Overexpression of PITPNM3 promotes hepatocellular carcinoma cell metastasis

详细信息    查看全文

• 作者：Chonghua He (1) (2)
  Shicheng Su (1) (2)
  Fei Chen (1) (2)
  Di Huang (1) (2)
  Fang Zheng (1)
  Wei Huang (1) (2)
  Jianing Chen (1) (2)
  Xiuying Cui (1)
  Qiang Liu (1) (2)
  Erwei Song (1) (2)
  Herui Yao (1) (3)
  Yujie Liu (1) (2)
  
• 关键词：PITPNM3 ; Hepatocellular carcinoma ; Invasion ; Metastasis
• 刊名：Chinese Science Bulletin
• 出版年：2014
• 出版时间：April 2014
• 年：2014
• 卷：59
• 期：12
• 页码：1326-1333
• 全文大小：1,552 KB
• 参考文献：1. Siegel R, Naishadham D, Jemal A (2012) Cancer statistics, 2012. CA Cancer J Clin 62:10-9 CrossRef
  2. Siegel R, Naishadham D, Jemal A (2013) Cancer statistics, 2013. CA Cancer J Clin 63:11-0 CrossRef
  3. Yang JD, Roberts LR (2010) Hepatocellular carcinoma: a global view. Nat Rev Gastroenterol Hepatol 7:448-58 CrossRef
  4. Jemal A, Bray F, Center MM et al (2011) Global cancer statistics. CA Cancer J Clin 61:69-0 CrossRef
  5. Yuen MF, Hou JL, Chutaputti A (2009) Hepatocellular carcinoma in the Asia pacific region. J Gastroenterol Hepatol 24:346-53 CrossRef
  6. Poon D, Anderson BO, Chen LT et al (2009) Management of hepatocellular carcinoma in Asia: consensus statement from the Asian Oncology Summit 2009. Lancet Oncol 10:1111-118 CrossRef
  7. Gupta GP, Massagué J (2006) Cancer metastasis: building a framework. Cell 127:679-95 CrossRef
  8. Poon RT, Fan ST, Wong J (2000) Risk factors, prevention, and management of postoperative recurrence after resection of hepatocellular carcinoma. Ann Surg 232:10-4 CrossRef
  9. Hanahan D, Weinberg RA (2000) The hallmarks of cancer. Cell 100:57-0 CrossRef
  10. Hanahan D, Weinberg RA (2011) Hallmarks of cancer: the next generation. Cell 144:646-74 CrossRef
  11. Karnoub AE, Weinberg RA (2007) Chemokine networks and breast cancer metastasis. Breast Dis 26:75-5
  12. Budhu A, Wang XW (2012) Transforming the microenvironment: a trick of the metastatic cancer cell. Cancer Cell 22:279-80 CrossRef
  13. Fidler IJ (2003) The pathogenesis of cancer metastasis: the ‘seed and soil-hypothesis revisited. Nat Rev Cancer 3:1- CrossRef
  14. Joyce JA, Pollard JW (2008) Microenvironmental regulation of metastasis. Nat Rev Cancer 9:239-52 CrossRef
  15. Whiteside TL (2008) The tumor microenvironment and its role in promoting tumor growth. Oncogene 27:5904-912 CrossRef
  16. Hernandez-Gea V, Toffanin S, Friedman SL et al (2013) Role of the microenvironment in the pathogenesis and treatment of hepatocellular carcinoma. Gastroenterology 144:512-27 CrossRef
  17. Calon A, Espinet E, Palomo-Ponce S et al (2012) Dependency of colorectal cancer on a TGF-β-driven program in stromal cells for metastasis initiation. Cancer Cell 22:571-84 CrossRef
  18. Goetz JG, Minguet S, Navarro-Lérida I et al (2011) Biomechanical remodeling of the microenvironment by stromal caveolin-1 favors tumor invasion and metastasis. Cell 146:148-63 CrossRef
  19. McMillin DW, Negri JM, Mitsiades CS (2013) The role of tumor–stromal interactions in modifying drug response: challenges and opportunities. Nat Rev Drug Discov 12:217-28 CrossRef
  20. Roussos ET, Condeelis JS, Patsialou A (2011) Chemotaxis in cancer. Nat Rev Cancer 11:573-87 CrossRef
  21. Luker KE, Lewin SA, Mihalko LA et al (2012) Scavenging of CXCL12 by CXCR7 promotes tumor growth and metastasis of CXCR4-positive breast cancer cells. Oncogene 31:4750-758 CrossRef
  22. Wu BL, Chien EY, Mol CD et al (2010) Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists. Science 330:1066-071 CrossRef
  23. Lazennec G, Richmond A (2010) Chemokines and chemokine receptors: new insights into cancer-related inflammation. Trends Mol Med 16:133-44 CrossRef
  24. Balkwill F (2004) Cancer and the chemokine network. Nat Rev Cancer 4:540-50 CrossRef
  25. Chew V, Chen J, Lee D et al (2012) Chemokine-driven lymphocyte infiltration: an early intratumoral event determining long-term survival in resectable hepatocellular carcinoma. Gut 61:427-38 CrossRef
  26. Dorsam RT, Gutkind JS (2007) G-protein-coupled receptors and cancer. Nat Rev Cancer 7:79-4 CrossRef
  27. Teicher BA, Fricker SP (2010) CXCL12 (SDF-1)/CXCR4 pathway in cancer. Clin Cancer Res 16:2927-931 CrossRef
  28. Gao Q, Zhao YJ, Wang XY et al (2012) CXCL6 upregulation contributes to a proinflammatory tumor microenvironment that drives metastasis and poor patient outcomes in hepatocellular carcinoma. Cancer Res 72:3546-556 CrossRef
  29. Chen J, Yao Y, Gong C et al (2011) CCL18 from tumor-associated macrophages promotes breast cancer metastasis via PITPNM3. Cancer Cell 19:541-55 CrossRef
  30. Lev S, Hernandez J, Martinez R et al (1999) Identification of a novel family of targets of PYK2 related to drosophila retinal degeneration B (rdgB) protein. Mol Cell Biol 19:2278-288
  31. Bianchi-Smiraglia A, Paesante S, Bakin AV (2012) Integrin beta5 contributes to the tumorigenic potential of breast cancer cells through the Src-FAK and MEK-ERK signaling pathways. Oncogene 32:3049-058 CrossRef
  32. Frame MC (2002) Src in cancer: deregulation and consequences for cell behavior. Biochim Biophys Acta 1602:114-30
  33. Genua M, Xu SQ, Buraschi S et al (2012) Proline-Rich Tyrosine Kinase 2 (Pyk2) Regulates IGF-I-Induced Cell Motility and Invasion of Urothelial Carcinoma Cells. PLoS One 7:e40148 CrossRef
  34. Strieter RM (2001) Chemokines: not just leukocyte chemoattractants in the promotion of cancer. Nat Immunol 2:285-86 CrossRef
  35. Catusse J, Wollner S, Leick M et al (2010) Attenuation of CXCR4 responses by CCL18 in acute lymphocytic leukemia B cells. J Cell Physiol 225:792-00 CrossRef
  36. Nada? P, Charbonnier AS, Chenivesse C et al (2006) Involvement of CCL18 in allergic asthma. J Immunol 176:6286-293
  37. Adema GJ, Hartgers F, Verstraten R et al (1997) A dendritic-cell-derived C–C chemokine that preferentially attracts naive T cells. Nature 387:713-17 CrossRef
  38. Prasse A, Pechkovsky DV, Toews GB et al (2007) CCL18 as an indicator of pulmonary fibrotic activity in idiopathic interstitial pneumonias and systemic sclerosis. Arthritis Rheumatol 56:1685-693 CrossRef
  39. Pochetuhen K, Luzina IG, Lockatell V et al (2007) Complex regulation of pulmonary inflammation and fibrosis by CCL18. Am J Pathol 171:428-37 CrossRef
  40. Günther C, Bello-Fernandez C, Kopp T et al (2005) CCL18 is expressed in atopic dermatitis and mediates skin homing of human memory T cells. J Immunol 174:1723-728
  
