Asian Pacific Journal of Cancer Prevention

Asian Pacific Journal of Cancer Prevention (아시아태평양암예방학회)
권호 표지
DOI QR코드

DOI QR Code

Identification of Histone Deacetylase 1 Protein Complexes in Liver Cancer Cells

  • Farooq, Muhammad (Bioproducts Research Group, Department of Zoology, College of Science, King Saud University) ;
  • Hozzein, Wael N. (Bioproducts Research Group, Department of Zoology, College of Science, King Saud University) ;
  • Elsayed, Elsayed A. (Bioproducts Research Group, Department of Zoology, College of Science, King Saud University) ;
  • Taha, Nael A. (Bioproducts Research Group, Department of Zoology, College of Science, King Saud University) ;
  • Wadaan, Mohammad A.M. (Bioproducts Research Group, Department of Zoology, College of Science, King Saud University)
  • Published : 2013.02.28
Download PDF
⟨ Previous Next ⟩

Abstract

Background: Hepatocellular carcinoma is one of the leading causes of mortalities worldwide. The search for new therapeutic targets is of utmost importance for improved treatment. Altered expression of HDAC1 in hepatocellular carcinoma (HCC) and its requirement for liver formation in zebrafish, suggest that it may regulate key events in liver carcinogenesis and organogenesis. However, molecular mechanisms of HDAC1 action in liver carcinogenesis are largely unknown. The present study was conducted to identify HDAC1 interacting proteins in HepG2 cells using modified SH-double-affinity purification coupled with liquid mass spectrophotemetery. Materials and Methods: HepG2 cells were transfected with a construct containing HDAC1 with a C-terminal strepIII-HA tag as bait. Bait proteins were confirmed to be expressed in HepG2 cells by western blotting and purified by double affinity columns and protein complexes for analysis on a Thermo LTQ Orbitrap XL using a C18 nano flow ESI liquid chromatography system. Results: There were 27 proteins which showed novel interactions with HDAC1 identified only in this study, while 14 were among the established interactors. Various subunits of T complex proteins (TCP1) and prefoldin proteins (PFDN) were identified as interacting partners that showed high affinity with HDAC1 in HepG2 cells. Conclusions: The double affinity purification method adopted in this study was very successful in terms of specificity and reproducibility. The novel HDAC1 complex identified in this study could be better therapeutic target for treatment of hepatocellular carcinoma.

