Molecular Biology Reports

, Volume 37, Issue 3, pp 1627–1632 | Cite as

Curcumin decreases the expression of Pokemon by suppressing the binding activity of the Sp1 protein in human lung cancer cells

  • Jiajun Cui
  • Xianfeng Meng
  • Xudong Gao
  • Guangxuan Tan
Article

Abstract

Pokemon, which stands for POK erythroid myeloid ontogenic factor, can regulate expression of many genes and plays an important role in tumorigenesis. Curcumin, a natural and non-toxic yellow compound, has capacity for antioxidant, free radical scavenger, anti-inflammatory properties. Recent studies shows it is a potential inhibitor of cell proliferation in a variety of tumour cells. To investigate whether curcumin can regulate the expression of Pokemon, a series of experiments were carried out. Transient transfection experiments demonstrated that curcumin could decrease the activity of the Pokemon promoter. Western blot analysis suggested that curcumin could significantly decrease the expression of the Pokemon. Overexpression of Sp1 could enhance the activity of the Pokemon promoter, whereas knockdown of Sp1 could decrease its activity. More important, we also found that curcumin could decrease the expression of the Pokemon by suppressing the stimulation of the Sp1 protein. Therefore, curcumin is a potential reagent for tumour therapy which may target Pokemon.

Keywords

Pokemon Curcumin Promoter Sp1 Expression 

Abbreviations

Sp1

Specificity protein 1

ChIP

Chromatin immunoprecipitation assay

GAPDH

Glyceraldehydes-3-phsphate dehydrogenase

References

  1. 1.
    Satoskar RR, Shah SJ, Shenoy SG (1986) Evaluation of anti-inflammatory property of curcumin (diferuloyl methane) in patients with postoperative inflammation. Int J Clin Pharmacol Ther Toxicol 24:651–654PubMedGoogle Scholar
  2. 2.
    Joe B, Vijaykuma M, Lokesh BR (2004) Biological properties of curcumin-cellular and molecular mechanisms of action. Crit Rev Food Sci Nutr 44:97–111CrossRefPubMedGoogle Scholar
  3. 3.
    Moragoda L, Jaszewski R, Majumdar AP (2001) Curcumin induced modulation of cell cycle and apoptosis in gastric and colon cancer cells. Anticancer Res 21:873–878PubMedGoogle Scholar
  4. 4.
    Deeb D, Jiang H, Gao X, Al-Holou S et al (2004) Curcumin sensitizes prostate cancer cells to tumor necrosis factor-related apoptosis-in-inducing ligand/Apo2L by inhibiting nuclear factor-kappaB through suppression of IkappaBalpha phosphorylation. Mol Cancer Ther 3:803–812PubMedGoogle Scholar
  5. 5.
    Karunagaran D, Rashmi R, Kumar TR (2005) Induction of apoptosis by curcumin and its implications for cancer therapy. Curr Cancer Drug Targets 5:117–129CrossRefPubMedGoogle Scholar
  6. 6.
    Pessler F, Pendergrast PS, Hernandez N (1997) Purification and characterization of FBI-1, a cellular factor that binds to the human immunodeficiency virus type 1 inducer of short transcripts. Mol Cell Biol 17:3786–3798PubMedGoogle Scholar
  7. 7.
    Morrison DJ, Pendergrast PS, Stavropoulos P et al (1999) FBI-1, a factor that binds to the HIV-1 inducer of short transcripts (IST), is a POZ domain protein. Nucleic Acids Res 7:1251–1262CrossRefGoogle Scholar
  8. 8.
    Pendergrast PS, Wang C, Hernandez N et al (2002) FBI-1 can stimulate HIV-1 Tat activity and is targeted to a novel subnuclear domain that includes the Tat-P-TEFb-containing nuclear speckles. Mol Biol Cell 13:915–929CrossRefPubMedGoogle Scholar
  9. 9.
    Laudes M, Christodoulides C, Sewter C et al (2004) Role of the POZ zinc finger transcription factor FBI-1 in human and murine adipogenesis. J Biol Chem 279:11711–11718CrossRefPubMedGoogle Scholar
  10. 10.
    Widom RL, Lee JY, Joseph C et al (2001) The hcKrox gene family regulates multiple extracellular matrix genes. Matrix Biol 20:451–462CrossRefPubMedGoogle Scholar
  11. 11.
