The synergistic effect of hyperthermia and ethanol on changing gene expression of mouse lymphocytes

1986 ◽  
Vol 28 (6) ◽  
pp. 1115-1124 ◽  
Author(s):  
David I. Rodenhiser ◽  
Jack H. Jung ◽  
Burr G. Atkinson
Keyword(s):  
Gene Expression ◽  
Elevated Temperature ◽  
Heat Shock ◽  
Rna Synthesis ◽  
Ethanol Stress ◽  
Short Term ◽  
Select Group ◽  
Molecular Masses ◽  
Shock Proteins ◽  
Mouse Lymphocytes

Cultured mouse lymphocytes respond to a brief incubation at an elevated temperature (41–43 °C) with the new and (or) enhanced synthesis of a select group of polypeptides (known as heat-shock proteins, HSPs) having relative molecular masses of 110, 100, 90, 70, and 65 kilodaltons (kDa). Expression of these HSPs is dependent on new RNA synthesis. Because the synthesis of any particular HSP is dependent on the temperature and the length of time cells remain at a particular elevated temperature, synthesis of each HSP is not necessarily coordinated with the synthesis of the other HSPs. Cultured mouse lymphocytes treated with arsenite or ethanol exhibit new and (or) enhanced synthesis of HSPs with molecular masses of 110, 90, 70, and 65 kDa but do not exhibit enhanced synthesis of the 100-kDa HSP. Short-term concurrent exposure of mouse lymphocytes to an elevated temperature and a level of ethanol, which individually do not induce detectable HSP synthesis, results in the pronounced synthesis of HSPs similar to those seen following exposure to higher levels of either stress applied separately. Thus, in this study we demonstrate that hyperthermia and ethanol stress can act synergistically to affect a dramatic change in the gene expression of mouse lymphocytes.Key words: heat shock, ethanol, gene expression, lymphocytes.

Mammalian lymphocytes: stress-induced synthesis of heat-shock proteins in vitro and in vivo

1985 ◽  
Vol 63 (7) ◽  
pp. 711-722 ◽  
Author(s):  
David Rodenhiser ◽  
Jack H. Jung ◽  
Burr G. Atkinson
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
White Blood Cells ◽  
Sodium Dodecyl ◽  
Molecular Masses ◽  
Febrile Episodes ◽  
Shock Proteins ◽  
Mouse Lymphocytes

Mammalian (human, mouse, and rabbit) white blood cells (lymphocytes) maintained in culture respond to a brief incubation at an elevated temperature (at or above 41 °C) by (i) the new and (or) enhanced synthesis of a small number of proteins (the so-called heat-shock proteins; HSPs) having molecular masses of approximately 110 000, 100 000, 90 000, 70 000, 65 000, and 26 000 daltons and (ii) the depressed synthesis of proteins normally made at 37 °C. The HSPs synthesized in culture by human, rabbit, and mouse (peripheral and splenic) lymphocytes are similar in number, molecular mass, and distribution on two-dimensional (isoelectric focusing and sodium dodecyl sulfate – polyacrylamide) electrophoretic gels to those synthesized in vivo by lymphocytes in hyperthermic mice. Since the level of hyperthermia used to induce HSP synthesis in mouse lymphocytes in vitro and in vivo is of a magnitude (41 °C) also used to promote thermotolerance in mice and is similar to temperatures attained during febrile episodes in rabbits and in humans, we suggest that the in vitro and in vivo synthesis of HSPs by mouse lymphocytes, demonstrated in this study, represents a relevant, physiological response which mammalian lymphocytes may normally use to survive periods of thermal stress.

Expression of the genes encoding hsp73, hsp18, and ubiquitin in radicles of heat-shocked maize seedlings

Genome ◽  
1989 ◽  
Vol 31 (2) ◽  
pp. 698-704 ◽  
Author(s):  
Burr G. Atkinson ◽  
Ling Liu ◽  
Ing Swie Goping ◽  
David B. Walden
Keyword(s):  
Elevated Temperature ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Continuous Exposure ◽  
State Control ◽  
Fourfold Increase ◽  
Genes Encoding ◽  
Molecular Masses ◽  
Shock Proteins ◽  
Steady State Control

