scholarly journals Expression and localization of heat-shock proteins during skeletal muscle cell proliferation and differentiation and the impact of heat stress

2019 ◽  
Vol 24 (4) ◽  
pp. 749-761 ◽  
Author(s):  
Savant S. Thakur ◽  
Janine L. James ◽  
Nicola J. Cranna ◽  
Victoria L. Chhen ◽  
Kristy Swiderski ◽  
...  
2017 ◽  
Vol 118 (12) ◽  
pp. 4285-4295 ◽  
Author(s):  
Zhixiong Tang ◽  
Huiling Qiu ◽  
Lan Luo ◽  
Nian Liu ◽  
Jiasheng Zhong ◽  
...  

2012 ◽  
Vol 1 (1) ◽  
pp. 125-131 ◽  
Author(s):  
Hisashi Naito ◽  
Toshinori Yoshihara ◽  
Ryo Kakigi ◽  
Noriko Ichinoseki-Sekine ◽  
Takamasa Tsuzuki

Author(s):  
Mahmoud Hussien Abou-Deif ◽  
Mohamed Abdel-Salam Rashed ◽  
Kamal Mohamed Khalil ◽  
Fatma El-Sayed Mahmoud

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.


2007 ◽  
Vol 41 (7) ◽  
pp. 453-455 ◽  
Author(s):  
Y. Ogura ◽  
H. Naito ◽  
T. Tsurukawa ◽  
N. Ichinoseki-Sekine ◽  
N. Saga ◽  
...  

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160529 ◽  
Author(s):  
Ashley E. Archer ◽  
Alex T. Von Schulze ◽  
Paige C. Geiger

Best known as chaperones, heat shock proteins (HSPs) also have roles in cell signalling and regulation of metabolism. Rodent studies demonstrate that heat treatment, transgenic overexpression and pharmacological induction of HSP72 prevent high-fat diet-induced glucose intolerance and skeletal muscle insulin resistance. Overexpression of skeletal muscle HSP72 in mice has been shown to increase endurance running capacity nearly twofold and increase mitochondrial content by 50%. A positive correlation between HSP72 mRNA expression and mitochondrial enzyme activity has been observed in human skeletal muscle, and HSP72 expression is markedly decreased in skeletal muscle of insulin resistant and type 2 diabetic patients. In addition, decreased levels of HSP72 correlate with insulin resistance and non-alcoholic fatty liver disease progression in livers from obese patients. These data suggest the targeted induction of HSPs could be a therapeutic approach for preventing metabolic disease by maintaining the body's natural stress response. Exercise elicits a number of metabolic adaptations and is a powerful tool in the prevention and treatment of insulin resistance. Exercise training is also a stimulus for increased HSP expression. Although the underlying mechanism(s) for exercise-induced HSP expression are currently unknown, the HSP response may be critical for the beneficial metabolic effects of exercise. Exercise-induced extracellular HSP release may also contribute to metabolic homeostasis by actively restoring HSP72 content in insulin resistant tissues containing low endogenous levels of HSPs. This article is part of the theme issue ‘Heat shock proteins as modulators and therapeutic targets of chronic disease: an integrated perspective’.


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