Ribosomal genes and heat shock proteins as putative markers for chronic, sublethal heat stress in Arctic charr: applications for aquaculture and wild fish

2011 ◽  
Vol 43 (18) ◽  
pp. 1056-1064 ◽  
Author(s):  
Nicole L. Quinn ◽  
Colin R. McGowan ◽  
Glenn A. Cooper ◽  
Ben F. Koop ◽  
William S. Davidson
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Temperature Stress ◽  
Ribosomal Proteins ◽  
Ribosome Biogenesis ◽  
Cold Water ◽  
Arctic Charr ◽  
Heat Exposure ◽  
Heat Shock Protein Expression ◽  
Shock Proteins

Arctic charr thrive at high densities and can live in freshwater year round, making this species especially suitable for inland, closed containment aquaculture. However, it is a cold-water salmonid, which both limits where the species can be farmed and places wild populations at particular risk to climate change. Previously, we identified genes associated with tolerance and intolerance to acute, lethal temperature stress in Arctic charr. However, there remained a need to examine the genes involved in the stress response to more realistic temperatures that could be experienced during a summer heat wave in grow-out tanks that are not artificially cooled, or under natural conditions. Here, we exposed Arctic charr to sublethal heat stress of 15–18°C for 72 h, and gill tissues extracted before, during (i.e., at 72 h), immediately after cooling and after 72 h of recovery at ambient temperature (6°C) were used for gene expression profiling by microarray and qPCR analyses. The results revealed an expected pattern for heat shock protein expression, which was highest during heat exposure, with significantly reduced expression (approaching control levels) quickly thereafter. We also found that the expression of numerous ribosomal proteins was significantly elevated immediately and 72 h after cooling, suggesting that the gill tissues were undergoing ribosome biogenesis while recovering from damage caused by heat stress. We suggest that these are candidate gene targets for the future development of genetic markers for broodstock development or for monitoring temperature stress and recovery in wild or cultured conditions.

scholarly journals Heat Treatment at an Early Age Has Effects on the Resistance to Chronic Heat Stress on Broilers

Animals ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 1022 ◽  
Author(s):  
Darae Kang ◽  
JinRyong Park ◽  
KwanSeob Shim
Keyword(s):  
Heat Stress ◽  
High Temperature ◽  
Heat Shock ◽  
Stress Hormones ◽  
Heat Exposure ◽  
Control Group ◽  
Heat Shock Factors ◽  
Gene Expressions ◽  
Stressed Group ◽  
Shock Proteins

This study was conducted to investigate the effects of early heat conditioning on growth performance, liver-specific enzymes (GOT and GPT), neuro-hormones (dopamine and serotonin), stress hormones (corticosterone), and the expression of HSPs (heat shock proteins), HSFs (heat shock factors), and pro-inflammatory cytokines under chronic high temperature. Broilers were raised with commercial feed and supplied with water ad libitum under conventional temperature. We separated the broilers into three groups: the control without any heat exposure (C), chronic heat-stressed group (CH), and early and chronic heat-stressed group (HH). At 5 days of age, the HH group was exposed to high temperatures (40 °C for 24 h), while the remaining groups were raised at a standard temperature. Between days 6 and 20, all three groups were kept under optimal temperature. From 21 to 35 days, the two heat-stressed groups (CH and HH) were exposed to 35 °C. Groups exposed to high temperature (CH and HH) showed significantly lower body weight and feed intake compared to the control. GOT and GPT were lower expressed in the CH and HH groups than the control group. In addition, the protein expressions of HSPs were down-regulated by chronic heat stress (CH and HH groups). The gene expressions of HSP60 and HSF3 were significantly down-regulated in the CH and HH groups, while HSP70 and HSP27 genes were up-regulated only in the HH group compared with the control group. The expression of pro-inflammatory cytokine genes was significantly up-regulated in the HH group compared with the control and CH groups. Thus, exposure of early Heat stress (HS) to broilers may affect the inflammatory response; however, early heat exposure did not have a positive effect on chronic HS of liver enzymes and heat shock protein expression.

The effect of heat stress on bull sperm quality and related HSPs expression

2016 ◽  
Vol 66 (3-4) ◽  
pp. 321-333 ◽  
Author(s):  
Yunyun Cheng ◽  
Songcai Liu ◽  
Ying Zhang ◽  
Dan Su ◽  
Gang Wang ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Molecular Mechanisms ◽  
Sperm Quality ◽  
Heat Shock Protein Expression ◽  
Shock Proteins

Heat stress dramatically decreases bull sperm quality and has recently received more attention due to the warmer global climate and more intensive production. However, no data exist regarding sperm quality or the related molecular mechanisms under heat stress. Recent studies showed that inducible heat shock proteins (HSPs) play an important role in the dairy heat stress regulation. In this article, to investigate the impacts of heat stress on sperm quality and the associated molecular mechanisms, sperm quality and enzyme activities concerning acrosome reaction were assessed in Simmental, Limousin and Yanbian bulls under heat stress. Subsequently, changes in heat shock protein expression profiles of Simmental bulls were observed, because we observed that sperm quality of these bulls was most sensitive to heat stress. Finally, the relationship between sperm quality and heat shock protein expression under heat stress was analyzed. The results show that summer heat stress decreased the sperm quality of the three bull breeds significantly. Moreover, different levels of heat stimulation induced various enzyme activity changes, among which the activity change in acrosomal enzyme was the most remarkable. Furthermore, the expression of heat shock proteins in the sperm was influenced by the imposed heat stress, among which the expression levels of HSP60 and HSP70 were increased while HSP90 decreased. In summary, our data show that heat stress seriously affects sperm quality and that HSP90 was most sensitive, although it should be noted that seasonal effects may confound these results. This change in heat shock protein expression may be the major factor that affected the sperm quality of the bulls. The findings may provide a new hypothesis for how heat stress impacts reproduction mechanistically.

scholarly journals Proteomic analysis of heat shock proteins in maize (Zea mays L.)

