The physiological effects of heat stress and the role of heat shock proteins in rainbow trout (Oncorhynchus mykiss) red blood cells

2003 ◽  
Vol 29 (1) ◽  
pp. 1-12 ◽  
Author(s):  
S.G. Lund ◽  
B.L. Tufts
Keyword(s):  
Heat Stress ◽  
Rainbow Trout ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Oncorhynchus Mykiss ◽  
Blood Cells ◽  
Physiological Effects ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Shock Proteins

scholarly journals Effects of heat stress on Hsp90a2b and Hsp10 mRNA expression and blood cell apoptosis in rainbow trout Oncorhynchus mykiss (Walbaum, 1972)

2019 ◽  
Vol 66 (4) ◽  
Author(s):  
Zhicheng Luo ◽  
Yanjing Zhou ◽  
Zhe Liu ◽  
Binpeng Xia ◽  
Yongjie Wang
Keyword(s):  
Heat Stress ◽  
Rainbow Trout ◽  
Heat Shock ◽  
Blood Cell ◽  
Oncorhynchus Mykiss ◽  
Blood Cells ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Shock Response ◽  
Heat Shock Protein Genes ◽  
Increasing Temperature

To study the response to heat stress in rainbow trout Oncorhynchus mykiss (Walbaum, 1972), the expression of heat shock protein genes Hsp90a2b and Hsp10 in selected tissues and apoptosis of blood cells were investigated at water temperatures of 18, 21, 23, 24, 25 and 26°C. Expressions of Hsp90a2b in the gill, mid-kidney, brain, heart and muscle were generally upregulated with increasing temperature. Hsp90a2b expression in the liver increased rapidly at 21°C and then showed a significant decrease and finally a significant increase at 25°C and 26°C (p<0.05). Hsp10 expression showed an irregular but overall increasing tendency in gill, spleen and mid-kidney and a wave-like increasing pattern in liver, heart and muscle. Levels of Hsp90a2b at 25°C and Hsp10 at 26°C in all tissues were always significantly higher compared to 18°C (p<0.05). The apoptosis rate at 21°C was significantly higher than that at 18°C, followed by a fall and was the highest at 25°C. All these data indicated that the heat shock response already occurred at 21°C which induced expressions of Hsp90a2b and Hsp10 as well as blood cells apoptosis and 25°C may be a key temperature for stress response in rainbow trout.

Synthesis of stress protein 70 (Hsp70) in rainbow trout (Oncorhynchus mykiss) red blood cells

1997 ◽  
Vol 200 (3) ◽  
pp. 607-614 ◽  
Author(s):  
S Currie ◽  
B Tufts
Keyword(s):  
Protein Synthesis ◽  
Rainbow Trout ◽  
Heat Shock ◽  
Oncorhynchus Mykiss ◽  
Red Blood Cells ◽  
Blood Cells ◽  
Stress Proteins ◽  
Stress Protein ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Hsp70 Synthesis

Unlike enucleated mammalian red blood cells (rbcs), the nucleated rbcs of lower vertebrates are capable of protein synthesis and may, therefore, serve as a valuable model to investigate the adaptive significance of stress protein synthesis in cells. This study examined the synthesis of stress protein 70 (Hsp70) in rbcs of the temperature-sensitive rainbow trout Oncorhynchus mykiss in response to heat shock and anoxia. Through western blot analysis, we have demonstrated that rainbow trout rbcs synthesize Hsp70 both constitutively and in response to an increase in temperature. Radioisotopic labelling experiments indicated that the temperature at which Hsp70 synthesis was induced in fish acclimated to 10 &deg;C was between 20 and 25 &deg;C. Actinomycin D blocked de novo Hsp70 synthesis, implying that synthesis of Hsp70 is regulated at the level of transcription in rainbow trout rbcs. Since trout rbcs rely heavily on aerobic metabolism, but may also experience very low oxygen levels within the circulation, we also examined the relative importance of (1) anoxia as a stimulus for Hsp70 synthesis and (2) oxygen as a requirement for protein synthesis under control and heat-shock conditions. We found that trout rbcs were capable of protein synthesis during 2 h of anoxia, but did not increase Hsp70 synthesis. Moreover, rbcs subjected to combined anoxia and heat shock exhibited increases in Hsp70 synthesis that were similar in magnitude to those in cells exposed to heat shock alone. The latter results suggest that rainbow trout rbcs are (1) able to synthesize non-stress proteins during anoxia, (2) capable of tolerating periods of reduced oxygen availability without increased synthesis of stress proteins and (3) able to maintain the integrity of their heat-shock response even during periods of anoxia.

