Phenytoin-Induced Stress Protein Synthesis In Mouse Embryonic Tissue

Exposure of mammalian cells to a nonlethal heat-shock treatment, followed by a recovery period at 37 degrees C, results in increased cell survival after a subsequent and otherwise lethal heat-shock treatment. Here we characterize this phenomenon, termed acquired thermotolerance, at the level of translation. In a number of different mammalian cell lines given a severe 45 degrees C/30-min shock and then returned to 37 degrees C, protein synthesis was completely inhibited for as long as 5 h. Upon resumption of translational activity, there was a marked induction of heat-shock (or stress) protein synthesis, which continued for several hours. In contrast, cells first made thermotolerant (by a pretreatment consisting of a 43 degrees C/1.5-h shock and further recovery at 37 degrees C) and then presented with the 45 degrees C/30-min shock exhibited considerably less translational inhibition and an overall reduction in the amount of subsequent stress protein synthesis. The acquisition and duration of such "translational tolerance" was correlated with the expression, accumulation, and relative half-lives of the major stress proteins of 72 and 73 kD. Other agents that induce the synthesis of the stress proteins, such as sodium arsenite, similarly resulted in the acquisition of translational tolerance. The probable role of the stress proteins in the acquisition of translational tolerance was further indicated by the inability of the amino acid analogue, L-azetidine 2-carboxylic acid, an inducer of nonfunctional stress proteins, to render cells translationally tolerant. If, however, analogue-treated cells were allowed to recover in normal medium, and hence produce functional stress proteins, full translational tolerance was observed. Finally, we present data indicating that the 72- and 73-kD stress proteins, in contrast to the other major stress proteins (of 110, 90, and 28 kD), are subject to strict regulation in the stressed cell. Quantitation of 72- and 73-kD synthesis after heat-shock treatment under a number of conditions revealed that "titration" of 72/73-kD synthesis in response to stress may represent a mechanism by which the cell monitors its local growth environment.

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Castor Bean Mitochondrial Protein Synthesis in Response to Temperature-Induced Stress

Plant Mitochondria ◽

10.1007/978-1-4899-3517-5_51 ◽

1987 ◽

pp. 309-312

Author(s):

Naheed Kaderbhai ◽

R. Brian Beechey ◽

Mustak Kaderbhai

Keyword(s):

Protein Synthesis ◽

Castor Bean ◽

Mitochondrial Protein ◽

Mitochondrial Protein Synthesis ◽

Induced Stress ◽

Response To Temperature

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Stress protein synthesis in cultured cardiac cells

Journal of Molecular and Cellular Cardiology ◽

10.1016/s0022-2828(87)80720-4 ◽

1987 ◽

Vol 19 ◽

pp. S32-S32

Author(s):

L BUGAISKY ◽

R HALL ◽

R MORIMOTO

Keyword(s):

Protein Synthesis ◽

Stress Protein ◽

Cardiac Cells

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Synthesis of 70K stress protein by human leukocytes: effect of exercise in the heat

Journal of Applied Physiology ◽

10.1152/jappl.1991.70.1.466 ◽

1991 ◽

Vol 70 (1) ◽

pp. 466-471 ◽

Cited By ~ 59

Author(s):

A. J. Ryan ◽

C. V. Gisolfi ◽

P. L. Moseley

Keyword(s):

Protein Synthesis ◽

Relative Humidity ◽

Treadmill Exercise ◽

Stress Protein ◽

Exercise Bout ◽

Time Dependent ◽

Dependent Manner ◽

Human Leukocytes ◽

Before And After

To determine whether reinduction of 70,000-Da (70K) stress protein synthesis could be used as an assay for thermal history and/or cellular levels of 70K stress protein in hyperthermic humans, leukocytes were obtained before and after 2 h of exercise and then incubated at 37 or 41 degrees C. Five healthy males completed 2 h of treadmill exercise consisting of running at 4–6 km/h for 30–45 min followed by 75–90 min of walking up a 2–10% grade. This exercise bout was performed by two subjects in hot (46 degrees C, 15% relative humidity) and by five subjects in cooler (30 degrees C, 40% relative humidity) environmental conditions. Exercise resulting in rectal temperature (Tre) less than 40 degrees C did not alter the amount of 70K stress protein synthesized by leukocytes incubated at 41 degrees C. In contrast, exercise resulting in Tre greater than 40 degrees C reduced the amount of 70K stress protein synthesized by leukocytes incubated at 41 degrees C. A protein immunoblot, probed with an antibody specific for the inducible 72K stress protein, showed that the reduction of 35S-labeled 70K stress protein in these postexercise leukocyte samples occurred without marked elevations of this protein. In vitro incubation of human leukocytes at 40 degrees C for 15–120 min reduced, in a time-dependent manner, the amount of 70K stress protein synthesized during a subsequent 41 degrees C heat stress. This reduction of 70K stress protein synthesis in 41 degrees C-treated leukocytes was abolished when cycloheximide was present during the 40 degrees C preincubation.(ABSTRACT TRUNCATED AT 250 WORDS)

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228 Cytotoxicity, inhibition of protein synthesis and induction of stress protein expression in HEP G2 cell line in response to zearalenone