Keywords

References

  1. Brinke A, Green PM, Giannelli F (1997). Characterization of the gene (VBP1) and transcript for the von Hippel-Lindau binding protein and isolation of the highly conserved murine homologue. Genomics, 45, 105-12. https://doi.org/10.1006/geno.1997.4902
  2. Coradini D, Speranza A (2005). Histone deacetylase inhibitors for treatment of hepatocellular carcinoma. Acta Pharmacol Sin, 26, 1025-33. https://doi.org/10.1111/j.1745-7254.2005.00195.x
  3. Delcuve GP, Khan DH, Davie JR (2013). Targeting class I histone deacetylases in cancer therapy. Expert Opin Ther Targets, 17, 29-41. https://doi.org/10.1517/14728222.2013.729042
  4. Farooq M, Sulochana KN, Pan X, et al (2008). Histone deacetylase 3 (hdac3) is specifically required for liver development in zebrafish. Dev Biol, 317, 336-53. https://doi.org/10.1016/j.ydbio.2008.02.034
  5. Fujioka Y, Taira T, Maeda Y, et al (2001). MM-1, a c-Myc-binding protein, is a candidate for a tumor suppressor in leukemia/lymphoma and tongue cancer. J Biol Chem, 276, 45137-44. https://doi.org/10.1074/jbc.M106127200
  6. Gahr S, Peter G, Wissniowski TT, et al (2008). The histone-deacetylase inhibitor MS-275 and the CDK-inhibitor CYC-202 promote anti-tumor effects in hepatoma cell lines. Oncol Rep, 20, 1249-56.
  7. Gingras AC, Gstaiger M, Raught B, Aebersold R (2007). Analysis of protein complexes using mass spectrometry. Nat Rev Mol Cell Biol, 8, 645-54. https://doi.org/10.1038/nrm2208
  8. Glatter T, Wepf A, Aebersold R, Gstaiger M (2009). An integrated workflow for charting the human interaction proteome: insights into the PP2A system. Mol Syst Biol, 5, 237.
  9. Guenther MG, Barak O, Lazar MA (2001). The SMRT and N-CoR corepressors are activating cofactors for histone deacetylase 3. Mol Cell Biol, 21, 6091-101. https://doi.org/10.1128/MCB.21.18.6091-6101.2001
  10. Guenther MG, Yu J, Kao GD, Yen TJ, Lazar MA (2002). Assembly of the SMRT-histone deacetylase 3 repression complex requires the TCP-1 ring complex. Genes Dev, 16, 3130-5. https://doi.org/10.1101/gad.1037502
  11. Halkidou K, Gaughan L, Cook S, et al (2004). Upregulation and nuclear recruitment of HDAC1 in hormone refractory prostate cancer. Prostate, 59, 177-89. https://doi.org/10.1002/pros.20022
  12. Ito T, Chiba T, Ozawa R, et al (2001). A comprehensive two-hybrid analysis to explore the yeast protein interactome. Proc Natl Acad Sci USA, 98, 4569-74. https://doi.org/10.1073/pnas.061034498
  13. Jemal A, Bray F, Center MM, et al (2011). Global cancer statistics. CA Cancer J Clin, 61, 69-90. https://doi.org/10.3322/caac.20107
  14. Junttila MR, Saarinen S, Schmidt T, Kast J, Westermarck J (2005). Single-step Strep-tag purification for the isolation and identification of protein complexes from mammalian cells. Proteomics, 5, 1199-203. https://doi.org/10.1002/pmic.200400991
  15. Karagianni P, Wong J (2007). HDAC3: taking the SMRT-N-CoRrect road to repression. Oncogene, 26, 5439-49. https://doi.org/10.1038/sj.onc.1210612
  16. Kocher T, Superti-Furga G (2007). Mass spectrometry-based functional proteomics: from molecular machines to protein networks. Nat Methods, 4, 807-15. https://doi.org/10.1038/nmeth1093
  17. Lachenmayer A, Toffanin S, Cabellos L, et al (2012). Combination therapy for hepatocellular carcinoma: additive preclinical efficacy of the HDAC inhibitor panobinostat with sorafenib. J Hepatol, 56, 1343-50. https://doi.org/10.1016/j.jhep.2012.01.009
  18. Lamesch P, Li N, Milstein S, et al (2007). hORFeome v3.1: a resource of human open reading frames representing over 10,000 human genes. Genomics, 89, 307-15. https://doi.org/10.1016/j.ygeno.2006.11.012
  19. Lin HY, Chen CS, Lin SP, Weng JR (2006). Targeting histone deacetylase in cancer therapy. Med Res Rev, 26, 397-413. https://doi.org/10.1002/med.20056
  20. Mori K, Maeda Y, Kitaura H, et al (1998). MM-1, a novel c-Myc-associating protein that represses transcriptional activity of c-Myc. J Biol Chem, 273, 29794-800. https://doi.org/10.1074/jbc.273.45.29794
  21. Myung JK, Afjehi-Sadat L, Felizardo-Cabatic M, Slavc I, Lubec G (2004). Expressional patterns of chaperones in ten human tumor cell lines. Proteome Sci, 2, 8. https://doi.org/10.1186/1477-5956-2-8
  22. Nakagawa M, Oda Y, Eguchi T, et al (2007). Expression profile of class I histone deacetylases in human cancer tissues. Oncol Rep, 18, 769-74.
  23. Noel ES, Casal-Sueiro A, Busch-Nentwich E, et al (2008).Organ-specific requirements for Hdac1 in liver and pancreas formation. Dev Biol, 322, 237-50. https://doi.org/10.1016/j.ydbio.2008.06.040
  24. Olsen JV, Schwartz JC, Griep-Raming J, et al (2009). A dual pressure linear ion trap Orbitrap instrument with very high sequencing speed. Mol Cell Proteomics, 8, 2759-69. https://doi.org/10.1074/mcp.M900375-MCP200
  25. Pathil A, Armeanu S, Venturelli S, et al (2006). HDAC inhibitor treatment of hepatoma cells induces both TRAIL-independent apoptosis and restoration of sensitivity to TRAIL. Hepatology, 43, 425-34. https://doi.org/10.1002/hep.21054