scholarly journals Heat shock protein (HSP) release mechanism under heat stress pressure in Goats: a review

2022 ◽  
Vol 335 ◽  
pp. 00046
Author(s):  
Rafika Febriani Putri ◽  
Tri Eko Susilorini ◽  
Nashi Widodo ◽  
Kuswati Kuswati ◽  
Suyadi Suyadi
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Scientific Evidence ◽  
Animal Health ◽  
Stressful Events ◽  
Release Mechanism ◽  
Stress Markers ◽  
Shock Proteins

Among the various climate variables, heat stress has been reported to be the most detrimental factor to the economy of the livestock industry. Heat stress is one of the most stressful events in the life of livestock with harmful consequences for animal health, productivity and product quality. Heat shock proteins (HSPs), also known as molecular chaperons, are prominent stress markers. Heat shock proteins consist of highly conserved protein expressed at the time of stress, and play an important role in adaptation to the environmental stress. This review discusses the scientific evidence regarding the effects of heat stress and role of HSP during heat stress on Goats.

Heat stress modulated gastrointestinal barrier dysfunction: role of tight junctions and heat shock proteins

2017 ◽  
Vol 52 (12) ◽  
pp. 1315-1319 ◽  
Author(s):  
Avinash Gupta ◽  
Nishant Ranjan Chauhan ◽  
Daipayan Chowdhury ◽  
Ajeet Singh ◽  
Ramesh Chand Meena ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tight Junctions ◽  
Barrier Dysfunction ◽  
Gastrointestinal Barrier ◽  
Shock Proteins

scholarly journals Role of Heat Shock Proteins in Improving Heat Stress Tolerance in Crop Plants

2016 ◽  
pp. 283-307 ◽  
Author(s):  
Palakolanu Sudhakar Reddy ◽  
Thammineni Chakradhar ◽  
Ramesha A. Reddy ◽  
Rahul B. Nitnavare ◽  
Srikrishna Mahanty ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Tolerance ◽  
Crop Plants ◽  
Heat Stress Tolerance ◽  
Shock Proteins

Physiological Functions of Heat Shock Proteins

2020 ◽  
Vol 21 (8) ◽  
pp. 751-760 ◽  
Author(s):  
Qiang Shan ◽  
Fengtao Ma ◽  
Jingya Wei ◽  
Hongyang Li ◽  
Hui Ma ◽  
...  
Keyword(s):  
Heart Disease ◽  
Heat Stress ◽  
Heat Shock ◽  
Cancer Therapy ◽  
Heat Shock Proteins ◽  
Immune Responses ◽  
Molecular Chaperones ◽  
General Medicine ◽  
Shock Proteins

Heat shock proteins (HSPs) are molecular chaperones involved in a variety of life activities. HSPs function in the refolding of misfolded proteins, thereby contributing to the maintenance of cellular homeostasis. Heat shock factor (HSF) is activated in response to environmental stresses and binds to heat shock elements (HSEs), promoting HSP translation and thus the production of high levels of HSPs to prevent damage to the organism. Here, we summarize the role of molecular chaperones as anti-heat stress molecules and their involvement in immune responses and the modulation of apoptosis. In addition, we review the potential application of HSPs to cancer therapy, general medicine, and the treatment of heart disease.

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