Synthesis of heat-shock proteins in six cotton cultivars at different heat treatments

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.

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Are the Effects of Heat on Physiology Due to Heat Shock Proteins?

HortScience ◽

10.21273/hortsci.31.4.691c ◽

1996 ◽

Vol 31 (4) ◽

pp. 691c-691

Author(s):

Robert E. Paull ◽

Chris B. Watkins

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Stress Responses ◽

Critical Role ◽

Chilling Injury ◽

Heat Treatments ◽

Adaptation To Heat ◽

Heat Shock Responses ◽

Shock Proteins

Production of heat shock proteins (HSP) in response to high temperatures are a highly recognizable feature of plant and animal systems. It is thought that such proteins play a critical role in survival under supraoptimal temperature conditions. The use of heat treatments has been examined extensively, especially for disinfestation of fruit and disease control. Heat treatments can affect physiological responses, such as ethylene production, softening, and other ripening factors, as well as reducing physiological disorders, including chilling injury. HSPs have been implicated in a number of stress responses, but the extent that they are involved, especially in amelioration of chilling injury, is a subject of debate. In a number of cases, heat shock proteins do not appear to be involved, and HSPs do not explain long-term adaptation to heat; other systems for which we do not have models may be at work. Resolution of these issues may require the use of transgenic plants with modified heat shock responses.

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Heat shock proteins: in vivo heat treatments reveal adipose tissue depot-specific effects

Journal of Applied Physiology ◽

10.1152/japplphysiol.00286.2014 ◽

2015 ◽

Vol 118 (1) ◽

pp. 98-106 ◽

Cited By ~ 12

Author(s):

Robert S. Rogers ◽

Marie-Soleil Beaudoin ◽

Joshua L. Wheatley ◽

David C. Wright ◽

Paige C. Geiger

Keyword(s):

Adipose Tissue ◽

Fatty Acid ◽

Heat Shock ◽

Heat Shock Proteins ◽

Ex Vivo ◽

Heat Treatments ◽

Whole Body ◽

Sham Treatment ◽

Shock Proteins

Heat treatments (HT) and the induction of heat shock proteins (HSPs) improve whole body and skeletal muscle insulin sensitivity while decreasing white adipose tissue (WAT) mass. However, HSPs in WAT have been understudied. The purpose of the present study was to examine patterns of HSP expression in WAT depots, and to examine the effects of a single in vivo HT on WAT metabolism. Male Wistar rats received HT (41°C, 20 min) or sham treatment (37°C), and 24 h later subcutaneous, epididymal, and retroperitoneal WAT depots (SCAT, eWAT, and rpWAT, respectively) were removed for ex vivo experiments and Western blotting. SCAT, eWAT, and rpWAT from a subset of rats were also cultured separately and received a single in vitro HT or sham treatment. HSP72 and HSP25 expression was greatest in more metabolically active WAT depots (i.e., eWAT and rpWAT) compared with the SCAT. Following HT, HSP72 increased in all depots with the greatest induction occurring in the SCAT. In addition, HSP25 increased in the rpWAT and eWAT, while HSP60 increased in the rpWAT only in vivo. Free fatty acid (FFA) release from WAT explants was increased following HT in the rpWAT only, and fatty acid reesterification was decreased in the rpWAT but increased in the SCAT following HT. HT increased insulin responsiveness in eWAT, but not in SCAT or rpWAT. Differences in HSP expression and induction patterns following HT further support the growing body of literature differentiating distinct WAT depots in health and disease.

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