Exercising mammals synthesize stress proteins

1990 ◽  
Vol 258 (4) ◽  
pp. C723-C729 ◽  
Author(s):  
M. Locke ◽  
E. G. Noble ◽  
B. G. Atkinson
Keyword(s):  
Heat Shock ◽  
Mammalian Cells ◽  
Stress Proteins ◽  
Sprague Dawley ◽  
Spleen Cells ◽  
Sprague Dawley Rats ◽  
Electrophoretic Separations ◽  
Shock Proteins ◽  
Sufficient Stimulus

Spleen cells, peripheral lymphocytes, and soleus muscles were removed from male Sprague-Dawley rats that had been run on a treadmill (24 m/min) for either 20, 40, or 60 min or to exhaustion (86 +/- 41 min) and were labeled in vitro with [35S]methionine at 37 degrees C. Similar tissues from nonrunning control rats were labeled in vitro at either 37 or 43 degrees C (heat shock). Fluorographic analyses of one- and two-dimensional polyacrylamide gel electrophoretic separations of the proteins from cells and tissues of exercised rats demonstrate the new or enhanced synthesis of proteins of approximately 65, 72, 90, and 100 kDa. Although synthesis of these proteins is low or not detectable in tissues from control rats labeled at 37 degrees C, they are prominent products of similar tissues labeled under heat-shock conditions (43 degrees C) and, in fact, correspond in Mr and pI with the so-called heat-shock proteins. These results suggest that exercise is a sufficient stimulus to induce or enhance the synthesis of heat shock and/or stress proteins in mammalian cells and tissues.

scholarly journals Disruption of the three cytoskeletal networks in mammalian cells does not affect transcription, translation, or protein translocation changes induced by heat shock.

1985 ◽  
Vol 5 (7) ◽  
pp. 1571-1581 ◽  
Author(s):  
W J Welch ◽  
J R Feramisco
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Mammalian Cells ◽  
Stress Proteins ◽  
Protein Translocation ◽  
Shock Response ◽  
Cytochalasin E ◽  
Cytoskeletal Networks ◽  
Shock Proteins ◽  
Cytoskeletal Elements

Mammalian cells show a complex series of transcriptional and translational switching events in response to heat shock treatment which ultimately lead to the production and accumulation of a small number of proteins, the so-called heat shock (or stress) proteins. We investigated the heat shock response in both qualitative and quantitative ways in cells that were pretreated with drugs that specifically disrupt one or more of the three major cytoskeletal networks. (These drugs alone, cytochalasin E and colcemid, do not result in induction of the heat shock response.) Our results indicated that disruption of the actin microfilaments, the vimentin-containing intermediate filaments, or the microtubules in living cells does not hinder the ability of the cell to undergo an apparently normal heat shock response. Even when all three networks were simultaneously disrupted (resulting in a loose, baglike appearance of the cells), the cells still underwent a complete heat shock response as assayed by the appearance of the heat shock proteins. In addition, the major induced 72-kilodalton heat shock protein was efficiently translocated from the cytoplasm into its proper location in the nucleus and nucleolus irrespective of the condition of the three cytoskeletal elements.

scholarly journals Regulation of heat shock protein synthesis by quercetin in human erythroleukaemia cells

1994 ◽  
Vol 300 (1) ◽  
pp. 201-209 ◽  
Author(s):  
G Elia ◽  
M G Santoro
Keyword(s):  
Heat Shock ◽  
Mammalian Cells ◽  
Elevated Temperatures ◽  
K562 Cells ◽  
Hsp70 Expression ◽  
Transcriptional Level ◽  
Hsp70 Mrna ◽  
Shock Proteins ◽  
Hsp70 Synthesis

