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.

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.

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.

Heat shock proteins functioning as molecular chaperones: their roles in normal and stressed cells

1993 ◽  
Vol 339 (1289) ◽  
pp. 327-333 ◽  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Stress Proteins ◽  
Elevated Temperatures ◽  
Metabolic Stress ◽  
Hsp 70 ◽  
Degree Of Protection ◽  
Stressed Cells ◽  
Shock Proteins

In response to either elevated temperatures or several other metabolic insults, cells from all organisms respond by increasing the expression of so-called heat shock proteins (hsp or stress proteins). In general, the stress response appears to represent a universal cellular defence mechanism. The increased expression and accumulation of the stress proteins provides the cell with an added degree of protection. Studies over the past few years have revealed a role for some of the stress proteins as being intimately involved in protein maturation. Members of the hsp 70 family, distributed throughout various intracellular compartments, interact transiently with other proteins undergoing synthesis, translocation, or higher ordered assembly. Although not yet proven, it has been suggested that members of the hsp 70 family function to slow down or retard the premature folding of proteins in the course of synthesis and translocation. Yet another family of stress proteins, the hsp 60 or GroEL proteins (chaperonins), appear to function as catalysts of protein folding. Here I discuss the role of those stress proteins functioning as molecular chaperones, both within the normal cell and in the cell subjected to metabolic stress.

scholarly journals 992 STRESS TOLERANCE INDUCTION: THE ROLE OF ABA AND HEAT STABLE PROTEINS

HortScience ◽  
1994 ◽  
Vol 29 (5) ◽  
pp. 571c-571
Author(s):  
L. V. Gusta
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Tolerance ◽  
Freezing Tolerance ◽  
Stress Responses ◽  
Stress Proteins ◽  
Practical Significance ◽  
Induced Response ◽  
Heat Stable ◽  
Shock Proteins

Plants acclimate to abiotic stresses, e.g. heat, freezing drought and salinity, in response to environmental cues such as temperature, daylength and water. Plants can respond within minutes to the cue e.g. heat tolerance or within hours or days, e.g. drought and freezing tolerance. Heat shock proteins are measurable within 20 to 30 minutes of a heat stress and the plants aclimate almost immediately. In contrast, proteins related to freezing tolerance are measurable within hours but days are required before a measurable increase in freezing tolerance can be detected. In almost all stresses it appears that the environmental cue effects the water status of the plant which in turn affects the level of endogenous abscisic acid (ABA). ABA has been implicated to ameliorate the stress by inducing genes to produce stress proteins. There is a certain degree of commodity between stresses in ragards to stress proteins, however each stress has their own unique set of stress proteins. For example heat shock proteins did not confer stress tolerance. Proteins involved in water and osmotic stress tolerance share a high degree of commonality. I” all stresses a unique class of proteins are synthesized which are classified as heat or boiling stable (do not coagulate at 100°). These proteins are suggested to be involved in the stress response. Many of these heat stable proteins are induced by ABA alone or in combination with jasmonic acid (JA). Analogs of ABA which are either slowly converted to ABA or are degraded slowly or taken up at a faster rate than ABA have been tested for the efficacy in inducing the stress responses. Analogs have also been identified which inhibit the ABA induced response. How these analogs may have practical significance will be discussed.

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.

scholarly journals Cell-specific expression of heat shock proteins in chicken reticulocytes and lymphocytes.

1984 ◽  
Vol 99 (4) ◽  
pp. 1316-1323 ◽  
Author(s):  
R Morimoto ◽  
E Fodor
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Gel Electrophoresis ◽  
Elevated Temperatures ◽  
Major Protein ◽  
Beta Globin ◽  
Specific Expression ◽  
Two Dimensional Gel Electrophoresis ◽  
Globin Synthesis ◽  
Shock Proteins

We have found that chicken reticulocytes respond to elevated temperatures by the induction of only one heat shock protein, HSP70, whereas lymphocytes induce the synthesis of all four heat shock proteins (89,000 mol wt, HSP89; 70,000 mol wt, HSP70; 23,000 mol wt, HSP23; and 22,000 mol wt, HSP22). The synthesis of HSP70 in lymphocytes was rapidly induced by small increases in temperature (2 degrees-3 degrees C) and blocked by preincubation with actinomycin D. Proteins normally translated at control temperatures in reticulocytes or lymphocytes were not efficiently translated after incubation at elevated temperatures. The preferential translation of mRNAs that encode the heat shock proteins paralleled a block in the translation of other cellular proteins. This effect was most prominently observed in reticulocytes where heat shock almost completely repressed alpha- and beta-globin synthesis. HSP70 is one of the major nonglobin proteins in chicken reticulocytes, present in the non-heat-shocked cell at approximately 3 X 10(6) molecules per cell. We compared HSP70 from normal and heat-shocked reticulocytes by two-dimensional gel electrophoresis and by digestion with Staphylococcus aureus V8 protease and found no detectable differences to suggest that the P70 in the normal cell is different from the heat shock-induced protein, HSP70. P70 separated by isoelectric focusing gel electrophoresis into two major protein spots, an acidic P70A (apparent pl = 5.95) and a basic P70B (apparent pl = 6.2). We observed a tissue-specific expression of P70A and P70B in lymphocytes and reticulocytes. In lymphocytes, P70A is the major 70,000-mol-wt protein synthesized at normal temperatures whereas only P70B is synthesized at normal temperatures in reticulocytes. Following incubation at elevated temperatures, the synthesis of both HSP70A and HSP70B was rapidly induced in lymphocytes, but synthesis of only HSP70B was induced in reticulocytes.

