Effect of herbimycin A on hsp30 and hsp70 heat shock protein gene expression in Xenopus cultured cells

1997 ◽  
Vol 75 (6) ◽  
pp. 777-782 ◽  
Author(s):  
Douglas Briant ◽  
Nicholas Ohan ◽  
John J Heikkila
Keyword(s):  
Gene Expression ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Proteins ◽  
Cultured Cells ◽  
Concurrent Treatment ◽  
Hsp70 Mrna ◽  
Mild Heat ◽  
Herbimycin A ◽  
Shock Proteins

We have examined the effect of herbimycin A, a benzoquinoid ansamycin antibiotic, on the pattern of gene expression in amphibians. Exposure of Xenopus laevis A6 kidney epithelial cells to 1 µg/mL herbimycin A induced the synthesis of the heat shock proteins hsp30 and hsp70 as well as 33- and 45-kDa proteins. Enhanced synthesis of a 34-kDa protein appears to be specific to herbimycin A because its synthesis did not increase after heat shock (35°C). In addition, the synthesis of hsp30 and hsp70 induced by herbimycin A was accompanied by an increase in their mRNAs. Herbimycin A induced a transient accumulation of hsp30 and hsp70 mRNA, which peaked between 4 and 6 h. Finally, concurrent treatment of cells with 0.5 µg/mL herbimycin A and a mild heat shock of 27°C yielded a synergistic accumulation of hsp30 and hsp70 mRNA. These studies demonstrate that herbimycin A can induce the expression of a set of stress proteins in amphibians and that concurrent treatment with herbimycin A and mild heat shock has a synergistic effect on the accumulation of hsp30 and hsp70 mRNA. Key words: heat shock, heat shock proteins, Xenopus, herbimycin A, mRNA.

Biochemical and Immunocytochemical Localization of Heat-Shock Proteins in Drosophila Cultured Cells

1985 ◽  
Vol 455 (1 Intermediate) ◽  
pp. 712-714 ◽  
Author(s):  
ROBERT M. TANGUAY ◽  
JEAN-LOUP DUBAND ◽  
FRANCINE LETTRE ◽  
JEAN-PAUL VALET ◽  
ANDRÉ PATRICK ARRIGO ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cultured Cells ◽  
Immunocytochemical Localization ◽  
Shock Proteins

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.

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.

Exertional heat injury and gene expression changes: a DNA microarray analysis study

2004 ◽  
Vol 96 (5) ◽  
pp. 1943-1953 ◽  
Author(s):  
Larry A. Sonna ◽  
C. Bruce Wenger ◽  
Scott Flinn ◽  
Holly K. Sheldon ◽  
Michael N. Sawka ◽  
...  
Keyword(s):  
Gene Expression ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Evidence ◽  
Peripheral Blood Mononuclear ◽  
Heat Injury ◽  
Shock Proteins

This study examined gene expression changes associated with exertional heat injury (EHI) in vivo and compared these changes to in vitro heat shock responses previously reported by our laboratory. Peripheral blood mononuclear cell (PBMC) RNA was obtained from four male Marine recruits (ages 17-19 yr) who presented with symptoms consistent with EHI, core temperatures ranging from 39.3 to 42.5°C, and elevations in serum enzymes such as creatine kinase. Controls were age- and gender-matched Marines from whom samples were obtained before and several days after an intense field-training exercise in the heat (“The Crucible”). Expression analysis was performed on Affymetrix arrays (containing ∼12,600 sequences) from pooled samples obtained at three times for EHI group (at presentation, 2-3 h after cooling, and 1-2 days later) and compared with control values (average signals from two chips representing pre- and post-Crucible samples). After post hoc filtering, the analysis identified 361 transcripts that had twofold or greater increases in expression at one or more of the time points assayed and 331 transcripts that had twofold or greater decreases in expression. The affected transcripts included sequences previously shown to be heat-shock responsive in PBMCs in vitro (including both heat shock proteins and non-heat shock proteins), a number of sequences whose changes in expression had not previously been noted as a result of in vitro heat shock in PBMCs (including several interferon-induced sequences), and several nonspecific stress response genes (including ubiquitin C and dual-specificity phosphatase-1). We conclude that EHI produces a broad stress response that is detectable in PBMCs and that heat stress per se can only account for some of the observed changes in transcript expression. The molecular evidence from these patients is thus consistent with the hypothesis that EHI can result from cumulative effects of multiple adverse interacting stimuli.

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.

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