Heat Shock Protein Alteration in the Gastrointestinal Tract Tissues of Chickens Exposed to Arsenic Trioxide

详细信息    查看全文

• 作者：Panpan Zhao ; Kexin Zhang ; Guangyang Guo ; Xiao Sun…
• 关键词：Arsenic trioxide ; Gastrointestinal tract tissues ; Heat shock proteins ; Chickens
• 刊名：Biological Trace Element Research
• 出版年：2016
• 出版时间：March 2016
• 年：2016
• 卷：170
• 期：1
• 页码：224-236
• 全文大小：3,332 KB
• 参考文献：1.Smith J D (1973) Arsenic, antimony and bismuth. In: Comprehensive inorganic chemistry, pp 547–684
  2.Gochfeld M (1995) Chemical agents. In: Environmental medicine. St. Louis: Mosby, pp 592–614
  3.Duker AA, Carranza EJM, Hale M (2005) Arsenic geochemistry and health. Environ Int 31:631–641CrossRef PubMed
  4.Dangleben NL, Skiblola CF, Smith MT (2013) Arsenic immunotoxicity: a review. Environ Heal 12:73CrossRef
  5.Cervantes C, Ji G, Ramirez JL, et al. (1994) Resistance to arsenic compounds in microorganisms. FEMS Microbiol Rev 15:355–367CrossRef PubMed
  6.Bell FG (1998) Environmental geology and health. Blackwell Science, London, pp. 487–500
  7.Squibb KS, Fowler BA (1983) Biological and environmental effects of arsenic, Chap 7. In: Fowler BA (ed) The toxicity of arsenic and its compounds. Elsevier Science Publishers, Amsterdam, pp. 233–269
  8.Al-Aqil A, Zulkifli I (2009) Changes in heat shock protein 70 expression and blood characteristics in transported broiler chickens as affected by housing and early age feed restriction. Poult Sci 88(7):1358–1364CrossRef PubMed
  9.Young RA (1990) Stress proteins and immunology. Annu Rev Immunol 8:401–420CrossRef PubMed
  10.Givisiez PEN, Mazzi CM, Ferro MIT, Ferro JA, et al. (2001) Heat or cold chronic stress affects organ weights and Hsp70 levels in chicken embryos. Can J Anim Sci 81:83–87CrossRef
  11.Iwama GK, Thomas PT, Forsyth RJB, Vijayan MM (1998) Heat shock protein expression in fish. Rev Fish Biol Fish 8:35–56CrossRef
  12.Feder ME, Hofmann GE (1999) Heat-shock proteins, molecular chaperones, and the stress response: evolutionary and ecological physiology. Annu Rev Physiol 61:243–282CrossRef PubMed
  13.Ang D, Liberek K, Skowyra D, Zylicz M, et al. (1991) Georgopoulos, biological role and regulation of the universally conserved heat shock proteins. J Biol Chem 266:24233–24236PubMed
  14.Rijk AFV, Bloemendal H (2000) Alpha-B-crystallin in neuropathology. Ophthalmology 214:7–12CrossRef
  15.Li J, Qian X, Sha B (2009) Heat shock protein 40: structural studies and their functional implications. Protein Pept Lett 16(6):606–612PubMedCentral CrossRef PubMed
  16.Razo LMD, Vega BQ, Colombres EB, Aranda ESC, et al. (2001) Stress proteins induced by arsenic. Toxicol Appl Pharmacol 177:132–148CrossRef PubMed
  17.Csermely P, Schnaider T, Soti C, Prohaszka Z, et al. (1998) The 90-kDa molecular chaperone family: structure, function, and clinical applications. Pharmacol Ther 79:129–168CrossRef PubMed
  18.Peirson SN, Butler JN, Foster RG (2003) Experimental validation of novel and conventional approaches to quantitative real-time PCR data analysis. Nucleic Acids Res 31(14):e73PubMedCentral CrossRef PubMed
  19.Livak KJ, Schmittgen TD (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2 (−delta delta C (T)) method. Methods 25:402–408CrossRef PubMed
  20.Xu GL, Hong SY, Song HB, et al. (1985) Keshan disease and selenium deficiency. Nutr Res 1:187
  21.Webb JL (1966) Enzymes and metabolic inhibitors. Academic Press, New York, pp. 595–793
  22.Ritossa F (1996) Discovery of the heat shock response. Cell Stress Chaperones 1:97–98PubMedCentral CrossRef PubMed
  23.Hendrick JP, Hartl FU (1993) Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem 62:349–384CrossRef PubMed
  24.Hugh RB, Pelham (1986) Speculations on the functions of the major heat shock and glucose-regulated proteins. Cell 46:959–961CrossRef
  25.Rothman JE (1989) Polypeptide chain binding proteins: catalysts of proteins folding and related processes in cells. Cell 59:591–601CrossRef PubMed
  26.Howard KJ, Holley SJ, Yamamoto KR, Distelhorst CW (1990) Mapping the HSP90 binding region of the glucocorticoid receptor. J Biol Chem 265:11928–11935PubMed
  27.Zhu YH, Liu XX, Wu LD, et al. (2013) The effect of manganese-induced cytotoxicity on mRNA expressions of HSP27, HSP40, HSP60, HSP70 and HSP90 in chicken spleen lymphocytes in vitro. Biol Trace Elem Res 156:144–152CrossRef PubMed
  28.Qiu XB, Shao YM, Miao S, Wang L (2006) The diversity of the DnaJ/Hsp40 family, the crucial partners for Hsp70 chaperones. Cell Mol Life Sci 63(22):2560–2570CrossRef PubMed
  29.Zhu YF, Zhu JB, Wan XY, Zhu YP, Zhang TB (2010) Gene expression of sHsps, Hsp40 and Hsp60 families in normal and abnormal embryonic development of mouse forelimbs. Toxicol Lett 193(3):242–251CrossRef PubMed
  30.Tsan MF, Gao B (2009) Heat shock proteins and immune system. J Leukoc Biol 85:905–910CrossRef PubMed
  31.Zhu XN, Chen LP, Bai Q, et al (2014) PP2A-AMPL alpha-HSF1 axis regulates the metal-inducible expression of HSPs and ROS clearance. Cell Signal 26(4):825–832CrossRef PubMed
  32.Zhao FQ, Zhang ZW, Qu JP (2014) Cold stress induces antioxidants and Hsps in chicken immune organs. Cell Stress Chaperones 19:635–648PubMedCentral CrossRef PubMed
  33.Xing HJ, Li S, Wang X, Gao XJ (2013) Effects of atrazine and chlorpyrifos on the mRNA levels of HSP70 and HSC70 in the liver, brain, kidney and gill of common carp (Cyprinus carpio L.). Chemosphere 90:910–916CrossRef PubMed
  34.Cintron NS, Toft D (2006) Defining the requirements for Hsp40 and Hsp70 in the Hsp90 chaperone pathway. J Biol Chem 281:26235–26244CrossRef PubMed
  35.Zhao FQ, Zhang ZW, Wang C, Zhang B (2013) The role of heat shock proteins in inflammatory injury induced by cold stress in chicken hearts. Cell Stress Chaperones 18(6):773PubMedCentral CrossRef PubMed
  36.Wheeler DS, Lahni P, Odoms K, Jacobs BR, et al. (2007) Extracellular heat shock protein 60 (Hsp60) levels in children with septic shock. Inflamm Res 56(5):216–219CrossRef PubMed
  37.Liu T, Zhang ZW, Chen DC, Wang LL, et al (2013) Effect of atrazine and chlorpyrifos exposure on heat shock protein response in the brain of common carp (Cyprinus carpio L.). Pestic Biochem Physiol 107:277–283CrossRef
  