Radicles of intact 5-day-old maize (cv. OH43) seedlings exposed to a rapid, short-term elevation (2 h) in environmental (25 to 42.5 °C) temperature exhibit new and (or) enhanced synthesis of a specific set of proteins, the so-called heat shock proteins (hsps), with molecular masses of 108 000, 89 000, 84 000, 76 000, 73 000, 30 000, 23 000, and 18 000. Continuous exposure of intact seedlings to this elevated temperature results in a depression in the synthesis of these hsps after 8 – 12 h and a shift in the pattern of the proteins synthesized to one that resembles those proteins synthesized by radicles from seedlings grown at 25 °C. The transient synthesis of hsp73 and the hsp18 family in radicles from seedlings exposed to, and maintained at, an elevated temperature correlates with the levels of hsp73 and hsp18 mRNAs associated with their polyribosomes. The heat shock induced accumulation of these hsp mRNAs occurs concomitantly with a fourfold increase in polyribosome-associated ubiquitin mRNAs. However, unlike the transient association of hsp73 and hsp18 mRNAs with polyribosomes in radicles from seedlings maintained at 42.5 °C (8 – 12 h), the level of uniquitin mRNAs associated with polyribosomes does not return to a steady-state control (25 °C) level for at least 24 h. The marked, rapid increase in the level of ubiquitin mRNAs associated with polyribosomes in radicles from heat-shocked seedlings provides the first evidence implicating ubiquitin as a heat shock protein of plants.Key words: heat Shock, heat shock proteins, ubiquitin, maize.

Effect of elevated temperatures on heat shock protein and ribulose-1,5-bisphosphate carboxylase gene expression in Brassica napus

1990 ◽  
Vol 68 (3) ◽  
pp. 609-615 ◽  
Author(s):  
J. R. Halle ◽  
S. Ghosh ◽  
E. B. Dumbroff ◽  
J. J. Heikkila
Keyword(s):  
Gene Expression ◽  
Brassica Napus ◽  
Heat Shock ◽  
Elevated Temperatures ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Immunoblot Analysis ◽  
Bisphosphate Carboxylase ◽  
Molecular Masses ◽  
Shock Proteins

Leaf segments of Brassica napus were exposed to 22, 35, 38, or 40 °C for up to 4 h. Analysis of radiolabeled proteins by two-dimensional sodium dodecyl sulfate – polyacrylamide gel electrophoresis and fluorography revealed two major groups of heat shock proteins (HSPs). One group comprised HSPs 70, 76, and 87, with (pIs) isoelectric points ranging from 5.7 to 6.1, whereas the second group had molecular masses ranging from 23 to 16 kilodaltons (kDa) and pIs from 5.6 to 6.9. Immunoblot analysis using antibodies directed against the large (RLSU) and small (RSSU) subunits of ribulose-1,5-bisphosphate carboxylase (RUBISCO) showed that increasing temperatures from 35 to 38° or 40 °C for the duration of thermal stress (i.e., from 1 to 5 h) did not affect levels of the RSSU (15 kDa), whereas levels of the RLSU (52 kDa) fell sharply. Nevertheless, the activity of RUBISCO was not adversely affected at 38 °C for periods of up to 5 h. Northern blot analysis revealed that the increase observed in HSP 70 synthesis during heat shock may be transcriptionally regulated, but the decrease in the RLSU was not accompanied by a corresponding reduction in levels of its mRNA.Key words: Brassica, heat shock, ribulose-1,5-bisphosphate carboxylase, gene expression.

scholarly journals Heat-induced expression of albumin during early stages of rat embryo development.

1987 ◽  
Vol 7 (12) ◽  
pp. 4599-4602 ◽  
Author(s):  
U K Srinivas ◽  
C J Revathi ◽  
M R Das
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Embryonic Liver ◽  
Rat Embryo ◽  
Adult Liver ◽  
Stages Of Development ◽  
Induced Expression ◽  
Molecular Events ◽  
Internal Change ◽  
Shock Proteins

An examination of heat-induced expression of proteins in tissues from adult and embryonic liver in rats shows that albumin, which is constitutively expressed in adult liver and is not synthesized in embryos before 16 days of gestation, appears in liver cells at earlier stages of development upon heat shock. On the basis of available evidence for the expression of heat shock proteins at distinct stages of development and on the basis of our findings, it may be argued that there could be common molecular events taking place during development and as a result of heat shock. We suggest also that one of the consequences of heat shock could be an internal change of pH within the cell which, in turn, might trigger alterations in gene expression.

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.

Induction of heat shock proteins in short-term cultured hepatocytes derived from normal and chronically griseofulvin-treated mice

Hepatology ◽  
1988 ◽  
Vol 8 (3) ◽  
pp. 607-612 ◽  
Author(s):  
Kurt Zatloukal ◽  
Ruth Sohar ◽  
Elisabeth Lackinger ◽  
Helmut Denk
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cultured Hepatocytes ◽  
Short Term ◽  
Shock Proteins
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