Differential expression and localisation of heat shock protein 70 (HSP70) and glutathione peroxidase 5 (GPX5) in the testis and epididymis of Sonid Bactrian camels
Gaowa HasiLiyasu WuTserennadmid SodnompilRuhan YiRihan WuRui ZhangHaya NaHejie LiuMusi JiWangwei XieNarenhua Nasenochir
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Heat shock protein 70 (HSP70) and glutathione peroxidase 5 (GPX5) are biomarkers of oxidative stress and stress in temperate, tropical environments, which are crucial for male reproduction. Their expression and distribution patterns in the testis and epididymis of Bactrian camels are still unknown.This study aims to investigate the HSP70 and GPX5 expression and localisation in 3- and 6-year-old Bactrian camel testis and epididymis.Reverse transcription quantitative polymerase chain reaction (qRT-PCR), Western blot and immunohistochemistry were used to detect HSP70 in the testis and epididymis (caput, corpus and cauda) and GPX5 in the epididymis at two developmental stages (3-year-old puberty group and 6-year-old adult group).HSP70 was upregulated in the testis. Immunohistochemistry results indicated the HSP70 protein was mainly detected in spermatids and Leydig cells of testicular tissue. In the epididymis, HSP70 was located at the luminal spermatozoa, the epithelium lining the epididymal and the epididymal interstitium. GPX5 expression was significantly higher in the caput epididymis than in the corpus and cauda epididymis. GPX5 protein was observed in the epithelium lining the epididymal, interstitium and luminal spermatozoa in the epididymis by immunohistochemistry.Bactrian camel HSP70 and GPX5 exhibited spatiotemporal expression specificity.HSP70 and GPX5 may be essential for germ cell development and reproductive success after sexual maturation in Sonid Bactrian camels.HSP60
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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.
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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.
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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.
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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
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2184 Ischemia causing a series of cellular changes is known to induce Heat-Shock-Protein70 (HSP70) in different tissues i.e. myocardium, brain, kidney and liver as shown in prior studies. It has been documented that HSP70 induction has protective effects against ischemic damage in these tissues. In a previous study on patients with peripheral arterial occlusive disease we observed an increased expression of HSP70 in involved muscles. This might suggest that ischemia in skeletal muscle induces HSP70 expression. Purpose: To investigate whether ischemia induces HSP70 expression in skeletal muscle. Methods: 21 3–4 months old swines were taken for the experiment. Complete ischemia was obtained by arterial ligation. Muscle biopsies were taken from the M. sternocleidomastoideus before ischemia (Normoperfusion, I0), after 2h of ischemia (I2) and after 4h of ischemia (I4). Total protein was extracted and after protein separation by SDS-PAGE HSP70 protein level was quantitated using Western Blot and densitometric analysis. Quantitative real-time RT-PCR was used to assess HSP70 mRNA level. Results: In comparison to I0 (34,9 ng for 25 ug protein loaded) HSP70 protein level showed a slight increase (N.S.) after 2h ischemia (37,5 ng) and an additional low increase after 4h ischemia (41,1 ng). However relative HSP70 mRNA concentration is clearly elevated in I2 (by 2,5 folds, p = 0,13) and there was a further significant upregulation in I4 compared to I0 (4,3 folds, p<0,05). Conclusion: The present study has demonstrated for the first time that ischemia can cause an upregulation of HSP70 expression in skeletal muscle. The lack of significant increase in HSP70 protein level may be attributed to reduced protein synthesis rate under ischemia. Therefore HSP70 induction might be considered as a stress indicator for the case of ischemia. Whether HSP70 upregulation can provide protection against ischemia in skeletal muscle as it has been shown in myocardium, requires further study.
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2184 Ischemia causing a series of cellular changes is known to induce Heat-Shock-Protein70 (HSP70) in different tissues i.e. myocardium, brain, kidney and liver as shown in prior studies. It has been documented that HSP70 induction has protective effects against ischemic damage in these tissues. In a previous study on patients with peripheral arterial occlusive disease we observed an increased expression of HSP70 in involved muscles. This might suggest that ischemia in skeletal muscle induces HSP70 expression. Purpose: To investigate whether ischemia induces HSP70 expression in skeletal muscle. Methods: 21 3–4 months old swines were taken for the experiment. Complete ischemia was obtained by arterial ligation. Muscle biopsies were taken from the M. sternocleidomastoideus before ischemia (Normoperfusion, I0), after 2h of ischemia (I2) and after 4h of ischemia (I4). Total protein was extracted and after protein separation by SDS-PAGE HSP70 protein level was quantitated using Western Blot and densitometric analysis. Quantitative real-time RT-PCR was used to assess HSP70 mRNA level. Results: In comparison to I0 (34,9 ng for 25 ug protein loaded) HSP70 protein level showed a slight increase (N.S.) after 2h ischemia (37,5 ng) and an additional low increase after 4h ischemia (41,1 ng). However relative HSP70 mRNA concentration is clearly elevated in I2 (by 2,5 folds, p = 0,13) and there was a further significant upregulation in I4 compared to I0 (4,3 folds, p<0,05). Conclusion: The present study has demonstrated for the first time that ischemia can cause an upregulation of HSP70 expression in skeletal muscle. The lack of significant increase in HSP70 protein level may be attributed to reduced protein synthesis rate under ischemia. Therefore HSP70 induction might be considered as a stress indicator for the case of ischemia. Whether HSP70 upregulation can provide protection against ischemia in skeletal muscle as it has been shown in myocardium, requires further study.
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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.
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