• 作者单位：Panpan Zhao (1)
  Kexin Zhang (1)
  Guangyang Guo (1)
  Xiao Sun (1)
  Hongliang Chai (1)
  Wen Zhang (1)
  Mingwei Xing (1)
  
  1. College of Wildlife Resources, Northeast Forestry University, Harbin, Heilongjiang Province, 150040, China
  
• 刊物主题：Biochemistry, general; Biotechnology; Nutrition; Oncology;
• 出版者：Springer US
• ISSN：1559-0720

文摘

Arsenic (As) is widely distributed in our living environment and is useful for industry, agriculture, medical treatment, and other fields. Arsenic trioxide (As₂O₃) is an existing form of As. Exposure to As₂O₃ has a toxic effect on humans and animals. It not only leads to skin cancer, peripheral vascular disease, hyperkeratosis, etc. but also interferes with the functioning of the gastrointestinal tract. The gastrointestinal tract is an important organ for animals to transform the food they eat into the nutrients their body needs for maintenance and growth. Heat shock proteins (Hsps) exist in the non-stress normal cells and their expression increases under stimuli. Therefore, we wonder whether the “stimulus” of As₂O₃ could change the messenger RNA (mRNA) abundance and expression level of Hsps in the gastrointestinal tract of birds. To investigate the relation between arseniasis and Hsp alterations in the chicken’s gastrointestinal tract induced by an As₂O₃-supplemented diet, we selected 72 one-day-old male Hy-line chickens and randomly divided them into four groups. They were fed either a commercial diet or an As₂O₃-supplemented diet containing 7.5, 15, and 30 mg/kg As₂O₃. The experiment lasted for 90 days, and gastrointestinal tract tissue samples (gizzard, glandular stomach, duodenum, jejunum, ileum, cecum, and rectum) were collected at 30, 60, and 90 days. The mRNA contents of Hsps (including Hsp27, Hsp40, Hsp60, Hsp70, and Hsp90) were examined by real-time PCR (RT-PCR). The correlation between As₂O₃ and Hsp genes was assessed. In addition, the protein expression levels of Hsp60 and Hsp70 in the gastrointestinal tract tissue samples were measured by western blot. The results indicated that the mRNA expression levels and the Hsp expression levels in the gastrointestinal tract tissues of chickens with As₂O₃ supplementation increased at different time points in a dose-dependent manner (p < 0.05 or p < 0.01). These data suggested that arseniasis influenced the mRNA abundance of Hsp27, Hsp40, Hsp60, Hsp70, and Hsp90 and the protein expression levels of Hsp60 and Hsp70 in the chicken’s gastrointestinal tract tissues. Keywords Arsenic trioxide Gastrointestinal tract tissues Heat shock proteins Chickens