Short-term heat shock proteins 70 and 90 mRNA expression profile and its relation to thermo-physiological parameters in goats exposed to heat stress

2019 ◽  
Vol 63 (4) ◽  
pp. 459-465
Author(s):  
M. F. El-Zarei ◽  
A. M. Alseaf ◽  
A. A. Alhaidary ◽  
E. F. Mousa ◽  
A. B. Okab ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mrna Expression ◽  
Expression Profile ◽  
Physiological Parameters ◽  
Mrna Expression Profile ◽  
Short Term ◽  
Shock Proteins

scholarly journals Effects of Short-term Acute Heat Stress on Physiological Responses and Heat Shock Proteins of Hanwoo Steer (Korean Cattle)

2019 ◽  
Vol 34 (3) ◽  
pp. 173-182
Author(s):  
Youl-Chang Baek ◽  
Minseok Kim ◽  
Jin-Young Jeong ◽  
Young-Kyoon Oh ◽  
Sung-Dae Lee ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Physiological Responses ◽  
Short Term ◽  
Korean Cattle ◽  
Acute Heat Stress ◽  
Shock Proteins

scholarly journals Effects from the induction of heat shock proteins in a murine model due to progression of aortic atherosclerosis

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Naoya Hashikawa ◽  
Masanobu Ido ◽  
Yuna Morita ◽  
Narumi Hashikawa-Hobara
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mrna Expression ◽  
Adhesion Molecule ◽  
Intercellular Adhesion Molecule ◽  
Aortic Atherosclerosis ◽  
Short Term ◽  
Shock Proteins ◽  
The Relationship ◽  
Progression Of Atherosclerosis

AbstractHeat shock proteins (HSPs) are molecular chaperones that repair denatured proteins. The relationship between HSPs and various diseases has been extensively studied. However, the relationship between HSPs and atherosclerosis remains unclear. In this study, we induced the expression of HSPs and analyzed the effects on the development/progression of atherosclerosis in vivo. Remarkably, when HSPs were induced in apolipoprotein E deficient (ApoE−/−) mice prior to the formation of atheromas, the progression of atherosclerosis was inhibited; the short-term induction of HSPs significantly decreased the mRNA expression of intercellular adhesion molecule 1 (ICAM-1) and vascular cell adhesion molecule 1 (VCAM-1) in the aorta. In contrast, the induction of HSPs after the formation of atheromas promoted the progression of atherosclerosis. In fact, the short-term induction of HSPs, after the formation of atheromas, significantly increased the mRNA expression of tumor necrosis factor-alpha, and interleukin 6 in the aorta. Of note, the induction of HSPs also promoted the formation of macrophage-derived foam cells. Overall, these results indicate that HSPs exerts different effects in the context of aortic atherosclerosis, depending on its degree of progression. Therefore, the induction and inhibition of HSPs should be considered for the prevention and treatment of atherosclerosis, respectively.

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.

scholarly journals Taurine Reduces Heat Stress by Regulating the Expression of Heat Shock Proteins in Broilers Exposed to Chronic Heat

2018 ◽  
Vol 20 (3) ◽  
pp. 479-486 ◽  
Author(s):  
SA Belal ◽  
DR Kang ◽  
ESR Cho ◽  
GH Park ◽  
KS Shim
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins

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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