Characterization of a heat-resistant strain of Tilapia ovary cells

Tilapia ovary cells (TO-2) cease to proliferate when moved from normal growth temperature of 31 degrees C to 37 degrees C, and arrest in G1 and G2 phases of the cell cycle. The ability of the arrested cells to re-enter the cell cycle when restored to 31 degrees C decreases inversely with time spent at 37 degrees C. A heat-resistant strain, TO-37c, cloned from the surviving fraction of TO-2 after heat treatment, has been found to re-enter the cell cycle with greater facility and to have a higher rate of survival. TO-37c cells have a smaller cell volume than TO-2 and show a distinct morphology at 37 degrees C. Most of the heat-shock proteins (hsps) induced on temperature change were similar, but in TO-37c the decline in the synthesis of a 27 X 10(3) Mr hsp was faster and a 37 degrees C-specific 60 X 10(3) Mr hsp was missing. Ultraviolet (u.v.) sensitivity was slightly affected if heat treatment was given after irradiation. However, when cells were preheated and then u.v. irradiated, the u.v. sensitivity increased sharply for TO-2 cells but not for TO-37c.

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Ethanol and carbon-source starvation enhance the accumulation of HSP80 in Neurospora crassa

Canadian Journal of Microbiology ◽

10.1139/m88-031 ◽

1988 ◽

Vol 34 (2) ◽

pp. 162-168 ◽

Cited By ~ 7

Author(s):

H. S. Roychowdhury ◽

M. Kapoor

Keyword(s):

Heat Shock ◽

Neurospora Crassa ◽

Carbon Catabolite Repression ◽

Normal Growth ◽

Carbon Starvation ◽

High Molecular Mass ◽

Sucrose Starvation ◽

Shock Response ◽

Shock Proteins ◽

Starvation Conditions

In Neurospora crassa, heat shock results in the induction of 9 to 11 heat shock proteins (HSP), of which HSP80 is the most abundant and the first to be synthesized. The induction of HSP80 was investigated during normal growth (2% sucrose) and under sucrose starvation. Transfer of mycelium to a medium supplemented with ethanol stimulated the synthesis of HSP80, even at the normal growth temperature of 28 °C. It was also synthesized under carbon starvation conditions, where the medium was supplemented with 0.02% sucrose, 0.3% acetate, 0.2% lactate, or ethanol. A 30–35 kilodalton polypeptide was induced by heat shock in carbon-sufficient media, but in 0.02% sucrose and 0.3% acetate containing media it was synthesized at normal temperatures. While the overall heat shock response remained unaltered in these cultures, the abundance of HSP90 and HSP70, relative to HSP80, was greater. HSP80 appears to be controlled by carbon-catabolite repression as well as heat shock. Another high molecular mass protein (tentatively designated alc'80') was observed to be induced by heat shock, provided carbon starvation conditions prevailed concurrently.

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Proteomic analysis of heat shock proteins in maize (Zea mays L.)

Bulletin of the National Research Centre ◽

10.1186/s42269-019-0251-2 ◽

2019 ◽

Vol 43 (1) ◽

Cited By ~ 1

Author(s):

Mahmoud Hussien Abou-Deif ◽

Mohamed Abdel-Salam Rashed ◽

Kamal Mohamed Khalil ◽

Fatma El-Sayed Mahmoud

Keyword(s):

