scholarly journals Differential activation of heat-shock and oxidation-specific stress genes in chemically induced oxidative stress

1995 ◽  
Vol 309 (2) ◽  
pp. 453-459 ◽  
Author(s):  
L Tacchini ◽  
G Pogliaghi ◽  
L Radice ◽  
E Anzon ◽  
A Bernelli-Zazzera
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Time Course ◽  
Consensus Sequence ◽  
Single Agent ◽  
Stress Protein ◽  
Hsp 70 ◽  
Activator Protein ◽  
Chemically Induced ◽  
Haem Oxygenase

Post-ischaemic reperfusion increases the level of the major heat-shock (stress) protein hsp 70 and of its mRNA by transcriptional mechanisms, and activates the binding of the heat-shock factor HSF to the consensus sequence HSE. In common with CoCl2 treatment, post-ischaemic reperfusion increases the level of haem oxygenase mRNA, an indicator of oxidative stress, but CoCl2 does not seem to induce the expression of the hsp 70 gene [Tacchini, Schiaffonati, Pappalardo, Gatti and Bernelli-Zazzera (1993) Lab. Invest. 68, 465-471]. Starting from these observations, we have now studied the expression of two genes of the hsp 70 family and of other possibly related genes under conditions of oxidative stress. Three different chemicals, which cause oxidative stress by various mechanisms and induce haem oxygenase, enhance the expression of the cognate hsc 73 gene, but do not activate the inducible hsp 70 gene. Expression of the other genes that have been studied seems to vary in intensity and/or time course, in relation to the particular mechanism of action of any single agent. The pattern of induction of the early-immediate response genes c-fos and c-jun observed during oxidative stress differs from that found in post-ischaemic reperfused livers. Oxidative-stress-inducing agents do not promote the binding of HSF to its consensus sequence HSE, such as occurs in heat-shock and post-ischaemic reperfusion, and fail to activate AP-1 (activator protein 1). With the possible exception of Phorone, the oxidative stress chemically induced in rat liver activates NFkB (nuclear factor kB) and AP-2 (activator protein 2) transcription factors.

scholarly journals Induction by prostaglandin A1 of haem oxygenase in myoblastic cells: an effect independent of expression of the 70 kDa heat shock protein

1995 ◽  
Vol 308 (2) ◽  
pp. 455-463 ◽  
Author(s):  
A Rossi ◽  
M G Santoro
Keyword(s):  
Heat Shock ◽  
Mammalian Cells ◽  
Present Report ◽  
Oxidant Stress ◽  
Stress Protein ◽  
Hsp70 Expression ◽  
Transcriptional Level ◽  
Protective Mechanisms ◽  
Haem Oxygenase ◽  
Prostaglandin A1

Prostaglandins of the A type (PGA) induce the synthesis of 70 kDa heat shock proteins (hsp70) in a large variety of mammalian cells. Induction of hsp70 has been associated with a cytoprotective effect of PGA1 after virus infection or thermal injury. In the present report we provide evidence that, in murine myoblasts, PGA1 is not able to induce hsp70 expression, whereas it increases the synthesis of the constitutive protein, hsc70, and dramatically induces the synthesis of a 32 kDa protein (p32). The p32 protein has been identified as haem oxygenase. PGA1 acts at the transcriptional level by inducing haem oxygenase mRNA synthesis, and the signal for induction appears to be associated with decreased intracellular GSH levels. Haem oxygenase, a low-molecular-mass stress protein induced in mammalian cells by oxidant stress, is known to be part of a general inducible antioxidant defence pathway. The fact that prostaglandin synthesis is stimulated in muscle during contraction and in the heart in response to ischaemia raises the possibility that induction of haem oxygenase by PGA in myoblasts could be part of a protective mechanisms in operation during stress and hypoxia.

Retinoic acid stimulates the synthesis of a novel heat shock protein in the regenerating forelimb of the newt

1993 ◽  
Vol 71 (1-2) ◽  
pp. 43-50 ◽  
Author(s):  
Robert L. Carlone ◽  
Robert P. Boulianne ◽  
K. Marion Vijh ◽  
Heather Karn ◽  
Gordon A. D. Fraser
Keyword(s):  
Retinoic Acid ◽  
Heat Shock ◽  
Stress Proteins ◽  
Limb Regeneration ◽  
Stress Protein ◽  
Cross Reactivity ◽  
Hsp 70 ◽  
Peptide Map ◽  
Shock Proteins