Synthesis of heat-shock proteins (HSPs) is universally induced in eukaryotic and prokaryotic cells by exposure to elevated temperatures or to other types of environmental stress. In mammalian cells, HSPs belonging to the 70 kDa family (HSP70) have a regulatory role in several cellular processes, and have been shown to be involved in the control of cell proliferation and differentiation. Although many types of HSP70 inducers have been identified, only a few compounds, all belonging to the flavonoid group, have been shown to inhibit HSP70 induction. Because inhibitors of HSP70 synthesis could be an important tool with which to study the function of this protein, we have investigated the effect of quercetin, a flavonoid with antiproliferative activity which is widely distributed in nature, on HSP70 synthesis in human K562 erythroleukaemia cells after treatment with severe or mild heat shock and with other inducers. Quercetin was found to affect HSP70 synthesis at more than one level, depending on the conditions used. Indeed, after severe heat shock (45 degrees C for 20 min) treatment with quercetin, at non-toxic concentrations, was found to inhibit HSP70 synthesis for a period of 3-4 h. This block appeared to be exerted at the post-transcriptional level and to be cell-mediated, as the addition of quercetin during translation of HSP70 mRNA in vitro had no effect. After prolonged (90 min) exposure at 43 degrees C, however, quercetin was found to inhibit also HSP70 mRNA transcription. Pretreatment of K562 cells with quercetin had no effect on HSP70 expression, and quercetin needed to be present during induction to be effective. Under all conditions tested, the quercetin-induced block of HSP70 synthesis was found to be transient and, after an initial delay, synthesis of HSP70 reached the control rate and continued at the same level for several hours after the time at which HSP70 synthesis had been turned off in control cells. Finally, inhibition of HSP70 synthesis by quercetin appeared to be dependent on the temperature used and on the type of stressor.

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.

Heat and nutritional shock-induced proteins of the fungus Achlya are different and under independent transcriptional control

1984 ◽  
Vol 62 (9) ◽  
pp. 837-846 ◽  
Author(s):  
Herb B. LéJohn ◽  
Cleantis E. Braithwaite
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Transcriptional Control ◽  
Stress Proteins ◽  
Reproductive Development ◽  
Nutritional Stress ◽  
In Vitro Translation ◽  
Stressed Cells ◽  
Shock Proteins

When the temperature of exponentially growing cells of the coenocytic fungus Achlya klebsiana strain 1969 was suddenly elevated from 24 to 37 °C (thermal stress), synthesis of at least 12 preexisting proteins (heat-shock proteins, HSPs) was vigorously induced while synthesis of most other cell proteins declined transiently. After 2–3 h of thermal stress, the cells recovered and resumed normal protein synthesis. If the cells were first starved of nutrients (nutritional stress) before the temperature was raised to 37 °C, the same 12 HSPs were induced, but synthesis of both heat-shock-inducible and nonheat-shock proteins declined to trace levels after 4 h of thermal stress. Molecular weights (MW) of the HSPs were approximately 96 000a, 96 000b, 85 000, 72 000, 70 000, 69 000a, 69 000b, 68 000, 60 000, 52 000, 26 000a, and 26 000b, and they had similar isoelectric points (5.8–6.2). Nutritionally stressed cells showed an induced synthesis of some 28 proteins (nutritional stress proteins, NSPs), when they were not heat shocked, and an induced synthesis of 20 NSPs when heat shocked. In the presence of glutamine, nutritionally stressed cells induced the synthesis of 15 NSPs when they were not heat shocked and 17 NSPs when they were heat shocked. The NSPs and HSPs were electrophoretically different proteins. Glutamine did not affect the induction pattern of the HSPs, but it arrested reproductive development of starving cells while altering the pattern of NSP synthesis. Since actinomycin D inhibited the induced synthesis of HSPs and some NSPs, they may be under transcriptional control. In vitro translation of poly(A)+ RNAs from heat-shocked cells showed that these cells were rich in HSP mRNAs and poor in NSP mRNAs. We speculate that NSPs, but not HSPs, may play a role in reproductive development and sporulation in this fungus.

Stress protein systems of mammalian cells

1986 ◽  
Vol 250 (1) ◽  
pp. C1-C17 ◽  
Author(s):  
J. R. Subjeck ◽  
T. T. Shyy
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Mammalian Cells ◽  
Stress Proteins ◽  
Heat Exposure ◽  
Stress Protein ◽  
Protective Role ◽  
Living Organisms ◽  
Shock Proteins ◽  
Glucose Regulated Proteins

Living organisms are known to react to a heat stress by the selective induction in the synthesis of several polypeptides. In this review we list the major stress proteins of mammalian cells that are induced by heat shock and other environments and categorize these proteins into specific subgroups: the major heat shock proteins, the glucose-regulated proteins, and the low-molecular-weight heat shock proteins. Characteristics of the localization and expression of proteins in each of these subgroups are presented. Specifically, the nuclear/nucleolar locale of certain of the major heat shock proteins is considered with respect to their association with RNA and the recovery of cells after a heat exposure. The induction of these major heat shock proteins and the repression of the glucose-regulated proteins as a result of reoxygenation of anoxic cells or by the addition of glucose to glucose-deprived cultures is described. Changes in the expression of these protein systems during embryogenesis and differentiation in mammalian and nonmammalian systems is summarized, and the protective role that some of these proteins appear to play in protecting the animal against the lethal effects of a severe heat treatment and against teratogenesis is critically examined.