2019 ◽  
Vol 43 (1) ◽  
Author(s):  
Mahmoud Hussien Abou-Deif ◽  
Mohamed Abdel-Salam Rashed ◽  
Kamal Mohamed Khalil ◽  
Fatma El-Sayed Mahmoud
Keyword(s):  
Heat Treatment ◽  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Proteome Analysis ◽  
High Temperature Stress ◽  
Heat Treatments ◽  
Maize Plants ◽  
Adverse Influence ◽  
Shock Proteins

Abstract Background Maize is one of the important cereal food crops in the world. High temperature stress causes adverse influence on plant growth. When plants are exposed to high temperatures, they produce heat shock proteins (HSPs), which may impart a generalized role in tolerance to heat stress. Proteome analysis was performed in plant to assess the changes in protein types and their expression levels under abiotic stress. The purpose of the study is to explore which proteins are involved in the response of the maize plant to heat shock treatment. Results We investigated the responses of abundant proteins of maize leaves, in an Egyptian inbred line of maize “K1”, upon heat stress through two-dimensional electrophoresis (2-DE) on samples of maize leaf proteome. 2-DE technique was used to recognize heat-responsive protein spots using Coomassie Brilliant Blue (CBB) and silver staining. In 2-D analysis of proteins from plants treated at 45 °C for 2 h, the results manifested 59 protein spots (4.3%) which were reproducibly detected as new spots where did not present in the control. In 2D for treated plants for 4 h, 104 protein spots (7.7%) were expressed only under heat stress. Quantification of spot intensities derived from heat treatment showed that twenty protein spots revealed clear differences between the control and the two heat treatments. Nine spots appeared with more intensity after heat treatments than the control, while four spots appeared only after heat treatments. Five spots were clearly induced after heat treatment either at 2 h or 4 h and were chosen for more analysis by LC-MSMS. They were identified as ATPase beta subunit, HSP26, HSP16.9, and unknown HSP/Chaperonin. Conclusion The results revealed that the expressive level of the four heat shock proteins that were detected in this study plays important roles to avoid heat stress in maize plants.

Localization of metallothionein, heat shock protein (Hsp70), and superoxide dismutase expression in Hemidiaptomus roubaui (Copepoda, Crustacea) exposed to cadmium and heat stress

2007 ◽  
Vol 85 (3) ◽  
pp. 362-371 ◽  
Author(s):  
Martine Liberge ◽  
Roxane-M. Barthélémy
Keyword(s):  
Superoxide Dismutase ◽  
Heat Stress ◽  
Heat Shock ◽  
Metal Binding ◽  
Stress Proteins ◽  
Reproductive Function ◽  
Cadmium Stress ◽  
Specific Distribution ◽  
Freshwater Crustacean ◽  
Shock Proteins

Immunohistochemical methods were applied in the present study to investigate the expression of stress proteins such as metallothioneins (MT), which are metal-binding proteins, and heat shock proteins (Hsp70), as well as an antioxidant enzyme (superoxide dismutase, SOD), in the freshwater crustacean copepod Hemidiaptomus roubaui (Richard, 1888) exposed to cadmium or heat stress. The results show a tissue-specific distribution of MT-like protein after cadmium exposure in the brain and in the nerve cord. Cadmium stress did not provoke inducible Hsp70 or SOD expression. Unlike cadmium, heat stress induced the expression of Hsp70 and SOD in the shell glands, a structure involved in the reproductive function, and more particularly in the formation of the diapause egg envelope. MT expression is not induced in animals exposed to heat stress.

scholarly journals Proteome and Transcriptome Reveal Involvement of Heat Shock Proteins and Indoleacetic Acid Metabolism Process in Lentinula Edodes Thermotolerance

2018 ◽  
Vol 50 (5) ◽  
pp. 1617-1637 ◽  
Author(s):  
Gang-Zheng Wang ◽  
Chao-Jun Ma ◽  
Yi Luo ◽  
Sha-Sha Zhou ◽  
Yan Zhou ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Indoleacetic Acid ◽  
Lentinula Edodes ◽  
Acid Biosynthesis ◽  
Over Expression ◽  
Indoleacetic Acid Biosynthesis ◽  
Shock Proteins ◽  
Exogenous Iaa

Background/Aims: Heat stress could cause huge losses for Lentinula edodes in China and other Asian cultivation areas. Yet our understanding of mechanism how to defend to heat stress is incomplete. Methods: Using heat-tolerant and heat-sensitive strains of L. edodes, we reported a combined proteome and transcriptome analysis of L. edodes response to 40 °C heat stress for 24 h. Meanwhile, the effect of LeDnaJ on the thermotolerance and IAA (indoleacetic acid) biosynthesis in L. edodes was analyzed via the over-expression method. Results: The proteome results revealed that HSPs (heat shock proteins) such as Hsp40 (DnaJ), Hsp70, Hsp90 and key enzymes involved in tryptophan and IAA metabolism process LeTrpE, LeTrpD, LeTam-1, LeYUCCA were more highly expressed in S606 than in YS3357, demonstrating that HSPs and tryptophan as well as IAA metabolism pathway should play an important role in thermotolerance. Over-expression of LeDnaJ gene in S606 strains showed better tolerance to heat stress. It was also documented that intracellular IAA accumulation of S606 (8-fold up) was more than YS3357 (2-fold up), and exogenous IAA enhanced L. edodes tolerance to heat stress. Conclusion: Our data support the interest of LeTrpE, LeDnaJ, tryptophan and IAA could play a pivotal role in enhancing organism thermotolerance.

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