• 作者单位：Chonghua He (1) (2)
  Shicheng Su (1) (2)
  Fei Chen (1) (2)
  Di Huang (1) (2)
  Fang Zheng (1)
  Wei Huang (1) (2)
  Jianing Chen (1) (2)
  Xiuying Cui (1)
  Qiang Liu (1) (2)
  Erwei Song (1) (2)
  Herui Yao (1) (3)
  Yujie Liu (1) (2)
  
  1. Guangdong Provincial Key Laboratory of Malignant Tumor Epigenetics and Gene Regulation, Medical Research Center, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, China
  2. Department of Breast Surgery, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, China
  3. Department of Oncology, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, 510120, China
  
• ISSN：1861-9541

文摘

A previous study indicated that C–C chemokine (C–C motif) ligand 18 (CCL18) is capable of inducing tumor cell invasion and metastasis by interacting with receptor membrane-associated phosphatidylinositol transfer protein 3 (PITPNM3) in breast cancer cells. The present study aims to investigate the correlation between the PITPNM3 expression and metastasis in hepatocellular carcinoma (HCC). Real-time quantitative polymerase chain reaction and Western blot were performed to detect the expression pattern of PITPNM3 in patient samples and HCC cell lines. Wound-healing and transwell chamber assays were performed to assess the migration and invasiveness of HCC cells, and the activation of the signaling protein downstream of PITPNM3 was also detected by Western blot and immunofluorescence. The results revealed that PITPNM3 was upregulated in HCC tissue compared to matched normal liver tissue. Silencing the expression of PITPNM3 by specific siRNAs markedly attenuated the invasive and metastatic abilities of HCC cells, whereas the upregulation of PITPNM3 significantly increased HCC cell mobility. Furthermore, inhibiting the expression of PITPNM3 suppressed the activation of Pyk2, FAK, and Src, while overexpression of PITPNM3 enhanced the phosphorylation of FAK and Src in HCC cells. Besides, suppression of Pyk2 can also impair the clustering of integrin. These results imply that PITPNM3 is a vital determinant of HCC migration and invasion.