Activation of heat-shock transcription factor in rat heart after heat shock and exercise

1995 ◽  
Vol 268 (6) ◽  
pp. C1387-C1394 ◽  
Author(s):  
M. Locke ◽  
E. G. Noble ◽  
R. M. Tanguay ◽  
M. R. Feild ◽  
S. E. Ianuzzo ◽  
...  
Keyword(s):  
Heat Shock ◽  
Cultured Cells ◽  
Treadmill Running ◽  
Rat Myocardium ◽  
Sprague Dawley ◽  
Mobility Shift ◽  
Heat Shock Element ◽  
Heat Shock Transcription Factors ◽  
Sprague Dawley Rats ◽  
Shock Proteins

Stress-induced transcriptional regulation of the heat-shock proteins (HSP) is mediated by activation and binding of the heat-shock transcription factors (HSF) to the heat-shock element (HSE). Given the similarities between the stressors known to activate the HSF in cultured cells and the physiological stresses known to occur during exercise, HSF activation was examined in the hearts from exercising animals. Sprague-Dawley rats (5 rats/group) were run on a treadmill (24 m/min) for either 0, 20, 40, or 60 min or to exhaustion (102 +/- 7 min). Protein extracts were assessed for HSF activation by mobility-shift gels. Extracts from the hearts of nonrunning rats demonstrated no HSF activation, whereas HSF activation was detected in 80% of the hearts from animals that run for at least 40 min. These results demonstrate that treadmill running is capable of activating the HSF and increasing 70-kDa HSP mRNA in the rat myocardium.

scholarly journals Synthesis of Heat Shock Proteins in Rat Brain Cortex after Transient Ischemia

1986 ◽  
Vol 6 (4) ◽  
pp. 505-510 ◽  
Author(s):  
Gerald A. Dienel ◽  
Marika Kiessling ◽  
Michael Jacewicz ◽  
William A. Pulsinelli
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Stress Proteins ◽  
Two Dimensional ◽  
Vessel Occlusion ◽  
Two Dimensional Gel Electrophoresis ◽  
Messenger Ribonucleic Acid ◽  
Rat Neocortex ◽  
Shock Proteins

Cell-free protein synthesis and two-dimensional gel autoradiography were used to characterize early postischemic protein synthesis in rat neocortex. Severe forebrain ischemia was induced for 30 min (four-vessel occlusion model) and followed by 3 h of recirculation. Polysomes were isolated from the cerebral cortex, translated in vitro in a reticulocyte system, and analyzed by two-dimensional gel electrophoresis. The translation products of postischemic polysomes included a major new protein family (70 kDa) with multiple isoelectric variants that was found to comigrate with the 68- to 70-kDa “heat shock” protein synthesized from polysomes of hyperthermic rats. Two other stress proteins (93 and 110 kDa) also appeared to be synthesized in increased amounts after ischemia. A complement of proteins that was indistinguishable from that of controls was also synthesized after ischemia, indicating that messenger ribonucleic acid coding for most brain proteins is preserved after ischemia and is bound to polysomes.

scholarly journals Heat shock does not attenuate low-frequency fatigue

1999 ◽  
Vol 77 (1) ◽  
pp. 64-70 ◽  
Author(s):  
J A Thomas ◽  
E G Noble
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Low Frequency ◽  
Shock Therapy ◽  
Whole Body ◽  
Sprague Dawley ◽  
Sprague Dawley Rats ◽  
Low Frequency Fatigue ◽  
Shock Proteins ◽  
Muscle Contractile

Whole-body hyperthermia or heat shock confers protection to myocardial contractility against reperfusion-induced injury. The purpose of this study was to determine whether heat shock could provide similar protection to skeletal muscle contractility against low-frequency fatigue. Male Sprague-Dawley rats (6 rats/group) were heat shocked at 41.5°C for 15 min either 24 h or 4 days prior to fatiguing stimulation to compare the contractile responses of the plantaris muscle with those of a nonheated group. Both 24 h and 4 days after heat shock, the 72-kDa heat shock protein (HSP72) was elevated above control levels. There were no differences between the heat-shocked and non-heat-shocked animals in measures of contractility prior to fatiguing contractions or in resistance to fatigue. Heat-shock preconditioning did not lead to improved postfatigue force recovery above control responses and, in fact, delayed the recovery of force. This study does not support the use of heat-shock therapy to improve skeletal muscle contractile performance under fatiguing conditions.Key words: heat shock proteins, rat, skeletal muscle, contractile properties, HSP72.