Morphogenetic effects of retinoic acid (RA) on the urodele amphibian limb regenerate pattern have been well documented, but little is known regarding the mechanism of this action of RA at the molecular level. Since exogenous RA, at concentrations sufficient to cause proximalization, represents a significant stress to newts and has been shown previously to elicit increased synthesis of heat shock proteins (HSPs) in mouse embryo limb buds, we investigated the effects of this putative morphogen on the synthesis of members of the 70-kilodalton (70-kDa) stress protein family in amputated forelimbs of the newt Notophthalmus viridescens. Injection (i.p.) of RA in dimethyl sulfoxide (DMSO), at a dose sufficient to cause significant proximal–distal reduplication of the pattern in 50% of animals treated, resulted in increased synthesis and accumulation of a 73-kDa protein with a pi of approximately 6.75. The synthesis of this same protein is increased in limb tissues as a result of a brief 35 °C heat shock. This protein is electrophoretically distinct from the newt HSP 70 family members, displays a different partial peptide map, and shows no immunological cross-reactivity with an anti-human HSP 70 monoclonal antibody. It may be a member of a separate family of 70- to 73-kDa HSPs. Interestingly, the synthesis of this protein is increased and it is more abundant in control, proximal moderate-early bud stage regenerates at 6 days after i.p. injection of DMSO than in similarly treated distal regenerates. This protein is, in addition, increased in distal regenerates to proximal levels by a prior injection of RA. The significance of these findings with regard to the possible role of stress proteins in the morphogenetic processes underlying limb regeneration is discussed.Key words: heat shock, limb regeneration, retinoic acid, pattern formation, newt.

Laboratory selection at different temperatures modifies heat-shock transcription factor (HSF) activation in Drosophila melanogaster

2001 ◽  
Vol 204 (2) ◽  
pp. 315-323 ◽  
Author(s):  
D.N. Lerman ◽  
M.E. Feder
Keyword(s):  
Transcription Factor ◽  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Time Course ◽  
Stress Protein ◽  
Laboratory Culture ◽  
Heat Shock Transcription Factor ◽  
Mobility Shift ◽  
Laboratory Selection ◽  
Mobility Shift Assay

The magnitude and time course of activation of the heat-shock transcription factor (HSF) differ among Drosophila melanogaster lines evolving at 18 degrees C, 25 degrees C or 28 degrees C for more than 20 years. At lower heat-shock temperatures (27–35 degrees C), flies from the 18 degrees C population had higher levels of activated HSF (as detected by an electrophoretic mobility shift assay) than those reared at 25 degrees C and 28 degrees C. At higher temperatures (36 and 37 degrees C), however, the 28 degrees C flies had the highest levels of HSF. These differences persisted after one generation of acclimation at 25 degrees C, suggesting that phenotypic plasticity was limited. In addition, larvae from the 28 degrees C lines activated HSF less rapidly after a 35 degrees C heat shock than those from the 18 degrees C and 25 degrees C populations. These results are similar but not identical to previously reported differences in expression of Hsp70 (the major heat-inducible stress protein in Drosophila melanogaster) among the experimental lines. We conclude that HSF activation evolves rapidly during laboratory culture at diverse temperatures and could play an important role in the evolution of the heat-shock response.

scholarly journals Rekombinan Vascular Endothelial Growth Factor-121 Menekan Ekspresi Heat Shock Protein-70 pada Plasenta Mencit Model Preeklampsia (VASCULAR ENDOTHELIAL GROWTH FACTOR-121 RECOMBINANT DEPRESSIS HEAT SHOCK PROTEIN-70 EXPRESSION IN PREECLAMPSIA MICE PLACENTA

2018 ◽  
Vol 18 (4) ◽  
pp. 589
Author(s):  
Sri Sulistyowati ◽  
Lungguk Helen Alfian Tanjung ◽  
Supriyadi Hari Respati ◽  
Soetrisno Soetrisno
Keyword(s):  
Oxidative Stress ◽  
Vascular Endothelial Growth Factor ◽  
Growth Factor ◽  
Heat Shock ◽  
Heat Shock Protein 70 ◽  
Vascular Endothelial ◽  
Model Group ◽  
Mice Model ◽  
Hsp 70 ◽  
Endothelial Growth Factor

Preeclampsia has remained a major cause of morbidity and maternal-perinatal mortality. Oxidative stress that occurs in preeclampsia increases HSP-70 expression. Therefore, VEGF therapy is expected to recover this oxidative stress. This research aimed to determine the role of VEGF-121 recombinant on HSP-70 expression in mice model of preeclampsia. This research was an explanatory study conducted at Animal Cage Experiment, Faculty of Veterinary Medicine, Airlangga University. The samples were 30 mice that were divided into 3 groups, namely a group of 10 normal pregnant mice, a group of 10 mice model of preeclampsia, and a group of 10 mice model of preeclampsia with VEGF-121 recombinant therapy. On the 16th day of gestation, HSP-70 expressions in the placenta of all mice were examined using immunohistochemical methods. The data were analyzed using Kruskall-Wallis test of SPSS program. The mean of HSP-70 expression in normal pregnancy group was 1.69 ± 0.68, in preeclampsia model group was 3.50 ± 0.95 with p = 0.00, and in preeclampsia model group with VEGF-121 recombinant therapy was 2.24 ± 0.84 with p = 0.00. In short, VEGF-121 recombinant has a role in lowering HSP-70 expression in mice placenta model of preeclampsia

scholarly journals Heat shock increases oxidative stress to modulate growth and physico-chemical attributes in diverse maize cultivars

