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Ethanol Extract of Ulmus pumila Ameliorates Heat Stress through the Induction of Heat Shock Proteins Expression in RAW264.7 Macrophage Cells

  • dela Cruz, Joseph (Department of Animal Life and Environmental Science, Hankyong National University) ;
  • Byambaragchaa, Munkhzaya (Department of Animal Life and Environmental Science, Hankyong National University) ;
  • Choi, Seok-Geun (Department of Animal Life and Environmental Science, Hankyong National University) ;
  • Hwang, Seong-Gu (Department of Animal Life and Environmental Science, Hankyong National University)
  • 투고 : 2014.10.10
  • 심사 : 2014.11.07
  • 발행 : 2014.12.30

초록

Heat stress is a significant burden to animal production in most areas of the world. Improving our knowledge of physiological and metabolic mechanisms of acclimation may contribute to the development of procedures that may help to maintain health and production efficiency under hot temperature. The effect of Ulmus pumila (UP) extract in inducing Heat Shock Proteins (HSPs) expression in heat-stressed RAW264.7 macrophage cells was investigated. Cell viability assay showed a dose dependent increase in cells after treatment with UP for 24 hours. RT-PCR and western blot analysis showed that increasing concentrations of UP induce the expression of Heat Shock Factor 1 (HSF1) and dose dependently upregulated the expression of Heat shock protein 70 (Hsp70) and Hsp90. LPS-induced nitric oxide was dose-dependently reduced while phagocytic activity greatly recovered with UP treatment. These data demonstrated that UP can be a potential candidate in the development of cytoprotective agent against heat stress.

키워드

참고문헌

  1. Cheng, A.W., Wan, F.C., Wang, J.Q., Jin, Z.Y., Xu, X.M., 2008. Macrophage immunomodulatory activity of polysaccharides isolated from Glycyrrhiza uralensis fish. International Immunopharmacology. 8:43-50. https://doi.org/10.1016/j.intimp.2007.10.006
  2. Collier, R.J., Baumgard, L.H., Lock, A.L., Bauman, D.E., 2005. Physiological Limitations, Nutrient Partitioning. In Yield of Farmed Species. Constraints and Opportunities in the 21st Century. Nottingham University Press, Nottingham UK, pp.351-377.
  3. Johnson, J.D., Fleshner, M., 2006. Releasing signals, secretory pathways, and immune function of endogenous extracellular heat shock protein 72. J. Leukoc. Biol. 79:425-434. https://doi.org/10.1189/jlb.0905523
  4. Kapila, N., Kishore, A., Sodhi, M., Sharma, A., Mohanty, A.K., Kumar, P., Mukesh, A., 2013. Temporal Changes In mRNA Expression Of Heat Shock Protein Genes In Mammary Epithelial Cells Of Riverine Buffalo In Response To Heat Stress In Vitro. I. J. Anim. Bio. 3:5-9.
  5. Kregel, K.C., 2002. Molecular Biology of Thermoregulation Invited Review: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance. J. Appl. Physiol. 92:2177-2186. https://doi.org/10.1152/japplphysiol.01267.2001
  6. Lee, W.C., Wen, H.C., Chang, C.P., Chen, M.Y., Lin, M.T., 2006. Heat Shock Protein 72 Overexpression Protects Against Hyperthermia, Circulatory Shock and Cerebral Ischemia During Heat Stroke. J. Appl. Pysiol. 100:2073-2082. https://doi.org/10.1152/japplphysiol.01433.2005
  7. Mayor, A., Martinon, F., De Smedt, T., Petrilli, V., Tschopp, J., 2007. A crucial function of SGT1 and HSP90 in inflammasome activity links mammalian and plant innate immune responses. Nat. Immunol. 8:497-503. https://doi.org/10.1038/ni1459
  8. Morange, F., 2006. HSFs in Development. Handbook of Experimental Pharmacology. 172:153-169. https://doi.org/10.1007/3-540-29717-0_7
  9. Prohaszka, Z., Fust, G., 2004. Immunological Aspects of Heat-Shock Proteins - The Optimum Stress of Life. Molecular Immunology. 41:29-44. https://doi.org/10.1016/j.molimm.2004.02.001
  10. Ross, O.A., Curran, M.D., Crum, K.A., Rea, I.M., Barnett, Y.A., Middleton D., 2003. Increased Frequency of the 2437 T Allele of the Heat Shock Protein 70-Hom Gene in an Aged Irish Population. Experimental Gerontology. 38:561-565. https://doi.org/10.1016/S0531-5565(03)00006-8
  11. Terao, J., 2009. Dietary flavonoids as antioxidants. Forum Nutr. 61:87-94. https://doi.org/10.1159/000212741
  12. Wang, R., Kovalchin, J.T., Muhlenkamp, P., Chandawarkar, R.Y., 2006. Exogenous heat shock protein 70 binds macrophage lipid raft micro domain and stimulates phagocytosis, processing and MHC-II presentation of antigens. Blood. 107:1636-1642. https://doi.org/10.1182/blood-2005-06-2559
  13. Wang, D., Xia, M., Cui, Z., 2006. New triterpenoids isolated from the root bark of Ulmus pumila L. Chem. Pharm. Bull. 54:775-778. https://doi.org/10.1248/cpb.54.775
  14. Van Morelle, W., Wielockx, B., Mahieu, T., Takada, M., Taniguchi, T., Sekikawa, K., Libert, C., 2002. HSP70 protects against TNF-induced lethal inflammatory shock. Immunity 16:685-695. https://doi.org/10.1016/S1074-7613(02)00310-2
  15. Voellmy, R., 1994. Transduction of the stress signal and mechanisms of transcriptional regulation of heat shock/stress protein gene expression in higher eukaryotes. Crit. Rev. Eukaryot. Gene Expr. 4:357-401.
  16. Zuo, J., Baler, R., Dahl, G., Voellmy, R., 1994. Activation of the DNA-binding ability of human heat shock transcription factor 1 may involve the transition from an intramolecular triple-stranded coiled-coil structure. Mol. Cell Biol. 14:7447-68.
  17. Zou, J., Guo, Y., Guettouche, T., Smith, D.F., Voellmy, R., 1998. Repression of heat shock transcription factor HSF1 activation by HSP90 (HSP90 complex) that forms a stress-sensitive complex with HSF1. Cell. 94:471-480. https://doi.org/10.1016/S0092-8674(00)81588-3