scholarly journals The Neuronal Stress Response: Nuclear Translocation of Heat Shock Proteins as an Indicator of Hyperthermic Stress

1996 ◽  
Vol 229 (1) ◽  
pp. 35-47 ◽  
Author(s):  
P. Manzerra ◽  
I.R. Brown
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Nuclear Translocation ◽  
Shock Proteins ◽  
Neuronal Stress

Role of plant heat-shock proteins and molecular chaperones in the abiotic stress response

2004 ◽  
Vol 9 (5) ◽  
pp. 244-252 ◽  
Author(s):  
Wangxia Wang ◽  
Basia Vinocur ◽  
Oded Shoseyov ◽  
Arie Altman
Keyword(s):  
Abiotic Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Chaperones ◽  
Abiotic Stress Response ◽  
Shock Proteins

scholarly journals The Major Heat Shock Proteins, Hsp70 and Hsp90, in 2-Methoxyestradiol-Mediated Osteosarcoma Cell Death Model

2020 ◽  
Vol 21 (2) ◽  
pp. 616
Author(s):  
Magdalena Gorska-Ponikowska ◽  
Alicja Kuban-Jankowska ◽  
Antonella Marino Gammazza ◽  
Agnieszka Daca ◽  
Justyna M. Wierzbicka ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Heat Shock ◽  
Nitric Oxide Synthase ◽  
Heat Shock Proteins ◽  
Nuclear Translocation ◽  
Neuronal Nitric Oxide Synthase ◽  
Osteosarcoma Cell ◽  
Anticancer Efficacy ◽  
Shock Proteins ◽  
Oxide Synthase

2-Methoxyestradiol is one of the natural 17β-estradiol derivatives and a potential novel anticancer agent currently being under evaluation in advanced phases of clinical trials. However, the mechanism of anticancer action of 2-methoxyestradiol has not been yet fully established. In our previous studies we have demonstrated that 2-methoxyestradiol selectively induces the expression and nuclear translocation of neuronal nitric oxide synthase in osteosarcoma 143B cells. Heat shock proteins (Hsps) are factors involved in the regulation of expression and activity of nitric oxide synthases. Herein, we chose osteosarcoma cell lines differed in metastatic potential, metastatic 143B and highly metastatic MG63.2 cells, in order to further investigate the anticancer mechanism of 2-methoxyestradiol. The current study aimed to determine the role of major heat shock proteins, Hsp90 and Hsp70 in 2-methoxyestradiol-induced osteosarcoma cell death. We focused on the implication of Hsp90 and Hsp70 in control under expression of neuronal nitric oxide synthase, localization of the enzyme, and further generation of nitro-oxidative stress. To give the insight into the role of Hsp90 in regulation of anticancer efficacy of 2-methoxyestradiol, we used geldanamycin as a potent Hsp90 inhibitor. Herein, we evidenced that inhibition of Hsp90 controls the protein expression of 2-methoxyestradiol-induced neuronal nitric oxide synthase and inhibits enzyme nuclear translocation. We propose that decreased level of neuronal nitric oxide synthase protein after a combined treatment with 2-methoxyestradiol and geldanamycin is directly associated with the accompanying upregulation of Hsp70 and downregulation of Hsp90. This interaction resulted in abrogation of anticancer efficacy of 2-methoxyestradiol by geldanamycin.

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.

scholarly journals Unraveling Regulation of the Small Heat Shock Proteins by the Heat Shock Factor HvHsfB2c in Barley: Its Implications in Drought Stress Response and Seed Development

PLoS ONE ◽  
2014 ◽  
Vol 9 (3) ◽  
pp. e89125 ◽  
Author(s):  
Palakolanu Sudhakar Reddy ◽  
Polavarapu B. Kavi Kishor ◽  
Christiane Seiler ◽  
Markus Kuhlmann ◽  
Lennart Eschen-Lippold ◽  
...  
Keyword(s):  
Drought Stress ◽  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Seed Development ◽  
Heat Shock Factor ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Expression of Heat Shock and Other Stress Response Proteins in Ticks and Cultured Tick Cells in Response to Anaplasma spp. Infection and Heat Shock

2010 ◽  
Vol 2010 ◽  
pp. 1-11 ◽  
Author(s):  
Margarita Villar ◽  
Nieves Ayllón ◽  
Ann T. Busby ◽  
Ruth C. Galindo ◽  
Edmour F. Blouin ◽  
...  
Keyword(s):  
Stress Response ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Molecular Interactions ◽  
Genetic Traits ◽  
Natural Vector ◽  
Stress Response Proteins ◽  
Shock Proteins

Ticks are ectoparasites of animals and humans that serve as vectors of Anaplasma and other pathogens that affect humans and animals worldwide. Ticks and the pathogens that they transmit have coevolved molecular interactions involving genetic traits of both the tick and the pathogen that mediate their development and survival. In this paper, the expression of heat shock proteins (HSPs) and other stress response proteins (SRPs) was characterized in ticks and cultured tick cells by proteomics and transcriptomics analyses in response to Anaplasma spp. infection and heat shock. The results of these studies demonstrated that the stress response was activated in ticks and cultured tick cells after Anaplasma spp. infection and heat shock. However, in the natural vector-pathogen relationship, HSPs and other SRPs were not strongly activated, which likely resulted from tick-pathogen coevolution. These results also demonstrated pathogen- and tick-specific differences in the expression of HSPs and other SRPs in ticks and cultured tick cells infected with Anaplasma spp. and suggested the existence of post-transcriptional mechanisms induced by Anaplasma spp. to control tick response to infection. These results illustrated the complexity of the stress response in ticks and suggested a function for the HSPs and other SRPs during Anaplasma spp. infection.

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