-11 is significantly associated with survival in prostatic adenocarcinoma. High levels may potentially be used for prediction of a poor prognosis. Asian Pac J Cancer Prev, 14, 3331-5. https://doi.org/10.7314/APJCP.2013.14.5.3331
  20. Peruzzi D, Mori F, Conforti A, et al (2009). MMP11: a novel target antigen for cancer immunotherapy. Clin Cancer Res, 15, 4104-13. https://doi.org/10.1158/1078-0432.CCR-08-3226
  21. Rouyer N, Wolf C, Chenard MP, et al (1994). Stromelysin-3 gene expression in human cancer: an overview. Invasion Metastasis, 14, 269-75.
  22. Shin HR, Oh JK, Masuyer E, et al (2010). Epidemiology of cholangiocarcinoma: an update focusing on risk factors. Cancer Sci, 101, 579-85. https://doi.org/10.1111/j.1349-7006.2009.01458.x
  23. Sripa B, Kaewkes S, Sithithaworn P, Met al (2007). Liver fluke induces cholangiocarcinoma. PLoS Med, 4, e201. https://doi.org/10.1371/journal.pmed.0040201
  24. Thamavit W, Bhamarapravati N, Sahaphong S, et al (1978). Effects of dimethylnitrosamine on induction of cholangiocarcinoma in Opisthorchis viverrini-infected Syrian golden hamsters. Cancer Res, 38, 4634-9.
  25. Thunyaharn N, Promthet S, Wiangnon S, Set al (2013). Survival of cholangiocarcinoma patients in northeastern Thailand after supportive treatment. Asian Pac J Cancer Prev, 14, 7029-32. https://doi.org/10.7314/APJCP.2012.14.11.7029
  26. Zhao ZS, Chu YQ, Ye ZY, et al (2010). Overexpression of matrix metalloproteinase 11 in human gastric carcinoma and its clinicopathologic significance. Hum Pathol, 41, 686-96. https://doi.org/10.1016/j.humpath.2009.10.010

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