Toxicology Letters ◽

10.1016/s0378-4274(03)90227-x ◽

2003 ◽

Vol 144 ◽

pp. s64-s65 ◽

Cited By ~ 1

Author(s):

Wafa Hassen ◽

Isabelle Baudrimont ◽

M. Moncef Ladjimi ◽

Edmond Creppy ◽

Hassen Bacha

Keyword(s):

Protein Synthesis ◽

Protein Expression ◽

Cell Line ◽

Stress Protein ◽

Hep G2 ◽

Inhibition Of Protein Synthesis

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Synthesis of stress protein 70 (Hsp70) in rainbow trout (Oncorhynchus mykiss) red blood cells

Journal of Experimental Biology ◽

10.1242/jeb.200.3.607 ◽

1997 ◽

Vol 200 (3) ◽

pp. 607-614 ◽

Cited By ~ 6

Author(s):

S Currie ◽

B Tufts

Keyword(s):

Protein Synthesis ◽

Rainbow Trout ◽

Heat Shock ◽

Oncorhynchus Mykiss ◽

Red Blood Cells ◽

Blood Cells ◽

Stress Proteins ◽

Stress Protein ◽

Rainbow Trout Oncorhynchus Mykiss ◽

Hsp70 Synthesis

Unlike enucleated mammalian red blood cells (rbcs), the nucleated rbcs of lower vertebrates are capable of protein synthesis and may, therefore, serve as a valuable model to investigate the adaptive significance of stress protein synthesis in cells. This study examined the synthesis of stress protein 70 (Hsp70) in rbcs of the temperature-sensitive rainbow trout Oncorhynchus mykiss in response to heat shock and anoxia. Through western blot analysis, we have demonstrated that rainbow trout rbcs synthesize Hsp70 both constitutively and in response to an increase in temperature. Radioisotopic labelling experiments indicated that the temperature at which Hsp70 synthesis was induced in fish acclimated to 10 °C was between 20 and 25 °C. Actinomycin D blocked de novo Hsp70 synthesis, implying that synthesis of Hsp70 is regulated at the level of transcription in rainbow trout rbcs. Since trout rbcs rely heavily on aerobic metabolism, but may also experience very low oxygen levels within the circulation, we also examined the relative importance of (1) anoxia as a stimulus for Hsp70 synthesis and (2) oxygen as a requirement for protein synthesis under control and heat-shock conditions. We found that trout rbcs were capable of protein synthesis during 2 h of anoxia, but did not increase Hsp70 synthesis. Moreover, rbcs subjected to combined anoxia and heat shock exhibited increases in Hsp70 synthesis that were similar in magnitude to those in cells exposed to heat shock alone. The latter results suggest that rainbow trout rbcs are (1) able to synthesize non-stress proteins during anoxia, (2) capable of tolerating periods of reduced oxygen availability without increased synthesis of stress proteins and (3) able to maintain the integrity of their heat-shock response even during periods of anoxia.

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Aortic perfusion pressure as early determinant of beta-isomyosin expression in perfused hearts

AJP Heart and Circulatory Physiology ◽

10.1152/ajpheart.1992.263.5.h1537 ◽

1992 ◽

Vol 263 (5) ◽

pp. H1537-H1545

Author(s):

C. Delcayre ◽

D. Klug ◽

V. T. Nguyen ◽

C. Mouas ◽

B. Swynghedauw

Keyword(s):

Protein Synthesis ◽

Total Protein ◽

Stress Protein ◽

Pressure Overload ◽

Aortic Pressure ◽

Mechanical Stimulus ◽

Beating Heart ◽

Specific Gene ◽

Coronary Pressure

Pressure overload in vivo induces an increase in cardiac protooncogene and stress protein expression that may initiate the long-term genetic changes observed in hypertrophy. To known whether mechanical stimulus is linked to specific gene transcription, expression of immediate early genes and synthesis of total proteins and myosin heavy chains (MHCs) were studied in beating and KCl-arrested isolated rat hearts perfused for 2 h under various coronary pressures. The main result of this study is that in the beating heart an augmentation of aortic pressure from 60 to 120 mmHg results in a pronounced enhancement of the synthesis of MHC (+59%) and of the expression of the beta-MHC isomyosin mRNA (iso-mRNA; +104%). Also, total protein synthesis and the amounts of poly-(A)+, c-fos, c-myc, and heat-shock protein HSP68 mRNAs were increased. To arrest the heart at 60 mmHg has no effect on total protein synthesis and on the amounts of poly(A)+, alpha-MHC and beta-MHC iso-mRNAs, and mRNAs coding for oncoproteins, but the synthesis of MHC decreased by 24%. By contrast with what we have observed in the beating heart, the augmentation of the coronary pressure in the arrested heart stimulates total protein synthesis and increases the amount of poly(A)+, c-fos, c-myc, and HSP68 mRNAs but has no effect on the expression of both MHC iso-mRNAs. In conclusion, the activation of myosin synthesis by high coronary pressure in this model has mainly a pretranslational origin when the heart is beating.(ABSTRACT TRUNCATED AT 250 WORDS)

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