scholarly journals Heat shock proteins (HSP 90, 70, 60, and 27) in Galleria mellonella (Lepidoptera) hemolymph are affected by infection with Conidiobolus coronatus (Entomophthorales)

PLoS ONE ◽  
2020 ◽  
Vol 15 (2) ◽  
pp. e0228556 ◽  
Author(s):  
Anna Katarzyna Wrońska ◽  
Mieczysława Irena Boguś
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Galleria Mellonella ◽  
Conidiobolus Coronatus ◽  
Shock Proteins ◽  
Hsp 90

scholarly journals Consequences of Atrial or Ventricular Tachypacing on the Heat Shock Proteins (HSP) level of Expression and Phosphorylation

2020 ◽  
Vol 12 (2) ◽  
Author(s):  
Matthew Shorofsky ◽  
Ange Maguy ◽  
Stanley Nattel
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Canine Model ◽  
Right Atrial ◽  
Expression Levels ◽  
Significant Difference ◽  
Canine Models ◽  
Shock Proteins ◽  
Hsp 90

Background - Uncontrolled atrial fibrillation (AF) results in complex changes in the cardiomyocyte electrical and contractile functioning that promote atrial remodeling and the continuation of AF. Recently there has been a growing interest in understanding the role of heat shock proteins (HSPs), which are cytoprotective molecular chaperones, in the pathophysiology of AF. Several groups have examined HSP expression in patients with AF but have yielded mixed results. To allow for  better consistency and reproducibility between subjects, we utilized canine models to reproduce AF- promoting conditions to better investigate the role of HSPs in the pathophysiology of AF. Methods - AF  promoting conditions were simulated in canine models with fifteen adult mongrel dogs (20.6 to 36.0 kg) divided into three groups: (1) Control (n=5), (2) two week ventricular tachypacing (VTP) induced congestive heart failure (CHF) (n=5), and (3) one week atrial tachypacying (ATP) (n=5). Quick frozen right atrial free wall tissue samples were used for protein isolation and were analyzed via Western  blotting with data was expressed as a relative ratio and were analyzed using a two-tailed, unpaired t- test and significance was set at p < 0.05. The expression levels of HSP 90, 70, and 25 were studied along  with the phosphorylation status of HSP27 at serine-78. Results - We first examined the effects of the ATP and CHF heart models on the expression of a select group of HSPs via Western Blot. We found that there was no significant difference in levels of expression of HSP 90, 70, or 25 when either ATP or CHF models were compared to control canines. The phosphorylation status of HSP27 was significantly decreased in the CHF canine model when compared to control (p < 0.0111) and it tended towards a decrease in the ATP canine model when compared to control (p=0.0923). Conclusion - This study showed that even though the expression levels of HSPs may remain constant, there are protein phosphorylation and dephosphorylation events that occur in AF that may have important consequences in its pathophysiology. It is therefore necessary to investigate the full scale of HSP modifications during AF and AF-promoting conditions.

Heat Shock Response in the Thermophilic Enteric Yeast Arxiozyma telluris

1998 ◽  
Vol 64 (8) ◽  
pp. 3063-3065 ◽  
Author(s):  
Michelle L. Deegenaars ◽  
Kenneth Watson
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Response ◽  
Ecological Niche ◽  
Hsp 70 ◽  
Shock Response ◽  
Heat Stress Tolerance ◽  
Shock Proteins ◽  
Hsp 90

ABSTRACT Heat stress tolerance was examined in the thermophilic enteric yeast Arxiozyma telluris. Heat shock acquisition of thermotolerance and synthesis of heat shock proteins hsp 104, hsp 90, hsp 70, and hsp 60 were induced by a mild heat shock at temperatures from 35 to 40°C for 30 min. The results demonstrate that a yeast which occupies a specialized ecological niche exhibits a typical heat shock response.