    Liu CJ, Prazak L, Fajardo et al (2004) Leukemia/lymphoma-related factor, a POZ domain-containing transcriptional repressor, interacts with histone deacetylase-1 and inhibits cartilage oligomeric matrix protein gene expression and chondrogenesis. J Biol Chem 279:47081–47091CrossRefPubMedGoogle Scholar
  12. 12.
    Pessler F, Hernandez N (2003) Flexible DNA binding of the BTB/POZ domain protein FBI-1. J Biol Chem 278:29327–29335CrossRefPubMedGoogle Scholar
  13. 13.
    Maeda T, Hobbs RM, Merghoub T et al (2005) Role of the proto-oncogene Pokemon in cellular transformation and ARF repression. Nature 433:278–285CrossRefPubMedGoogle Scholar
  14. 14.
    Maeda T, Hobbs RM, Pandolfi PP (2005) The transcription factor Pokemon: a new key player in cancer pathogenesis. Cancer Res 65:8575–8578CrossRefPubMedGoogle Scholar
  15. 15.
    Gidoni D, Dynan WS, Tjian R (1984) Multiple specific contacts between a mammalian transcription factor and its cognate promoters. Nature 312:409–413CrossRefPubMedGoogle Scholar
  16. 16.
    Suske G (1999) The Sp-family of transcription factors. Gene 238:291–300CrossRefPubMedGoogle Scholar
  17. 17.
    Matys V, Kel-Margoulis OV, Fricke E et al (2006) TRANSFAC® and its module TRANSCompel®: transcriptional gene regulation in eukaryotes. Nucleic Acids Res 34(1):D108–D110CrossRefPubMedGoogle Scholar
  18. 18.
    Choi WI, Jeon BN, Yun CO et al (2009) Proto-oncogene FBI-1 represses transcription of P21CIP1 by inhibition of transcription activation by p53 and Sp1. J Biol Chem 284:11711–11718Google Scholar
  19. 19.
    Hanif R, Qiao L, Shiff SJ, Rigas B (1997) Curcumin, a natural plant phenolic food additive, inhibits cell proliferation and induces cell cycle changes in colon adenocarcinoma cell lines by a prostaglandin-independent pathway. J Lab Clin Med 130:576–584CrossRefPubMedGoogle Scholar
  20. 20.
    Chen H, Zhang ZS, Zhang YL et al (1999) Curcumin inhibits cell proliferation by interfering with the cell cycle and inducing apoptosis in colon carcinoma cells. Anticancer Res 19:3675–3680PubMedGoogle Scholar
  21. 21.
    Chen YR, Tan TH (1998) Inhibition of the c-Jun N-terminal kinase (JNK) signaling pathway by curcumin. Oncogene 17:173–178CrossRefPubMedGoogle Scholar
  22. 22.
    Leu TH, Maa MC (2002) The molecular mechanisms for the anti-tumorigenic effect of curcumin. Curr Med Chem Anticancer Agents 2:357–370CrossRefPubMedGoogle Scholar
  23. 23.
    Lin JK, Pan MH, Lin-Shiau SY (2000) Recent studies on the biofunctions and biotransformations of curcumin. Biofactors 13:153–158CrossRefPubMedGoogle Scholar
  24. 24.
    Aggarwal BB, Kumar A, Bharti AC (2003) Anticancer potential of curcumin: preclinical and clinical studies. Anticancer Res 23:363–398PubMedGoogle Scholar
  25. 25.
    Chadalapala G, Jutooru I, Chintharlapalli S et al (2008) Curcumin decreases specificity protein expression in bladder cancer cell. Cancer Res 68:5345–5354CrossRefGoogle Scholar
  26. 26.
    Thayyullathil F, Chathoth S, Hago A et al (2008) Rapid reactive oxygen species (ROS) generation induced by curcumin leads to caspase-dependent and -independent apoptosis in L929 cells. Free Radic Biol Med 45:1403–1412CrossRefPubMedGoogle Scholar
  27. 27.
    Webster KA, Prentice H, Bishopric NH (2001) Oxidation of zinc finger transcription factors: physiological consequences. Antioxid Redox Signal 3:535–548CrossRefPubMedGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2009

Authors and Affiliations

  • Jiajun Cui
    • 1
    • 3
  • Xianfeng Meng
    • 2
  • Xudong Gao
    • 4
  • Guangxuan Tan
    • 1
  1. 1.Zhoukou Normal UniversityZhoukouPeople’s Republic of China
  2. 2.Tanshan Medical UniversityBeijingPeople’s Republic of China
  3. 3.Beijing Institute of BiotechnologyBeijingPeople’s Republic of China
  4. 4.307 Hospital of PLABeijingPeople’s Republic of China

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