Acute and Genotoxic Profile of a Dimeric Impurity of Cefotaxime

2004 ◽  
Vol 23 (1) ◽  
pp. 41-45 ◽  
Author(s):  
Shiv Kumar Agarwal ◽  
Upendra Bhatnagar ◽  
Navin Rajesh
Keyword(s):  
Mammalian Cells ◽  
Mutagenic Activity ◽  
Clinical Signs ◽  
Chinese Hamster ◽  
Metabolic Activation ◽  
Sprague Dawley ◽  
Bacterial Strains ◽  
Sprague Dawley Rats ◽  
A Cell

The manufacturing and storage of cefotaxime produces different impurities of various concentrations, which may influence the efficacy and safety of the drugs. Because no report of toxicity data is available on the impurities of cefotaxime, the present acute and genotoxicity studies were designed and conducted to provide the information for establishing the safety profile and qualification of the dimeric impurity. Histidine-requiring mutants of Salmonella typhimurium TA97a, TA98, TA100, TA102, and TA1535 strains, with or without metabolic activation (S-9), were used for point-mutation tests. Neither increase in numbers of revertants, indicative of mutagenic activity, nor inhibition of bacterial growth, indicative of cytotoxicity, was observed when the dimeric impurity of cefotaxime at concentrations of 0.62, 1.85, 5.56, 16.67, and 50 μg/plate was incorporated into plates containing S. typhimurium bacterial strains. Cultures of Chinese hamster ovary (CHO) cells at a cell density of 2 × 105 cells per culture were exposed to the dimeric impurity of cefotaxime at the concentration of 11.25, 22.5, and 45 mg per culture, with or without metabolic activation, and harvested at 18 h after exposure. No chromosomal aberrations in the cultured mammalian cells were recorded. Acute intramuscular administration of the dimeric impurity of cefotaxime in Sprague-Dawley rats did not result in any clinical signs and gross pathological changes up to 2000 mg/kg-body weight. The results of these studies indicated that the dimeric impurity of cefotaxime is nonmutagenic in Ames test, nonclastogenic in vitro, and acutely nontoxic in rats.

Disruption of the three cytoskeletal networks in mammalian cells does not affect transcription, translation, or protein translocation changes induced by heat shock

1985 ◽  
Vol 5 (7) ◽  
pp. 1571-1581
Author(s):  
W J Welch ◽  
J R Feramisco
Keyword(s):  
Heat Shock ◽  
Heat Shock Response ◽  
Mammalian Cells ◽  
Stress Proteins ◽  
Protein Translocation ◽  
Shock Response ◽  
Cytochalasin E ◽  
Cytoskeletal Networks ◽  
Shock Proteins ◽  
Cytoskeletal Elements

Mammalian cells show a complex series of transcriptional and translational switching events in response to heat shock treatment which ultimately lead to the production and accumulation of a small number of proteins, the so-called heat shock (or stress) proteins. We investigated the heat shock response in both qualitative and quantitative ways in cells that were pretreated with drugs that specifically disrupt one or more of the three major cytoskeletal networks. (These drugs alone, cytochalasin E and colcemid, do not result in induction of the heat shock response.) Our results indicated that disruption of the actin microfilaments, the vimentin-containing intermediate filaments, or the microtubules in living cells does not hinder the ability of the cell to undergo an apparently normal heat shock response. Even when all three networks were simultaneously disrupted (resulting in a loose, baglike appearance of the cells), the cells still underwent a complete heat shock response as assayed by the appearance of the heat shock proteins. In addition, the major induced 72-kilodalton heat shock protein was efficiently translocated from the cytoplasm into its proper location in the nucleus and nucleolus irrespective of the condition of the three cytoskeletal elements.

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