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Phosphatase of regenerating liver-3 (PRL-3) is associated with metastasis and poor prognosis in gastric carcinoma
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  • 作者:Xiaofang Xing (1)
    Shenyi Lian (2)
    Ying Hu (3)
    Ziyu Li (4)
    Lianhai Zhang (4)
    Xianzi Wen (1)
    Hong Du (3)
    Yongning Jia (4)
    Zhixue Zheng (4)
    Lin Meng (2)
    Chengchao Shou (2)
    Jiafu Ji (1)
  • 关键词:PRL ; 3 ; Gastric cancer ; Prognosis ; Metastasis
  • 刊名:Journal of Translational Medicine
  • 出版年:2013
  • 出版时间:December 2013
  • 年:2013
  • 卷:11
  • 期:1
  • 全文大小:787 KB
  • 参考文献:1. Ferlay J, Shin HR, Bray F, Forman D, Mathers C, Parkin DM: / GLOBOCAN 2008, Cancer incidence and mortality worldwide. Lyon, France: International Agency for Research on Cancer; 2010.
    2. Al-Aidaroos AQ, Zeng Q: PRL-3 phosphatase and cancer metastasis. / J Cell Biochem 2010, 111:1087-098. CrossRef
    3. Saha S, Bardelli A, Buckhaults P, Velculescu VE, Rago C, St Croix B, Romans KE, Choti MA, Lengauer C, Kinzler KW, Vogelstein B: A phosphatase associated with metastasis of colorectal cancer. / Science 2001, 294:1343-346. CrossRef
    4. Peng L, Xing X, Li W, Qu L, Meng L, Lian S, Jiang B, Wu J, Shou C: PRL-3 promotes the motility, invasion, and metastasis of LoVo colon cancer cells through PRL-3-integrin beta1-ERK1/2 and-MMP2 signaling. / Mol Cancer 2009, 8:110. CrossRef
    5. Kato H, Semba S, Miskad UA, Seo Y, Kasuga M, Yokozaki H: High expression of PRL-3 promotes cancer cell motility and liver metastasis in human colorectal cancer: a predictive molecular marker of metachronous liver and lung metastases. / Clin Cancer Res 2004, 10:7318-328. CrossRef
    6. Xing X, Peng L, Qu L, Ren T, Dong B, Su X, Shou C: Prognostic value of PRL-3 overexpression in early stages of colonic cancer. / Histopathology 2009, 54:309-18. CrossRef
    7. Radke I, Gotte M, Kersting C, Mattsson B, Kiesel L, Wulfing P: Expression and prognostic impact of the protein tyrosine phosphatases PRL-1, PRL-2, and PRL-3 in breast cancer. / Br J Cancer 2006, 95:347-54. CrossRef
    8. Yamashita S, Masuda Y, Matsumoto K, Okumura Y, Matsuzaki H, Kurizaki T, Haga Y, Katafuchi S, Murayama T, Ikei S, Kawahara K: Down-regulation of the human PRL-3 gene is associated with the metastasis of primary non-small cell lung cancer. / Ann Thorac Cardiovasc Surg 2007, 13:236-39.
    9. Polato F, Codegoni A, Fruscio R, Perego P, Mangioni C, Saha S, Bardelli A, Broggini M: PRL-3 phosphatase is implicated in ovarian cancer growth. / Clin Cancer Res 2005, 11:6835-839. CrossRef
    10. Zhao WB, Li Y, Liu X, Zhang LY, Wang X: Evaluation of PRL-3 expression, and its correlation with angiogenesis and invasion in hepatocellular carcinoma. / Int J Mol Med 2008, 22:187-92.
    11. Miskad UA, Semba S, Kato H, Yokozaki H: Expression of PRL-3 phosphatase in human gastric carcinomas: close correlation with invasion and metastasis. / Pathobiology 2004, 71:176-84. CrossRef
    12. Li ZR, Wang Z, Zhu BH, He YL, Peng JS, Cai SR, Ma JP, Zhan WH: Association of tyrosine PRL-3 phosphatase protein expression with peritoneal metastasis of gastric carcinoma and prognosis. / Surg Today 2007, 37:646-51. CrossRef
    13. Wang Z, He YL, Cai SR, Zhan WH, Li ZR, Zhu BH, Chen CQ, Ma JP, Chen ZX, Li W, Zhang LJ: Expression and prognostic impact of PRL-3 in lymph node metastasis of gastric cancer: its molecular mechanism was investigated using artificial microRNA interference. / Int J Cancer 2008, 123:1439-447. CrossRef
    14. Pryczynicz A, Guzinska-Ustymowicz K, Chang XJ, Kisluk J, Kemona A: PTP4A3 (PRL-3) expression correlate with lymphatic metastases in gastric cancer. / Folia Histochem Cytobiol 2010, 48:632-36.