  26. Qian-Lin Z, Ting-Feng W, Qi-Feng C, Min-Hua Z, Ai-Guo L (2010). Inhibition of cytosolic chaperonin CCTzeta-1 expression depletes proliferation of colorectal carcinoma in vitro. J Surg Oncol, 102, 419-23. https://doi.org/10.1002/jso.21625
  27. Quint K, Agaimy A, Di Fazio P, et al (2011). Clinical significance of histone deacetylases 1, 2, 3, and 7: HDAC2 is an independent predictor of survival in HCC. Virchows Arch, 459, 129-39. https://doi.org/10.1007/s00428-011-1103-0
  28. Satou A, Taira T, Iguchi-Ariga SM, Ariga H (2001). A novel transrepression pathway of c-Myc. Recruitment of a transcriptional corepressor complex to c-Myc by MM-1, a c-Myc-binding protein. J Biol Chem, 276, 46562-7. https://doi.org/10.1074/jbc.M104937200
  29. Tsuchiya H, Iseda T, Hino O (1996). Identification of a novel protein (VBP-1) binding to the von Hippel-Lindau (VHL) tumor suppressor gene product. Cancer Res, 56, 2881-5.
  30. Uetz P, Giot L, Cagney G, et al (2000). A comprehensive analysis of protein-protein interactions in Saccharomyces cerevisiae. Nature, 403, 623-7. https://doi.org/10.1038/35001009
  31. Vainberg IE, Lewis SA, Rommelaere H, et al (1998). Prefoldin, a chaperone that delivers unfolded proteins to cytosolic chaperonin. Cell, 93, 863-73. https://doi.org/10.1016/S0092-8674(00)81446-4
  32. Venturelli S, Armeanu S, Pathil A, et al (2007). Epigenetic combination therapy as a tumor-selective treatment approach for hepatocellular carcinoma. Cancer, 109, 2132-41. https://doi.org/10.1002/cncr.22652
  33. Walhout AJ, Sordella R, Lu X, et al (2000). Protein interaction mapping in C. elegans using proteins involved in vulval development. Science, 287, 116-22. https://doi.org/10.1126/science.287.5450.116
  34. Wen YD, Perissi V, Staszewski LM, et al (2000). The histone deacetylase-3 complex contains nuclear receptor corepressors. Proc Natl Acad Sci USA, 97, 7202-7. https://doi.org/10.1073/pnas.97.13.7202
  35. Wilson AJ, Byun DS, Popova N, et al (2006). Histone deacetylase 3 (HDAC3) and other class I HDACs regulate colon cell maturation and p21 expression and are deregulated in human colon cancer. J Biol Chem, 281, 13548-58. https://doi.org/10.1074/jbc.M510023200
  36. Witt O, Deubzer HE, Milde T, Oehme I (2009). HDAC family: What are the cancer relevant targets? Cancer Lett, 277, 8-21. https://doi.org/10.1016/j.canlet.2008.08.016
  37. Wong CW, Privalsky ML (1998). Transcriptional repression by the SMRT-mSin3 corepressor: multiple interactions, multiple mechanisms, and a potential role for TFIIB. Mol Cell Biol, 18, 5500-10.
  38. Wu LM, Yang Z, Zhou L, et al (2010). Identification of histone deacetylase 3 as a biomarker for tumor recurrence following liver transplantation in HBV-associated hepatocellular carcinoma. PLoS One, 5, 14460. https://doi.org/10.1371/journal.pone.0014460
  39. Yang Z, Zhou L, Wu LM, et al (2010). Combination of polymorphisms within the HDAC1 and HDAC3 gene predict tumor recurrence in hepatocellular carcinoma patients that have undergone transplant therapy. Clin Chem Lab Med, 48, 1785-91.
  40. Yokota S, Yamamoto Y, Shimizu K, et al (2001). Increased expression of cytosolic chaperonin CCT in human hepatocellular and colonic carcinoma. Cell Stress Chaperones, 6, 345-50. https://doi.org/10.1379/1466-1268(2001)006<0345:IEOCCC>2.0.CO;2
  41. Yue F, Wang LS, Xia L, et al (2009). Modulated T-complex protein 1 zeta and peptidyl-prolyl cis-trans isomerase B are two novel indicators for evaluating lymph node metastasis in colorectal cancer: Evidence from proteomics and bioinformatics. Proteomics Clin Appl, 3, 1225-35. https://doi.org/10.1002/prca.200900028
  42. Zhang Z, Yamashita H, Toyama T, et al (2005). Quantitation of HDAC1 mRNA expression in invasive carcinoma of the breast*. Breast Cancer Res Treat, 94, 11-6. https://doi.org/10.1007/s10549-005-6001-1

Cited by

  1. Epigenetic targets in hepatocellular carcinoma cells: identification of chaperone protein complexes with histone deacetylases vol.5, pp.5, 2013, https://doi.org/10.2217/epi.13.45
  2. In vitro Evaluation of Cytotoxic Activities of Essential Oil from Moringa oleifera Seeds on HeLa, HepG2, MCF-7, CACO-2 and L929 Cell Lines vol.16, pp.11, 2015, https://doi.org/10.7314/APJCP.2015.16.11.4671
  3. Targeting Histone Deacetylases in Diseases: Where Are We? vol.23, pp.1, 2015, https://doi.org/10.1089/ars.2013.5776
  4. Changes in the in vitro activity of platinum drugs when administered in two aliquots vol.16, pp.1, 2016, https://doi.org/10.1186/s12885-016-2731-1
  5. Prefoldin 1 promotes EMT and lung cancer progression by suppressing cyclin A expression vol.36, pp.7, 2017, https://doi.org/10.1038/onc.2016.257
  6. Differential HDAC1/2 network analysis reveals a role for prefoldin/CCT in HDAC1/2 complex assembly vol.8, pp.1, 2018, https://doi.org/10.1038/s41598-018-32009-w