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

HortScience ◽  
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.

Invited Review: Heat shock proteins: modifying factors in physiological stress responses and acquired thermotolerance

2002 ◽  
Vol 92 (5) ◽  
pp. 2177-2186 ◽  
Author(s):  
Kevin C. Kregel
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Stress Proteins ◽  
Elevated Temperatures ◽  
Physiological Stress ◽  
Critical Role ◽  
Cellular Damage ◽  
Modifying Factors ◽  
Shock Proteins

Cells from virtually all organisms respond to a variety of stresses by the rapid synthesis of a highly conserved set of polypeptides termed heat shock proteins (HSPs). The precise functions of HSPs are unknown, but there is considerable evidence that these stress proteins are essential for survival at both normal and elevated temperatures. HSPs also appear to play a critical role in the development of thermotolerance and protection from cellular damage associated with stresses such as ischemia, cytokines, and energy depletion. These observations suggest that HSPs play an important role in both normal cellular homeostasis and the stress response. This mini-review examines recent evidence and hypotheses suggesting that the HSPs may be important modifying factors in cellular responses to a variety of physiologically relevant conditions such as hyperthermia, exercise, oxidative stress, metabolic challenge, and aging.

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.

Acetylcholinesterase (AChE) and heat shock proteins (Hsp70) of gypsy moth (Lymantria dispar L.) larvae in response to long-term fluoranthene exposure

Chemosphere ◽  
2016 ◽  
Vol 159 ◽  
pp. 565-569 ◽  
Author(s):  
Marija Mrdaković ◽  
Larisa Ilijin ◽  
Milena Vlahović ◽  
Dragana Matić ◽  
Anja Gavrilović ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Gypsy Moth ◽  
Lymantria Dispar ◽  
Shock Proteins

Induced Expression of the Heat Shock Protein Genes uspA and grpE during Starvation at Low Temperatures and Their Influence on Thermal Resistance of Escherichia coli O157:H7

2003 ◽  
Vol 66 (11) ◽  
pp. 2045-2050 ◽  
Author(s):  
YI ZHANG ◽  
MANSEL W. GRIFFITHS
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Thermal Tolerance ◽  
Molecular Mechanisms ◽  
Fluorescent Protein ◽  
Bacterial Cells ◽  
Induced Expression ◽  
Green Fluorescent ◽  
Shock Proteins

Heat shock proteins play an important role in protecting bacterial cells against several stresses, including starvation. In this study, the promoters for two genes encoding heat shock proteins involved in many stress responses, UspA and GrpE, were fused with the green fluorescent protein (gfp) gene. Thus, the expression of the two genes could be quantified by measuring the fluorescence emitted by the cells under different environmental conditions. The heat resistance levels of starved and nonstarved cells during storage at 5, 10, and 37°C were compared with the levels of expression of the uspA and grpE genes. D52-values (times required for decimal reductions in count at 52°C) increased by 11.5, 14.6, and 18.5 min when cells were starved for 3 h at 37°C, for 24 h at 10°C, and for 2 days at 5°C, respectively. In all cases, these increases were significant (P < 0.01), indicating that the stress imposed by starvation altered the ability of E. coli O157:H7 to survive subsequent heat treatments. Thermal tolerance was correlative with the induction of UspA and GrpE. At 5°C, the change in the thermal tolerance of the pathogen was positively linked to the induced expression of the grpE gene but negatively related to the expression of the uspA gene. The results obtained in this study indicate that UspA plays an important role in starvation-induced thermal tolerance at 37°C but that GrpE may be more involved in regulating this response at lower temperatures. An improvement in our understanding of the molecular mechanisms involved in these cross-protection responses may make it possible to devise strategies to limit their effects.

Heat shock proteins and heat adaptation of the whole organism

1997 ◽  
Vol 83 (5) ◽  
pp. 1413-1417 ◽  
Author(s):  
Pope L. Moseley
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Endotoxin Tolerance ◽  
Heat Adaptation ◽  
Adaptation To Heat ◽  
Shock Proteins

Moseley, Pope L. Heat shock proteins and heat adaptation of the whole organism. J. Appl. Physiol. 83(5): 1413–1417, 1997.—Adaptation to heat may occur through acclimatization or thermotolerance; however, the linkage of these phenomena is poorly understood. The importance of heat shock proteins (HSPs) in thermotolerance and differences in their accumulation in organisms adapted to the heat suggest a role for HSPs in acclimatization as well. The role of HSPs in heat adaptation of the whole organism and the interrelationships among heat adaptation, endotoxin tolerance, and cytokine resistance through HSPs are reviewed.

Bio-effect-monitoring of long-term thermal wastes on the oyster, Crassostrea gigas, using heat shock proteins

2017 ◽  
Vol 119 (1) ◽  
pp. 359-364 ◽  
Author(s):  
Jin-Hyoung Kim ◽  
Su-Young Jeong ◽  
Pyung-Joong Kim ◽  
Hans-Uwe Dahms ◽  
Kyung-Nam Han
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Crassostrea Gigas ◽  
Effect Monitoring ◽  
Shock Proteins

Heat shock and stress response of Taenia solium and T. crassiceps (Cestoda)

Parasitology ◽  
2001 ◽  
Vol 122 (5) ◽  
pp. 583-588 ◽  
Author(s):  
L. VARGAS-PARADA ◽  
C. F. SOLÍS ◽  
J. P. LACLETTE
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Stress Proteins ◽  
Taenia Solium ◽  
Western Blots ◽  
Prolonged Incubation ◽  
Larval Stages ◽  
Shock Proteins

Heat shock and stress responses are documented for the first time in larval stages of the cestodes Taenia solium and Taenia crassiceps. Radioactive metabolic labelling after in vitro incubation of cysts at 43 °C, revealed the induction of heat shock proteins. In T. crassiceps, the major heat shock proteins were 80, 70 and 60 kDa. After prolonged incubation, a set of low molecular weight heat shock proteins (27, 31, 33 and 38 kDa), were also induced. In vitro incubation of cysts at 4 °C, induced the synthesis of stress proteins ranging from 31 to 80 kDa, indicating the parasite is also able to respond to cold shock. T. solium cysts exposure to temperature stress also resulted in an increased synthesis of 2 major heat shock proteins of 80 and 70 kDa. Western blots using the excretory–secretory products of T. solium showed that 2 heat shock proteins were recognized by antibodies in the sera of cysticercotic patients: one of 66 kDa and another migrating close to the run front. The T. solium 66 kDa protein was also recognized by specific antibodies directed to a 60 kDa bacterial heat shock protein, suggesting that it belongs to this family of proteins.

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