    15. Guzinska-Ustymowicz K, Pryczynicz A: PRL-3, an emerging marker of carcinogenesis, is strongly associated with poor prognosis. / Anticancer Agents Med Chem 2011, 11:99-08. CrossRef
    16. Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I: Structural insights into molecular function of the metastasis-associated phosphatase PRL-3. / J Biol Chem 2004, 279:11882-1889. CrossRef
    17. Peng L, Jin G, Wang L, Guo J, Meng L, Shou C: Identification of integrin alpha1 as an interacting protein of protein tyrosine phosphatase PRL-3. / Biochem Biophys Res Commun 2006, 342:179-83. CrossRef
    18. Forte E, Orsatti L, Talamo F, Barbato G, De Francesco R, Tomei L: Ezrin is a specific and direct target of protein tyrosine phosphatase PRL-3. / Biochim Biophys Acta 2008, 1783:334-44. CrossRef
    19. Wang H, Quah SY, Dong JM, Manser E, Tang JP, Zeng Q: PRL-3 down-regulates PTEN expression and signals through PI3K to promote epithelial-mesenchymal transition. / Cancer Res 2007, 67:2922-926. CrossRef
    20. Liu Y, Zhou J, Chen J, Gao W, Le Y, Ding Y, Li J: PRL-3 promotes epithelial mesenchymal transition by regulating cadherin directly. / Cancer Biol Ther 2009, 8:1352-359. CrossRef
    21. Guo K, Li J, Wang H, Osato M, Tang JP, Quah SY, Gan BQ, Zeng Q: PRL-3 initiates tumor angiogenesis by recruiting endothelial cells in vitro and in vivo. / Cancer Res 2006, 66:9625-635. CrossRef
    22. Al-Aidaroos AQ, Yuen HF, Guo K, Zhang SD, Chung TH, Chng WJ, Zeng Q: Metastasis-associated PRL-3 induces EGFR activation and addiction in cancer cells. / J Clin Invest 2013, 123:3459-471. CrossRef
    23. Kim KA, Song JS, Jee J, Sheen MR, Lee C, Lee TG, Ro S, Cho JM, Lee W, Yamazaki T, / et al.: Structure of human PRL-3, the phosphatase associated with cancer metastasis. / FEBS Lett 2004, 565:181-87. CrossRef
    24. Zeng Q, Dong JM, Guo K, Li J, Tan HX, Koh V, Pallen CJ, Manser E, Hong W: PRL-3 and PRL-1 promote cell migration, invasion, and metastasis. / Cancer Res 2003, 63:2716-722.
    25. Peng L, Li Y, Meng L, Shou C: Preparation and characterization of monoclonal antibody against protein tyrosine phosphatase PRL-3. / Hybrid Hybridomics 2004, 23:23-7. CrossRef
    26. Mayinuer A, Yasen M, Mogushi K, Obulhasim G, Xieraili M, Aihara A, Tanaka S, Mizushima H, Tanaka H, Arii S: Upregulation of protein tyrosine phosphatase type IVA member 3 (PTP4A3/PRL-3) is associated with tumor differentiation and a poor prognosis in human hepatocellular carcinoma. / Ann Surg Oncol 2013, 20:305-17. CrossRef
    27. De Palma M, Hanahan D: The biology of personalized cancer medicine: facing individual complexities underlying hallmark capabilities. / Mol Oncol 2012, 6:111-27. CrossRef
    28. Peng LR, Shou CC: Phosphatase of regenerating liver-3 (PRL-3) and tumor metastasis. / Zhonghua Zhong Liu Za Zhi 2007, 29:1-.