Heat Treatment ◽

Heat Stress ◽

Heat Shock ◽

Heat Shock Proteins ◽

Proteome Analysis ◽

High Temperature Stress ◽

Heat Treatments ◽

Maize Plants ◽

Adverse Influence ◽

Shock Proteins

Abstract Background Maize is one of the important cereal food crops in the world. High temperature stress causes adverse influence on plant growth. When plants are exposed to high temperatures, they produce heat shock proteins (HSPs), which may impart a generalized role in tolerance to heat stress. Proteome analysis was performed in plant to assess the changes in protein types and their expression levels under abiotic stress. The purpose of the study is to explore which proteins are involved in the response of the maize plant to heat shock treatment. Results We investigated the responses of abundant proteins of maize leaves, in an Egyptian inbred line of maize “K1”, upon heat stress through two-dimensional electrophoresis (2-DE) on samples of maize leaf proteome. 2-DE technique was used to recognize heat-responsive protein spots using Coomassie Brilliant Blue (CBB) and silver staining. In 2-D analysis of proteins from plants treated at 45 °C for 2 h, the results manifested 59 protein spots (4.3%) which were reproducibly detected as new spots where did not present in the control. In 2D for treated plants for 4 h, 104 protein spots (7.7%) were expressed only under heat stress. Quantification of spot intensities derived from heat treatment showed that twenty protein spots revealed clear differences between the control and the two heat treatments. Nine spots appeared with more intensity after heat treatments than the control, while four spots appeared only after heat treatments. Five spots were clearly induced after heat treatment either at 2 h or 4 h and were chosen for more analysis by LC-MSMS. They were identified as ATPase beta subunit, HSP26, HSP16.9, and unknown HSP/Chaperonin. Conclusion The results revealed that the expressive level of the four heat shock proteins that were detected in this study plays important roles to avoid heat stress in maize plants.

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Characterization of progesterone receptor binding to the 90- and 70-kDa heat shock proteins.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(18)54835-3 ◽

1991 ◽

Vol 266 (31) ◽

pp. 21165-21173 ◽

Cited By ~ 3

Author(s):

D.B. Schowalter ◽

W.P. Sullivan ◽

N.J. Maihle ◽

A.D. Dobson ◽

O.M. Conneely ◽

...

Keyword(s):

Heat Shock ◽

Heat Shock Proteins ◽

Progesterone Receptor ◽

Receptor Binding ◽

Shock Proteins

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Heat shock response of Saccharomyces cerevisiae mutants altered in cyclic AMP-dependent protein phosphorylation

Molecular and Cellular Biology ◽

10.1128/mcb.7.1.244-250.1987 ◽

1987 ◽

Vol 7 (1) ◽

pp. 244-250

Author(s):

D Y Shin ◽

K Matsumoto ◽

H Iida ◽

I Uno ◽

T Ishikawa

Keyword(s):

Heat Treatment ◽

Saccharomyces Cerevisiae ◽

Heat Shock ◽

Cyclic Amp ◽

Heat Shock Proteins ◽

Temperature Shift ◽

G1 Phase ◽

Shock Response ◽

Dependent Protein ◽

Shock Proteins

When Saccharomyces cerevisiae cells grown at 23 degrees C were transferred to 36 degrees C, they initiated synthesis of heat shock proteins, acquired thermotolerance to a lethal heat treatment given after the temperature shift, and arrested their growth transiently at the G1 phase of the cell division cycle. The bcy1 mutant which resulted in production of cyclic AMP (cAMP)-independent protein kinase did not synthesize the three heat shock proteins hsp72A, hsp72B, and hsp41 after the temperature shift. The bcy1 cells failed to acquire thermotolerance to the lethal heat treatment and were not arrested at the G1 phase after the temperature shift. In contrast, the cyr1-2 mutant, which produced a low level of cAMP, constitutively produced three heat shock proteins and four other proteins without the temperature shift and was resistant to the lethal heat treatment. The results suggest that a decrease in the level of cAMP-dependent protein phosphorylation results in the heat shock response, including elevated synthesis of three heat shock proteins, acquisition of thermotolerance, and transient arrest of the cell cycle.

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Identification and characterization of molecular interactions between mortalin/mtHsp70 and HSP60

Biochemical Journal ◽

10.1042/bj20050861 ◽

2005 ◽

Vol 391 (2) ◽

pp. 185-190 ◽

Cited By ~ 64

Author(s):

Renu Wadhwa ◽

Syuichi Takano ◽

Kamaljit Kaur ◽

Satoshi Aida ◽

Tomoko Yaguchi ◽

...

