Skip to main content

Advertisement

Log in

An investigation of hormesis of trichloroethylene in L-02 liver cells by differential proteomic analysis

  • Published:
Molecular Biology Reports Aims and scope Submit manuscript

Abstract

Hormesis is the dose–response pattern of the biological responses to toxic chemicals, characterized by low-dose stimulation and high-dose inhibition. Although it is known that some cell types exhibit an adaptive response to low levels of cytotoxic agents, its molecular mechanism is still unclear and it has yet to be established whether this is a universal phenomenon that occurs in all cell types in response to exposure to every chemical. Trichloroethylene (TCE) is an organic solvent widely used and is released into the atmosphere from industrial degreasing operations. Acute (short-term) and chronic (long-term) inhalation exposure to trichloroethylene can affect the human health. In order to elucidate a cell-survival adaptive response of L-02 liver cells exposed to low dose of TCE, CCK-8 assay was used to assess cytotoxicity, and examined the possible mechanisms of hormesis by proteomics technology. We found that exposure of L-02 liver cells to low level of TCE resulted in adaptation to further exposure to higher level, about 1,000 protein-spots were obtained by two-dimensional electrophoresis (2-DE) and five protein spots were identified by matrix-assisted laser desorption/ionization mass spectrometry and tandem mass spectrometry sequencing of tryptic peptides. Our results suggest that a relationship may exist between identified proteins and TCE-induced hormesis, which are very useful for further study of the mechanism and risk assessment of TCE.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

References

  1. Calabrese EJ, Baldwin LA (2003) Hormesis: the dose–response revolution. Annu Rev Pharmacol Toxicol 43:175–197. doi:10.1146/annurev.pharmtox.43.100901.140223

    Article  CAS  PubMed  Google Scholar 

  2. Yu-Fei D, Yu-Xin Z (2003) The renew scan of central dogma in toxicology—the dose–effect relationship of intoxicant excitability and the effect to the development of toxicology. Foreign Med Sci 30:246–249 Section of Hygiene

    Google Scholar 

  3. Calabrese EJ (2004) Hormesis—basic, generalizable, central to toxicology and a method to improve the risk-assessment process. Int J Occup Environ Health 10:466–467

    PubMed  Google Scholar 

  4. Calabrese EJ (2005) Toxicological awakenings: the rebirth of hormesis as a central pillar of toxicology. Toxicol Appl Pharmacol 204:1–8. doi:10.1016/j.taap.2004.11.015

    Article  CAS  PubMed  Google Scholar 

  5. Ming-Xia H (2001) Advancement of trichloroethylene in toxicological research. Foreign Med Sci 28:155–158 Section of Hygiene

    Google Scholar 

  6. Gharahdaghi F, Weinberg CR, Meagher DA et al (1999) Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: a method for the removal of silver ions to enhance sensitivity. Electrophoresis 20:601–605. doi:10.1002/(SICI)1522-2683(19990301)20:3<601::AID-ELPS601>3.0.CO;2-6

    Article  CAS  PubMed  Google Scholar 

  7. Myung K, Braastad C, He DM et al (1998) KARP-1 is induced by DNA damage in a p53- and ataxia telangiectasia mutated-dependent fashion. Proc Natl Acad Sci USA 95:7664–7669. doi:10.1073/pnas.95.13.7664

    Article  CAS  PubMed  Google Scholar 

  8. Myung K, He DM, Lee SE et al (1997) KARP-1: a novel leucine zipper protein expressed from the Ku86 autoantigen locus is implicated in the control of DNA-dependent protein kinase activity. EMBO J 16:3172–3184. doi:10.1093/emboj/16.11.3172

    Article  CAS  PubMed  Google Scholar 

  9. Eunju D, Eiichi T, Yasuyuki I et al (2003) Molecular cloning and characterization of rKAB1, which interacts with KARP-1, localizes in the nucleus and protects cells against oxidative death. Mol Cell Biochem 248:77–83. doi:10.1023/A:1024157515342

    Article  Google Scholar 

  10. Camurri L, Codeluppi S, Pedroni C et al (1983) Chromosomal aberrations and sister-chromatid exchanges in workers exposed to styrene. Mutat Res 119:361–369. doi:10.1016/0165-7992(83)90186-0

    Article  CAS  PubMed  Google Scholar 

  11. Kinoshita A, Wanibuchi H, Wei M et al (2006) Hormesis in carcinogenicity of non-genotoxic carcinogens. J Toxicol Pathol 19:111–122. doi:10.1293/tox.19.111

    Article  CAS  Google Scholar 

  12. Kuwabara H, Yoneda M, Nagai M et al (2004) A new polyclonal antibody that recognizes a human receptor for hyaluronan mediated motility. Cancer Lett 210:73–80. doi:10.1016/j.canlet.2004.01.004

    Article  CAS  PubMed  Google Scholar 

  13. Rein DT, Roehrig K, Schondorf T et al (2003) Expression of the hyaluronan receptor RHAMM in endometrial carcinomas suggests a role in tumour progression and metastasis. J Cancer Res Clin Oncol 129:161–164

    CAS  PubMed  Google Scholar 

  14. Tolg C, Poon R, Fodde R et al (2003) Genetic deletion of receptor for hyaluronan-mediated motility (RHAMM) attenuates the formation of aggressive fibromatosis (desmoid tumor). Oncogene 22:6873–6882. doi:10.1038/sj.onc.1206811

    Article  CAS  PubMed  Google Scholar 

  15. Maxwell CA, Keats JJ, Belch AR et al (2005) Receptor for hyaluronan-mediated motility correlates with centrosome abnormalities in multiple myeloma and maintains mitotic integrity. Cancer Res 65:850–860

    CAS  PubMed  Google Scholar 

  16. Adele K, Elizabeth MP, James MP (2002) Effects of chlorinated aliphatic hydrocarbons on the fidelity of cell division in human CYP2E1 expression cells. Exp Mol Med 34:83–89

    Google Scholar 

  17. Board PG, Anders MW (2007) Glutathione transferase omega 1 catalyzes the reduction of S-(Phenacyl) glutathiones to acetophenones. Chem Res Toxicol 20:149–154. doi:10.1021/tx600305y

    Article  CAS  PubMed  Google Scholar 

  18. Nebert DW, Vasiliou V (2004) Analysis of the glutathione S-transferase (GST) gene family. Hum Genomics 1:460–464

    CAS  PubMed  Google Scholar 

  19. Townsend DM, Tew KD (2003) The role of glutathione-S-transferase in anti-cancer drug resistance. Oncogene 22:7369–7375. doi:10.1038/sj.onc.1206940

    Article  CAS  PubMed  Google Scholar 

  20. Meyer-Hoffert U, Wingertszahn J, Wiedow O (2004) Human leukocyte elastase induces keratinocyte proliferation by epidermal growth factor receptor activation. J Invest Dermatol 123:338–345. doi:10.1111/j.0022-202X.2004.23202.x

    Article  CAS  PubMed  Google Scholar 

Download references

Acknowledgments

This study was supported by National Basic Research Program of China (973 Program, No.: 2002CB512903), National Natural Science Foundation of China (30571557), Guangdong Natural Science Foundation (5009153).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Zhi-Xiong Zhuang.

Additional information

Hai-Yan Huang and Jian-Jun Liu have contributed equally.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Huang, HY., Liu, JJ., Xi, RR. et al. An investigation of hormesis of trichloroethylene in L-02 liver cells by differential proteomic analysis. Mol Biol Rep 36, 2119–2129 (2009). https://doi.org/10.1007/s11033-008-9424-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s11033-008-9424-z

Keywords

Navigation