Journal of Diagnostics Concepts & Practice >

2019 , Vol. 18 >Issue 2: 170 - 176

DOI: https://doi.org/10.16150/j.1671-2870.2019.02.010

Original articles

Study on ANP32B expression in hepatocellular carcinoma and its significance

Expand
  • 1. Center of Molecular Medicine, Ruijin Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200025, China
    2. Department of Hematology, Renji Hospital, Shanghai Jiao Tong University School of Medicine, Shanghai 200127, China

Received date: 2019-01-07

  Online published: 2019-04-25

Fold

Abstract

Objective: To investigate the ANP32B (acidic leucine-rich nuclear phosphoprotein 32B）expression in hepatocellular carcinoma and determine its clinical significance. Methods: The mRNA expression of ANP32B in hepatocellular carcinoma and the overall survival were analyzed using international public datasets. The protein expression of ANP32B in hepatocellular carcinoma tissue was detected by immunoblotting. ANP32B was knockdown by shRNA in HCC cell lines, and cell growth and colony formation were analyzed; cell cycle and apoptosis were detected by flow cytometry. Results: ANP32B mRNA and protein level were highly expressed in hepatocellular carcinoma, and the higher ANP32B mRNA level was associated with shorter survival. Knockdown of ANP32B in HCC cell lines inhibited cell growth and colony formation, induced cell cycle arrest and cell apoptosis. Conclusions: ANP32B is highly expressed in hepatocellular carcinoma. Knockdown of ANP32B in HCC cell lines inhibited cell growth and colony formation, induced cell cycle arrest and cell apoptosis.

Key words： Acidic leucine-rich nuclear phosphoprotein 32B (ANP32B); Hepatocellular carcinoma; Cell growth

Cite this article

ZHU Di, ZHU Xiaona, YANG Shuo, HE Ping, SHEN Shaoming, YU Yun . Study on ANP32B expression in hepatocellular carcinoma and its significance[J]. Journal of Diagnostics Concepts & Practice, 2019 , 18(2) : 170 -176 . DOI: 10.16150/j.1671-2870.2019.02.010

References

[1] Torre LA, Bray F, Siegel RL, et al. Global cancer statistics, 2012[J]. CA Cancer J Clin, 2015, 65(2):87-108.
[2] Reilly PT, Yu Y, Hamiche A, et al. Cracking the ANP 32 whips: important functions, unequal requirement, and hints at disease implications[J]. Bioessays, 2014, 36(11):1062-1071.
[3] Matilla A, Radrizzani M. The Anp32 family of proteins containing leucine-rich repeats[J]. Cerebellum. 2005; 4(1):7-18.
[4] Seo SB, McNamara P, Heo S, et al. Regulation of histone acetylation and transcription by INHAT, a human cellular complex containing the set oncoprotein[J]. Cell, 2001, 104(1):119-130.
[5] Obri A, Ouararhni K, Papin C, et al. ANP32E is a histone chaperone that removes H2A.Z from chromatin[J]. Nature, 2014, 505(7485):648-653.
[6] Habrukowich C, Han DK, Le A, et al. Sphingosine inte-raction with acidic leucine-rich nuclear phosphoprotein-32A (ANP32A) regulates PP2A activity and cyclooxygenase (COX)-2 expression in human endothelial cells[J]. J Biol Chem, 2010, 285(35):26825-26831.
[7] Katayose Y, Li M, Al-Murrani SW, et al. Protein phosphatase 2A inhibitors, I(1)(PP2A) and I(2)(PP2A), asso-ciate with and modify the substrate specificity of protein phosphatase 1[J]. J Biol Chem, 2000, 275(13):9209-9214.
[8] Fries B, Heukeshoven J, Hauber I, et al. Analysis of nucleocytoplasmic trafficking of the HuR ligand APRIL and its influence on CD83 expression[J]. J Biol Chem, 2007, 282(7):4504-4515.
[9] Moore MJ, Rosbash M. Cell biology. TAPping into mRNA export[J]. Science, 2001, 294(5548):1841-1842.
[10] Reilly PT, Afzal S, Gorrini C, et al. Acidic nuclear phosphoprotein 32kDa (ANP32) B-deficient mouse reveals a hierarchy of ANP32 importance in mammalian development[J]. Proc Natl Acad Sci U S A, 2011, 108(25):10243-10248.
[11] Yu Y, Wang LS, Shen SM, et al. Subcellular proteome analysis of camptothecin analogue NSC606985-treated acute myeloid leukemic cells[J]. J Proteome Res, 2007, 6(9):3808-3818.
[12] Yu Y, Shen SM, Zhang FF, et al. Acidic leucine-rich nuclear phosphoprotein 32 family member B (ANP32B) contributes to retinoic acid-induced differentiation of leukemic cells[J]. Biochem Biophys Res Commun, 2012, 423(4):721-725.
[13] Shen SM, Yu Y, Wu YL, et al. Downregulation of ANP32B, a novel substrate of caspase-3, enhances caspase-3 activation and apoptosis induction in myeloid leukemic cells[J]. Carcinogenesis, 2010, 31(3):419-426.
[14] Yang S, Zhou L, Reilly PT, et al. ANP32B deficiency impairs proliferation and suppresses tumor progression by regulating AKT phosphorylation[J]. Cell Death Dis, 2016, 7:e2082.
[15] Pan W, da Graca LS, Shao Y, et al. PHAPI/pp 32 suppresses tumorigenesis by stimulating apoptosis[J]. J Biol Chem, 2009, 284(11):6946-6954.
[16] Chen TH, Brody JR, Romantsev FE, et al. Structure of pp32, an acidic nuclear protein which inhibits oncogene-induced formation of transformed foci[J]. Mol Biol Cell, 1996, 7(12):2045-2056.
[17] Kadkol SS, Brody JR, Pevsner J, et al. Modulation of oncogenic potential by alternative gene use in human prostate cancer[J]. Nat Med, 1999, 5(3):275-279.
[18] Kadkol SS, El Naga GA, Brody JR, et al. Expression of pp 32 gene family members in breast cancer[J]. Breast Cancer Res Treat, 2001, 68(1):65-73.
[19] Zhu BD, Li XL, Liu Y, et al. Involvement of hepatopoie-tin Cn in the development of human hepatocellular car-cinoma[J]. Clin Exp Metastasis, 2010, 27(8):571-580.
[20] Tsukamoto Y, Uchida T, Karnan S, et al. Genome-wide analysis of DNA copy number alterations and gene expression in gastric cancer[J]. J Pathol, 2008, 216(4):471-482.
[21] Björck E, Ek S, Landgren O, et al. High expression of cyclin B1 predicts a favorable outcome in patients with follicular lymphoma[J]. Blood, 2005, 105(7):2908-2915.
[22] Ohno Y, Koizumi M, Nakayama H, et al. Downregulation of ANP32B exerts anti-apoptotic effects in hepatocellular carcinoma[J]. PLoS One, 2017, 12(5):e0177343.
[23] Tochio N, Umehara T, Munemasa Y, et al. Solution structure of histone chaperone ANP32B: interaction with core histones H3-H4 through its acidic concave domain[J]. J Mol Biol, 2010, 401(1):97-114.
[24] Munemasa Y, Suzuki T, Aizawa K, et al. Promoter region-specific histone incorporation by the novel histone chaperone ANP32B and DNA-binding factor KLF5[J]. Mol Cell Biol, 2008, 28(3):1171-1181.
Options
Outlines

/

〈 〉