2016 ◽  
Vol 30 (4) ◽  
pp. 519-531 ◽  
Author(s):  
Iqbal Hussain ◽  
Muhammad Arslan Ashraf ◽  
Rizwan Rasheed ◽  
Muhammad Iqbal ◽  
Muhammad Ibrahim ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Heat Shock ◽  
Membrane Permeability ◽  
Photosynthetic Pigments ◽  
Time Course ◽  
Significant Rise ◽  
Enzymatic Antioxidants ◽  
Maize Cultivars ◽  
Chemical Attributes ◽  
Relative Membrane Permeability

Abstract The present investigation was conducted to appraise the physiochemical adjustments in contrasting maize cultivars, namely, PakAfgoi (tolerant) and EV-5098 (sensitive) subjected to heat shock. Seven-day-old seedlings were exposed to heat shock for different time intervals (1, 3, 6, 24, 48 and 72 h) and data for various physiochemical attributes determined to appraise time course changes in maize. After 72 h of heat shock, the plants were grown under normal conditions for 5 d and data for different growth attributes and photosynthetic pigments recorded. Exposure to heat shock reduced growth and photosynthetic pigments in maize cultivars. The plants exposed to heat shock for up to 3 h recovered growth and photosynthetic pigments when stress was relieved. A time course rise in the relative membrane permeability, hydrogen peroxide (H2O2) and malondialdehyde contents was recorded particularly in the EV-5098 indicating that heat shock-induced oxidative stress. Activities of different enzymatic antioxidants greatly altered due to heat shock. For instance, an increase in superoxide dismutase activity was recorded in both maize cultivars. The activity of ascorbate peroxidase was greater in Pak-Afgoi. However, the peroxidase and catalase activities were higher in plants of EV-5098. Heat shock caused a significant rise in the proline and decline in the total free amino acids. Overall, the performance of Pak-Afgoi was better in terms of having lesser oxidative damage and greater cellular levels of proline. The results suggested that oxidative stress indicators (relative membrane permeability, H2O2 and malondialdehyde) and proline can be used as markers for heat shock tolerant plants.

Cytotoxicity and the induction of the stress protein Hsp 70 in Chang liver cells in response to zearalenone-induced oxidative stress

2013 ◽  
Vol 36 (2) ◽  
pp. 732-740 ◽  
Author(s):  
Hyungkyoung Lee ◽  
Changgeun Kang ◽  
Yong-San Yoo ◽  
Do-Yun Hah ◽  
Chung Hui Kim ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Stress Protein ◽  
Liver Cells ◽  
Hsp 70 ◽  
Chang Liver

scholarly journals The Role of Oxidative Stress in Koenimbine-Induced DNA Damage and Heat Shock Protein Modulation in HepG2 Cells

2016 ◽  
Vol 16 (4) ◽  
pp. 563-571 ◽  
Author(s):  
Yahya Hasan Hobani
Keyword(s):  
Oxidative Stress ◽  
Dna Damage ◽  
Ascorbic Acid ◽  
Heat Shock ◽  
Hepg2 Cells ◽  
Time Dependent ◽  
Dependent Manner ◽  
Hsp 70 ◽  
Hsp 90

Background. Murraya koenigii (L.) Spreng, is a significant herb of traditional Ayurvedic system of medicine. Koenimbine, a carbazole alkaloid isolated from this plant holds antiproliferative and apoptotic effects. The aim of this study was to assess koenimbine-induced DNA damage and to clarify the role of free radicals in cell death mechanisms, using HepG2 cells. Methods. The level of cytotoxicity was assayed by MTT assay. To elucidate the role of glutathione (GSH), the intracellular GSH level was analyzed. The effect of koenimbine in the cell mitochondria was evaluated using mitochondrial membrane potential (MMP) changes. Single cell gel electrophoresis assay was used to examine the level of DNA damage. Heat shock proteins, Hsp 70 and Hsp 90 expressions were checked at mRNA and protein level. Ascorbic acid and catalase were used as control antioxidants. Results. It was observed that koenimbine considerably increased DNA damage in HepG2 cells at subcytotoxic concentrations. Koenimbine induced the increased levels of reactive oxygen species (ROS) and reduction of GSH level in HepG2 cells, together with time-dependent loss of MMP. In addition, results clearly showed that koenimbine encouraged cells to express Hsp 70 and Hsp 90 in a concentration-dependent manner up to a concentration of 100 µM and a time-dependent manner at 24-hour incubation both at transcriptional and translational levels. The antioxidant capacity of ascorbic acid was found to be not as prominent as to catalase throughout the study. Conclusion. Based on these data it can be concluded that koenimbine causes DNA strand breaks in HepG2 cells, probably through oxidative stress. Moreover, the oxidative stress induced was closely associated with MMP reduction and GSH depletion associated with HSP modulation at subcytotoxic concentration.

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