Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
권호 표지

Talin1, a Valuable Marker for Diagnosis and Prognostic Assessment of Human Hepatocelluar Carcinomas

Zhang, Jian-Lin;Qian, Ye-Ben;Zhu, Li-Xin;Xiong, Qi-Ru

  • Published : 20111200
⟨ Previous Next ⟩

Abstract

Background/Aims: Hepatocellular carcinoma (HCC) is one of the most lethal and prevalent cancers in the human population. Despite its significance, there is only limited understanding of pathological mechanisms and therapeutic options. Talin1, a focal adhesion complex protein that is required for cell adhesion and motility, regulates integrin interactions with extracellular matrix (ECM). In the present study, we aimed to study the possible role of Talin1 in diagnosis and prognosis of HCC. Methods: Expression of Talin1 protein was detected in normal liver tissues (n=10), HCC tissues (n=32) and adjacent non-cancerous tissues (n=32) by immunohistochemistry and real time PCR. Results: While Talin1 was observed in all tissues, the protein and mRNA expression of Talin1 in HCC tissues was significantly lower than that in the adjacent non-cancerous tissues and normal liver tissues(P<0.05). In addition, the expression of Talin1 in HCCs was significantly correlated with pathological differentiation, integrity of the tumor capsule, portal vein tumor thrombus and tumor size (P<0.05). Conclusions: Talin1 is possibly involved in the process of the carcinogenesis, infiltration and metastasis of HCC and has potential as a marker for diagnosis and prognostic assessment.

Keywords

References

  1. Aravalli RN, Steer CJ, Cressman EN (2008). Molecular mechanisms of hepatocellular carcinoma. Hepatology, 48, 2047-63 https://doi.org/10.1002/hep.22580
  2. Chen H, Choudhury DM, Craig SW (2006). Coincidence of actin filaments and talin is required to activate vinculin. J Biol Chem, 281, 40389-98 https://doi.org/10.1074/jbc.M607324200
  3. Cheng C, Liu H, Ge H, et al (2007). Essential role of Src suppressed C kinase substrates in endothelial cell adhesion and spreading. Biochem Biophys Res Commun, 358, 342-8 https://doi.org/10.1016/j.bbrc.2007.04.147
  4. Farazi PA, DePinho RA (2006). Hepatocellular carcinoma pathogenesis: from genes to environment. Nat Rev Cancer, 6, 674-87 https://doi.org/10.1038/nrc1934
  5. Liang YL, Lei TW, Wu H, et al (2003). S-phase delay in human hepatocellular carcinoma cells induced by overexpression of integrin beta1. World J Gastroenterol, 9, 1689-96
  6. Ma HQ, Liang XT, Zhao JJ, et al (2009). Decreased expression of Neurensin-2 correlates with poor prognosis in hepatocellular carcinoma. World J Gastroenterol, 15, 4844-8 https://doi.org/10.3748/wjg.15.4844
  7. Martel V, Racaud-Sultan C, Dupe S, et al (2001). Conformation, localization, and integrin binding of talin depend on its interaction with phosphoinositides. J Biol Chem, 276, 21217-27 https://doi.org/10.1074/jbc.M102373200
  8. Matsushima-Nishiwaki R, Okuno M, Adachi S, et al (2001). Phosphorylation of retinoid X receptor alpha at serine 260 impairs its metabolism and function in human hepatocellular carcinoma. Cancer Res, 61, 7675-82
  9. Matsushima-Nishiwaki R, Okuno M, Takano Y, et al (2003). Molecular mechanism for growth suppression of human hepatocellular carcinoma cells by acyclic retinoid. Carcinogenesis, 24, 1353-9 https://doi.org/10.1093/carcin/bgg090
  10. Matsushima-Nishiwaki R, Shidoji Y, Nishiwaki S, (1996). Aberrant metabolism of retinoid X receptor proteins in human hepatocellular carcinoma. Mol Cell Endocrinol, 121, 179-90 https://doi.org/10.1016/0303-7207(96)03863-4
  11. Muto Y, Moriwaki H, Saito A (1999). Prevention of second primary tumors by an acyclic retinoid in patients with hepatocellular carcinoma. N Engl J Med, 340, 1046-7 https://doi.org/10.1056/NEJM199904013401315
  12. Qin LX, Tang ZY (2002). The prognostic molecular markers in hepatocellular carcinoma. World J Gastroenterol, 8, 385-92
  13. Qin LX, Tang ZY (2002). The prognostic molecular markers in hepatocellular carcinoma. World J Gastroenterol, 8, 385-92
  14. Sakamoto S, McCann RO, Dhir R, Kyprianou N (2010). Talin1 promotes tumor invasion and metastasis via focal adhesion signaling and anoikis resistance. Cancer Res, 70, 1885-95 https://doi.org/10.1158/0008-5472.CAN-09-2833
  15. Scibelli A, d'Angelo D, Pelagalli A, et al (2003). Expression levels of the focal adhesion-associated proteins paxillin and p130CAS in canine and feline mammary tumors. Vet Res, 34, 193-202 https://doi.org/10.1051/vetres:2002066
  16. Senetar MA, McCann RO (2005). Gene duplication and functional divergence during evolution of the cytoskeletal linker protein talin. Gene, 362, 141-52
  17. Senetar MA, Moncman CL, McCann RO (2007). Talin2 is induced during striated muscle differentiation and is targeted to stable adhesion complexes in mature muscle. Cell Motil Cytoskeleton, 64, 157-73 https://doi.org/10.1002/cm.20173
  18. Slater M, Cooper M, Murphy CR (2007). The cytoskeletal proteins alpha-actinin, Ezrin, and talin are De-expressed in endometriosis and endometrioid carcinoma compared with normal uterine epithelium. Appl Immunohistochem Mol Morphol, 15, 170-4 https://doi.org/10.1097/01.pai.0000194762.78889.26
  19. Tadokoro S, Shattil SJ, Eto K, et al (2003). Talin binding to integrin beta tails: a final common step in integrin activation. Science, 302, 103-6 https://doi.org/10.1126/science.1086652
  20. Tsujioka M, Yoshida K, Inouye K (2004). Talin B is required for force transmission in morphogenesis of dictyostelium. EMBO J, 23, 2216-25 https://doi.org/10.1038/sj.emboj.7600238
  21. Zhang X, Jiang G, Cai Y, et al (2008). Talin depletion reveals independence of initial cell spreading from integrin activation and traction. Nat Cell Biol, 10, 1062-8 https://doi.org/10.1038/ncb1765