scholarly journals Pemodelan Farmakofor untuk Identifikasi Inhibitor Heat Shock Proteins-90 (HSP-90)

2020 ◽  
Author(s):  
Muhammad Arba
Keyword(s):  
Hydrogen Bond ◽  
Molecular Docking ◽  
Heat Shock ◽  
Binding Energy ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Operating Characteristics ◽  
Hydrogen Bond Donor ◽  
Shock Proteins ◽  
Hsp 90

Heat shock proteins-90 (HSP-90) is a protein that plays an important role in the life cycle of normal and cancer cells for their self protection from thermal stress, oxidative damage, and cell hypoxia. Inhibition of HSP90 is one way to suppress the growth of cancer cells. In this study, pharmacophore modeling and molecular docking were conducted to identify hit compounds as inhibitors of HSP-90. The pharmacophore feature consists of three hydrogen bond acceptors, one hydrogen bond donor and one hydrophobic feature with Area Under Curve of Receiver Operating Characteristics (AUC-ROC) is 0.5 and the Goodness of Hit (GH) value is 0.752. Screening in the ZINC database generated 1,500 hit compounds, were subjected to molecular docking to determine their binding energy and interactions with HSP-90. The range of binding energy (E) of all hit compounds is -5.68 to -12.24 kcal/mol and there are four best hit compounds namely lig_543, lig_527, lig_1337 and lig_337, when compared to native ligands (PU2, E=-8.25 kkal/mol) based on the binding energy and orientation, which indicate their potential as new HSP-90 inhibitors.

scholarly journals Pemodelan Farmakofor untuk Identifikasi Inhibitor Heat Shock Proteins-90 (HSP-90)

2020 ◽  
Vol 6 (2) ◽  
Author(s):  
Muhammad Arba ◽  
Arfan ◽  
Ayu Trisnawati ◽  
Desi Kurniawati
Keyword(s):  
Hydrogen Bond ◽  
Molecular Docking ◽  
Heat Shock ◽  
Binding Energy ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Operating Characteristics ◽  
Hydrogen Bond Donor ◽  
Shock Proteins ◽  
Hsp 90

Heat shock proteins-90 (HSP-90) is a protein that plays an important role in the life cycle of normal and cancer cells for their self protection from thermal stress, oxidative damage, and cell hypoxia. Inhibition of HSP90 is one way to suppress the growth of cancer cells. In this study, pharmacophore modeling and molecular docking were conducted to identify hit compounds as inhibitors of HSP-90. The pharmacophore feature consists of three hydrogen bond acceptors, one hydrogen bond donor and one hydrophobic feature with Area Under Curve of Receiver Operating Characteristics (AUCROC) is 0.5 and the Goodness of Hit (GH) value is 0.752. Screening in the ZINC database generated 1,500 hit compounds, were subjected to molecular docking to determine their binding energy and interactions with HSP-90. The range of binding energy (E) of all hit compounds is -5.68 to -12.24 kcal/mol and there are four best hit compounds namely lig_543, lig_527, lig_1337 and lig_337, when compared to native ligands (PU2, E=-8.25 kkal/mol) based on the binding energy and orientation, which indicate their potential as new HSP-90 inhibitors.     

Synthesis of heat-shock proteins HSP-70 and HSP-90 in flowers of common buckwheat (Fagopyrum esculentum) under thermal stress

2020 ◽  
Vol 71 (8) ◽  
pp. 760 ◽  
Author(s):  
A. Płażek ◽  
K. Hura ◽  
T. Hura ◽  
A. Słomka ◽  
M. Hornyák ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Photochemical Efficiency ◽  
Fagopyrum Esculentum ◽  
Common Buckwheat ◽  
Hsp 70 ◽  
Flower Bud ◽  
Shock Proteins ◽  
Hsp 90

