Identification of Histone Deacetylase 1 Protein Complexes in Liver Cancer Cells

Farooq, Muhammad; Hozzein, Wael N.; Elsayed, Elsayed A.; Taha, Nael A.; Wadaan, Mohammad A.M.

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저자정보: 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)

저널정보: 아시아태평양암예방학회 Asian Pacific journal of cancer prevention : APJCP Asian Pacific journal of cancer prevention : APJCP 제14권 제2호

발행연도: 2013.1

수록면: 915 - 921 (7page)

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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.

#Histone deacetylase 1 #HDAC1) #double affinity tag purification #hepatocellular carcinoma

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Farooq, Muhammad

소속기관 Bioproducts Research Chair, Department of Zoology, College of Science, King Saud University