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    The evaluation of potential immunotoxicity induced by environmental pollutant ammonia in broilers
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    Abstract:
    Ammonia (NH3) is a harmful gas with irritating odor, and higher NH3 concentration was found in intensive poultry houses. Although the toxicity of NH3 is well known, little attention has been given to the mechanism of NH3 poisoning in chicken immune organs. To investigate NH3-caused inflammatory damage of broiler spleens, in this study, a broiler model for NH3 poisoning was established, and 3 levels (including microRNA [miRNA], mRNA, and protein) were performed using qRT-PCR and western blot. The results indicated that NH3 exposure caused inflammatory damage using microstructure observation; decreased 2 inflammation-related miRNAs (miR-133a and miR-6615), 2 cytokines secreted by T helper cells 1 (Th1), and heme oxygenase-1 (HO-1); and increased 2 target genes (LOC101747543 and mothers against decapentaplegic homolog 7 [SMAD7]) of the 2 miRNAs, 7 inflammation-related factors, 3 cytokines secreted by Th2, and 5 heat shock proteins (HSPs) in broiler spleens. Our study suggested that Th1/Th2 imbalance, nuclear factor-κB (NF-κB) pathway, and compensatory response of HSPs were involved in NH3-caused inflammatory damage in broiler spleens; there was immunotoxic effect in excess NH3 on broilers. For the first time, we discovered miR-6615 and LOC101747543 may be involved in the mechanism of broiler spleen inflammatory damage caused by NH3 via the NF-κB pathway, and further mechanism needs to be investigated. This study provides new insights for NH3 toxicity identification and risk assessment in animal husbandry production practice.
    Keywords:
    Proinflammatory cytokine
    Heat shock proteins (HSPs) are remarkably conserved in all living organisms. The upregulation of expression of HSPs is triggered by a variety of physiological and environmental insults. HSPs play an important role in protecting against protein denaturation and subsequent celluar stress, which damages the intestinal mucosa and reduces the protective function of the mucosal barrier, resulting in the formation of stress ulcers. Heat shock protein 70 (HSP70) is the most widely studied of all HSPs and has numerous important chaperoning functions. Stress accelerates the synthesis of HSP70, which in turn inhibits the apoptosis of intestinal mucosal cells. In this article, we review the main classification of HSPs, the expression and regulation of HSPs and their roles in stress ulcers. We also discuss the role of functional amino acids in regulating the expression of HSPs (particularly HSP70) and protecting the intestinal mucosa and other tissues.
    Intestinal mucosa
    Citations (28)
    The treatment of either elemene (50 #mu#g/ml, 1h) or heat shock (42deg C, 1h) could increase the membrane expression of HSP70, ActD had a synergistic action with both treatments. HSP70EP (Enhancer protein) gene was up-regulated and HSPA2 gene was down-regulated in both treatments. HSF1 gene was up-regulated in heat shock treatment but down-regulated in elemene treatment. The genes closely correlated with tumor immune, such as HSP70, HSP72, HSP75, HSP90 and gp96 were not changed. Comparing with heat shock treatment, elemene can cause a higher percentn of HSP70 membrane expression in HepG2 cells and that may be caused by its altering the distribution of the already existing HSP70 and/or accelerating the HSP70 mRNA translation. Both treatments can change the expression of genes associated with the transcription control factors of HSPs and decrease HSPA2 gene expression.
    Elemene
    HSF1
    Heat shock factor
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    Objective:To study the influnence of elemene or heat shock treatment upon the expression of membrane HSP70 and HSPs genes in HepG 2 cells.Methods:HSP70 expression was observed by immunofluorescence and FCM techniques.HSP70 gene transcription was blocked by ActD.Genechip was used to study the expression of HSPs genes and the genes associated with the control of HSPs transcription.Results:The treatment of either elemene(50 μg/ml,1 h) or heat shock(42℃,1 h)could increase the membrane expression of HSP70,ActD had a synergistic action with both treatments.HSP70EP(Enhancer Protein) gene was up regulated and HSPA2 gene was down regulated in both treatments.HSF1 gene was up regulated in heat shock treatment but down regulated in elemene treatment.The genes closely correlated with tumor immune,such as HSP70,HSP72,HSP75,HSP90 and gp96 were not changed.Conclusion:Comparing with heat shock treatment,elemene can cause a higher percent of HSP70 membrane expression in HepG 2 cells and that may be caused by its altering the distribution of the already existing HSP70 and/or accelerating the HSP70 mRNA translation.Both treatments can change the expression of genes associated with the transcription control factors of HSPs and decrease HSPA2 gene expression.
    Elemene
    Heat shock factor
    Transcription
    Citations (1)
    Abstract Heat shock proteins (Hsps) are a ubiquitous feature of cells in which these proteins cope with stress‐induced denaturation of other proteins. Among the different families of Hsps, the 70 kDa family ( hsp70 ) is the most highly conserved and has been most extensively studied. Apart from their primary role in cellular defense under stress condition, a number of studies in recent years have shown the immense potential of hsp70 in pollution monitoring using even transgenic approach both in vivo and in vitro. This article reviews the recent developments in the widespread application of hsp70 in environmental risk assessment. © 2003 Wiley Periodicals, Inc. J Biochem Mol Toxicol 17:249–254, 2003; Published online in Wiley InterScience (www.interscience.wiley.com). DOI 10.1002/jbt.10086
    Denaturation (fissile materials)
    Environmental stress
    Citations (151)
    As an important kind of nonspecific cytoprotective proteins,heat shock proteins(HSPs) play a vital role in the stress tolerance and stress protection of immune cells,acting as molecular chaperones or anti-apoptosis effects in the maintenance of the immune cells survival and the stability of the internal environment.HSP70 and HSP27 of small heat shock proteins(sHPSs),an important member of HSPs,have been proved to have significant effect on mediating the cell proliferation,differentiation and apoptosis process.In this paper,the protective effect of HSP70/HSP27 on immune cells under the condition of heat stress was reviewed.
    Hsp27
    Citations (1)