Common buckwheat (Fagopyrum esculentum Moench) is a valuable crop plant with cereal-like seed chemical composition; however, it is susceptible to thermal stress. The aim of the study was to determine whether heat-shock proteins HSP-90 and HSP-70 can protect common buckwheat against thermal stress during development of microspores and embryo sacs. The study was performed on two accessions of common buckwheat, Panda and PA15, which differed in their tolerance to thermal stress. Accumulation of these proteins was determined in buds, open and wilted flowers, and donor leaves of plants grown at 20°C (control) and 30°C (thermal stress). Photochemical efficiency of donor leaves, closest to the inflorescences, based on chlorophyll a fluorescence (ChlF) was also analysed. All plants demonstrated higher values of ChlF at 30°C than at 20°C, which suggests that this 30°C temperature is more conducive to their vegetative growth. Pollen grains of both accessions demonstrated normal development at 30°C, whereas embryo sacs showed many developmental disturbances. Panda was more sensitive to thermal stress than PA15, as manifested in a higher percentage of degenerated embryo sacs at the flower bud phase. Moreover, a decrease in both HSPs in the studied organs of Panda was found relative to the control. At 30°C, both accessions accumulated more HSP-70 than HSP-90. These results suggest that, under heat stress, HSP-70 plays a protective role for flowers of common buckwheat. The analyses indicated that the donor leaf closest to the flower cluster may be a reliable indicator of temperature sensitivity in buckwheat flowers.

Expression and Prognostic Examination of Heat Shock Proteins (HSP 27, HSP 70, and HSP 90) in Medulloblastoma

2006 ◽  
Vol 28 (7) ◽  
pp. 461-466 ◽  
Author(s):  
P??ter Hauser ◽  
Zolt??n Hanz??ly ◽  
Zsuzsanna Jakab ◽  
L??szl??n?? Ol??h ◽  
Erika Szab?? ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Hsp 70 ◽  
Hsp 27 ◽  
Shock Proteins ◽  
Hsp 90

scholarly journals Mitogen activation induces the enhanced synthesis of two heat-shock proteins in human lymphocytes.

1988 ◽  
Vol 106 (3) ◽  
pp. 883-891 ◽  
Author(s):  
R N Haire ◽  
M S Peterson ◽  
J J O'Leary
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Culture Media ◽  
Human Peripheral Blood ◽  
Polyclonal Antibodies ◽  
Human Lymphocytes ◽  
Hsc 70 ◽  
Shock Proteins ◽  
Hsp 90

We have used mitogenic lectin (PHA) and a monoclonal antibody (OKT3) to stimulate human peripheral blood (G0) lymphocytes, in the presence of monocytes, and have found two major preferentially synthesized proteins, 73 and 95 kD, which are induced by the mitogens. The elevated synthesis of both proteins begins approximately 4-6 h after mitogen addition (early to mid G0/G1) before entry into first S phase. Maximum synthesis of both proteins is reached by 12 h after mitogen addition when P95 synthesis represents approximately 4%, and P73 approximately 2%, of the total protein synthesis, compared with less than 0.5% for each protein in cells cultured without mitogen. Thus, the proteins appear to be major components of activated cells. We find that both P73 and P95 are induced by heat stress as well as mitogenic stimulation. The induction of the proteins is not affected by either deleting glucose from the culture media or, alternatively, by supplementing it. Using polyclonal antibodies prepared to each of the proteins isolated from mitogen activated cells and monoclonal antibodies that were raised to heat shock proteins, we are able to show that P95 is electrophoretically and immunologically identical to the HSP 90 induced by heat stress. P73 is one of the 70 kD HSPs, (termed HSC 70; Pelham, H. R. B. 1986. Cell. 46: 959-961), but is different from the most strongly heat inducible form of HSP 70 (72 kD). The distribution of both proteins in subcellular fractions of mitogen activated lymphocytes is similar to the reported localization of the respective HSP's in other cell types. The results suggest that HSP 90 and HSC 70 may have functional roles in stress response and growth processes of human lymphocytes.

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