    29. Guo K, Li J, Tang JP, Koh V, Gan BQ, Zeng Q: Catalytic domain of PRL-3 plays an essential role in tumor metastasis: formation of PRL-3 tumors inside the blood vessels. / Cancer Biol Ther 2004, 3:945-51. CrossRef
    30. Cates CA, Michael RL, Stayrook KR, Harvey KA, Burke YD, Randall SK, Crowell PL, Crowell DN: Prenylation of oncogenic human PTP(CAAX) protein tyrosine phosphatases. / Cancer Lett 1996, 110:49-5. CrossRef
    31. Zeng Q, Si X, Horstmann H, Xu Y, Hong W, Pallen CJ: Prenylation-dependent association of protein-tyrosine phosphatases PRL-1, -2, and ? with the plasma membrane and the early endosome. / J Biol Chem 2000, 275:21444-1452. CrossRef
    32. Bessette DC, Wong PC, Pallen CJ: PRL-3: a metastasis-associated phosphatase in search of a function. / Cells Tissues Organs 2007, 185:232-36. CrossRef
    33. Zeng Q, Hong W, Tan YH: Mouse PRL-2 and PRL-3, two potentially prenylated protein tyrosine phosphatases homologous to PRL-1. / Biochem Biophys Res Commun 1998, 244:421-27. CrossRef
    34. Dumaual CM, Sandusky GE, Soo HW, Werner SR, Crowell PL, Randall SK: Tissue-specific alterations of PRL-1 and PRL-2 expression in cancer. / Am J Transl Res 2012, 4:83-01.
    35. Achiwa H, Lazo JS: PRL-1 tyrosine phosphatase regulates c-Src levels, adherence, and invasion in human lung cancer cells. / Cancer Res 2007, 67:643-50. CrossRef
    36. Winter-Vann AM, Casey PJ: Post-prenylation-processing enzymes as new targets in oncogenesis. / Nat Rev Cancer 2005, 5:405-12. CrossRef
    37. Chiu VK, Bivona T, Hach A, Sajous JB, Silletti J, Wiener H, Johnson RL 2nd, Cox AD, Philips MR: Ras signalling on the endoplasmic reticulum and the Golgi. / Nat Cell Biol 2002, 4:343-50.
    38. Di Paolo A, Danesi R, Caputo S, Macchia M, Lastella M, Boggi U, Mosca F, Marchetti A, Del Tacca M: Inhibition of protein farnesylation enhances the chemotherapeutic efficacy of the novel geranylgeranyltransferase inhibitor BAL9611 in human colon cancer cells. / Br J Cancer 2001, 84:1535-543. CrossRef
    39. Dowlati A, Kluge A, Nethery D, Halmos B, Kern JA: SCH66336, inhibitor of protein farnesylation, blocks signal transducer and activators of transcription 3 signaling in lung cancer and interacts with a small molecule inhibitor of epidermal growth factor receptor/human epidermal growth factor receptor 2. / Anticancer Drugs 2008, 19:9-6. CrossRef
  • 作者单位:Xiaofang Xing (1)
    Shenyi Lian (2)
    Ying Hu (3)
    Ziyu Li (4)
    Lianhai Zhang (4)
    Xianzi Wen (1)
    Hong Du (3)
    Yongning Jia (4)
    Zhixue Zheng (4)
    Lin Meng (2)
    Chengchao Shou (2)
    Jiafu Ji (1)

    1. Department of gastrointestinal translational research, Peking University Cancer Hospital & Institute, #52 Fu-Cheng Road, Hai-Dian District, Beijing, 100142, China
    2. Department of Biochemistry and Molecular Biology, Peking University Cancer Hospital & Institute, #52 Fu-Cheng Road, Hai-Dian District, Beijing, 100142, China
    3. Tissue bank, Peking University Cancer Hospital & Institute, Beijing, China
    4. Department of gastrointestinal surgery, Peking University Cancer Hospital & Institute, Beijing, China
  • ISSN:1479-5876
文摘
Background PRL-3 is a member of phosphatases of regenerating liver family, characterized by phosphatase active domain and C-terminal prenylation motif. Overexpression of PRL-3 has been implicated in multiple cancers. Here we examined the clinical significance of PRL-3 in gastric cancer together with its metastatic biological functions utilizing different structural mutants. Methods PRL-3 expression was analyzed immunohistochemically in 196 gastric cancer patients and 21 cases of liver metastasis. A series of wild type PRL-3 or its mutant plasmids were expressed in BGC823 cells to investigate the relationship between its catalytic activity, cellular localization and metastatic potential in vitro. Results Positive staining of PRL-3 was observed in 19.4% (38/196) gastric cancer tissues compared with 76.2% (16/21) in liver metastasis. Statistical analysis revealed that PRL-3 expression correlated with lymph node metastasis and vascular invasion (P-lt;-.05). Patients with high PRL-3 expression showed poorer 5-year overall survival (P--.011). Wild type PRL-3 expressing cells resulted in enhanced migration and invasion ability, which were greatly crippled in form of PRL-3(C104S) or PRL-3(ΔCAAX) mutants accompanied with its alteration in subcellular localization. Conclusions Metastasis associated protein PRL-3 may serve as a potential prognostic biomarker in human gastric cancer. Both the phosphatase catalytic activity and cellular localization are critical for its function.

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