The expression of temperature-stress proteins in a desert cactus (Opuntia ficus indica)

Genome ◽  
1991 ◽  
Vol 34 (6) ◽  
pp. 940-943 ◽  
Author(s):  
Daryl J. Somers ◽  
Randal W. Giroux ◽  
W. Gary Filion
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Stress Proteins ◽  
Protein S ◽  
Protein Families ◽  
Opuntia Ficus Indica ◽  
Stress Acclimation ◽  
Molecular Masses ◽  
Shock Proteins

Opuntia ficus indica roots grown hydroponically at 20 or 30 °C were subjected to a range of heat-shock temperatures as high as 50 °C for 2 h. Roots grown at 30 °C sustained a greater level of total protein synthesis than did 20 °C-grown roots following heat-shock treatments ≥ 45 °C. The 30 °C-grown roots synthesized 31 families of heat-shock proteins between 38 and 47 °C in comparison with 20 °C-grown roots, which synthesized 19 families of heat-shock proteins at 45 °C. In both groups of roots, the heat-shock response was dominated equally by the 71–75 and a 62 kDa heat-shock protein families. In addition, the 20 °C-grown roots expressed 11 families of cold-shock proteins following 2 h at 4 °C, five of which had similar relative molecular masses to heat-shock protein families. There were numerous qualitative differences in the heat shock protein profiles between the roots grown at 20 and 30 °C; the 30 °C-grown roots expressed several unique heat shock protein families.Key words: heat-shock protein(s), cactus, thermal stress, acclimation.

Acidic extracellular environment induces only a subset of heat-shock proteins in primary mouse kidney cell cultures

1990 ◽  
Vol 68 (4) ◽  
pp. 804-807 ◽  
Author(s):  
Edward W. Khandjian
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Cultures ◽  
Kidney Cell ◽  
Acidic Medium ◽  
Stress Proteins ◽  
Cdna Probe ◽  
Mouse Kidney ◽  
Primary Mouse ◽  
Shock Proteins

Exposure of primary mouse kidney cell cultures to acidic medium (pH 5.5) induced the expression of a 70 kilodalton (kDa) protein. This protein was identified as the major inducible heat-shock protein 70 (hsp70) by immunoprecipitation with anti-hsp70 serum and Northern blot analysis with a hsp70 cDNA probe. Maximum induction of the 70-kDa protein at pH 5.5 after 240 min was about 30% of that observed after 60 min of thermal treatment at 43 °C. In addition, there was an apparent induction of the glucose-regulated proteins (GRPs) of 76–78 and 98–100 kDa, but not of the other hsps. This subset induction of the heat-shock response by acidic medium suggests that different mechanisms are responsible for the induction of the various families of hsps.Key words: heat-shock proteins, stress proteins, acidic induction, viral infection, mouse kidney cells.

scholarly journals Extracellular cell stress (heat shock) proteins—immune responses and disease: an overview

2017 ◽  
Vol 373 (1738) ◽  
pp. 20160522 ◽  
Author(s):  
A. Graham Pockley ◽  
Brian Henderson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Proteins ◽  
Biological Fluids ◽  
Stress Protein ◽  
Cell Stress ◽  
Immune Reactivity ◽  
Protein Levels ◽  
Shock Proteins ◽  
Adaptive Immune Systems

Extracellular cell stress proteins are highly conserved phylogenetically and have been shown to act as powerful signalling agonists and receptors for selected ligands in several different settings. They also act as immunostimulatory ‘danger signals’ for the innate and adaptive immune systems. Other studies have shown that cell stress proteins and the induction of immune reactivity to self-cell stress proteins can attenuate disease processes. Some proteins (e.g. Hsp60, Hsp70, gp96) exhibit both inflammatory and anti-inflammatory properties, depending on the context in which they encounter responding immune cells. The burgeoning literature reporting the presence of stress proteins in a range of biological fluids in healthy individuals/non-diseased settings, the association of extracellular stress protein levels with a plethora of clinical and pathological conditions and the selective expression of a membrane form of Hsp70 on cancer cells now supports the concept that extracellular cell stress proteins are involved in maintaining/regulating organismal homeostasis and in disease processes and phenotype. Cell stress proteins, therefore, form a biologically complex extracellular cell stress protein network having diverse biological, homeostatic and immunomodulatory properties, the understanding of which offers exciting opportunities for delivering novel approaches to predict, identify, diagnose, manage and treat disease. 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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