Keyword(s):

Heat Shock ◽

Molecular Interactions ◽

Heat Shock Protein 60 ◽

Hsp60 Expression ◽

Mitochondrial Hsp70 ◽

Shock Proteins ◽

First Time

Mortalin/mtHsp70 (mitochondrial Hsp70) and HSP60 (heat-shock protein 60) are heat-shock proteins that reside in multiple subcellular compartments, with mitochondria being the predominant one. In the present study, we demonstrate that the two proteins interact both in vivo and in vitro, and that the N-terminal region of mortalin is involved in these interactions. Suppression of HSP60 expression by shRNA (short hairpin RNA) plasmids caused the growth arrest of cancer cells similar to that obtained by suppression of mortalin expression by ribozymes. An overexpression of mortalin, but not of HSP60, extended the in vitro lifespan of normal fibroblasts (TIG-1). Taken together, this study for the first time delineates: (i) molecular interactions of HSP60 with mortalin; (ii) their co- and exclusive localizations in vivo; (iii) their involvement in tumorigenesis; and (iv) their functional distinction in pathways involved in senescence.

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Expression of heat shock protein 70 is insufficient to extend Drosophila melanogaster longevity

10.1101/753269 ◽

2019 ◽

Author(s):

Chengfeng Xiao ◽

Danna Hull ◽

Shuang Qiu ◽

Joanna Yeung ◽

Jie Zheng ◽

...

Keyword(s):

Heat Treatment ◽

Drosophila Melanogaster ◽

Heat Shock ◽

Heat Shock Protein ◽

Stress Resistance ◽

Heat Shock Protein 70 ◽

Biological Effect ◽

Hsp70 Expression ◽

Gene Encoding ◽

Shock Proteins

AbstractIt has been known for over 20 years that Drosophila melanogaster flies with twelve additional copies of the hsp70 gene encoding the 70 kDa heat shock protein lives longer after a non-lethal heat treatment. Since the heat treatment also induces the expression of additional heat shock proteins, the biological effect can be due either to HSP70 acting alone or in combination. This study used the UAS/GAL4 system to determine whether hsp70 is sufficient to affect the longevity and the resistance to thermal, oxidative or desiccation stresses of the whole organism. We observed that HSP70 expression in the nervous system or muscles has no effect on longevity or stress resistance but ubiquitous expression reduces the life span of males. We also observed that the down-regulation of Hsp70 using RNAi did not affect longevity.

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The Acquisition and Maintenance of Thermotolerance in Australian Wheats

Functional Plant Biology ◽

10.1071/pp9900037 ◽

1990 ◽

Vol 17 (1) ◽

pp. 37 ◽

Cited By ~ 10

Author(s):

C Blumenthal ◽

F Bekes ◽

CW Wrigley ◽

EWR Barlow

Keyword(s):

Heat Treatment ◽

Triticum Aestivum ◽

Protein Synthesis ◽

High Temperature ◽

Heat Shock ◽

High Temperature Stress ◽

Time Interval ◽

Degree Of Protection ◽

Concomitant Reduction ◽

Shock Proteins

The exposure of wheat (Triticum aestivum) coleoptiles to a transient high temperature stress results in the synthesis of a group of proteins known as the heat shock proteins (hsps). The appearance of these proteins is associated with a concomitant reduction in normal protein synthesis and has been correlated with the acquisition of thermotolerance (assessed as growth of coleoptiles). Pretreatment with a sublethal heat shock confers protection to a subsequent heat shock that would otherwise have been lethal. In addition, we find that increasing the time interval between the sublethal heat treatment and the subsequent heat shock from 0 to 72 h reduces the protective effect of the sublethal heat treatment considerably. The five cultivars examined (Sunelg, Sunco, Hartog, Vulcan, Halberd) showed differences in the degree of protection acquired, and in the length of time for which protection was maintained. Hartog was found to be the most thermotolerant, and acquired the greatest degree of protection from exposure to a sublethal heat treatment, but the duration of this acquired protection was shorter than in the remaining cultivars. Sunelg was most susceptible to a heat shock but the duration of acquired protection was the greatest.

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