Adaptive stabilization of structures and adaptive protection of the heart in rats of two different genetic strains: Role of heat-shock proteins hsp 70

1994 ◽  
Vol 118 (2) ◽  
pp. 812-815
Author(s):  
E. V. Malysheva ◽  
A. V. Zamotrinskii ◽  
I. Yu. Malyshev
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Adaptive Stabilization ◽  
Hsp 70 ◽  
Adaptive Protection ◽  
Genetic Strains ◽  
Shock Proteins

The role of heat-shock proteins in thermotolerance

1993 ◽  
Vol 339 (1289) ◽  
pp. 279-286 ◽  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
High Temperatures ◽  
Fruit Fly ◽  
Yeast Cells ◽  
Major Protein ◽  
Wild Type ◽  
Hsp 70 ◽  
Shock Proteins

The role of heat-shock proteins (hsps) in thermotolerance was examined in the budding yeast Saccharomyces cerevisiae and in the fruit fly Drosophila melanogaster . In yeast cells, the major protein responsible for thermotolerance is hsp 100. In cells carrying mutations in the hsp 100 gene, HSP 104 , growth is normal at both high and low temperatures, but the ability of cells to survive extreme temperatures is severely impaired. The loss of thermotolerance is apparently due to the absence of the hsp 104 protein itself because, with the exception of the hsp 104 protein, no differences in protein profiles were observed between mutant and wild-type cells. Aggregates found in mutant cells at high temperatures suggest that the cause of death may be the accumulation of denatured proteins. No differences in the rates of protein degradation were observed between mutant and wild-type cells. This, and genetic analysis of cells carrying multiple hsp 70 and hsp 104 mutations, suggests that the primary function of hsp 104 is to rescue proteins from denaturation rather than to degrade them once they have been denatured. Drosophila cells do not produce a protein in the hsp 100 class in response to high temperatures. In this organism, hsp 70 appears to be the primary protein involved in thermotolerance. Thus, the relative importance of different hsps in thermotolerance changes from organism to organism.

scholarly journals Role of heat-shock proteins and cobalamine in maintaining methionine synthase activity.

2012 ◽  
Vol 59 (4) ◽  
Author(s):  
Michał Grabowski ◽  
Rafał Banasiuk ◽  
Alicja Węgrzyn ◽  
Barbara Kędzierska ◽  
Jan Lica ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Conditions ◽  
Methionine Synthase ◽  
Atheromatous Plaque ◽  
Hsp 70 ◽  
Functional Relations ◽  
Shock Proteins

Atheromatous plaque is one of the most common cardiovascular-related diseases. Reports show a connection between its development and the levels of homocysteine. In pathological states high levels of homocysteine in the organism can be caused by the malfunction of the methionine synthase pathway. Bacterial methionine synthase (MetH) is a homologue of the human methionine syntase (MS). In this study we aimed to investigate the functional relations between MetH and its cofactor--cobalamine--under stress conditions. We have demonstrated that heat shock proteins (Hsp 70/100 system or HtpG) can protect MetH activity under stress conditions. Moreover, in the presence of cobalamine they can restore the activity of partially denatured methionine synthase.

scholarly journals Diagnostic value of chaperone activity of heat shock proteins 70 in coronary atherosclerosis

2019 ◽  
Vol 10 (3) ◽  
pp. 60-64
Author(s):  
Julia A. Kotova ◽  
Anna A. Zuikova ◽  
Alexander N. Pashkov
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Coronary Atherosclerosis ◽  
Negative Relationship ◽  
Diagnostic Value ◽  
Chaperone Activity ◽  
Hsp 70 ◽  
Significant Negative Relationship ◽  
Shock Proteins

Aim. The aim of the research was to study the role of chaperone activity heat shock proteins (HSP) 70 in pathogenesis and diagnostic in patients with coronary atherosclerosis. Materials and methods. We examined 354 patients with coronary heart disease, who had coronary atherosclerosis of varying degrees, according to coronary angiography (was performed by the Judkins technique). The severity of coronary atherosclerosis was determined on the basis of the Gensini index. According to the Gensini index, patients were divided into 2 groups: GS0 - 152 patients without signs of coronary atherosclerosis, GS1 - 202 patients with coronary lesions. Chaperone activity was determined by thermodynamic method. Results. The study showed significant differences in the level of chaperone activity HSP70 in patients with different severity of coronary atherosclerosis. The correlation analysis revealed a significant negative relationship between chaperone activity HSP70 and the Gensini index. The cut-off value of chaperone activity of HSP70, by which can be judged on the presence or absence of coronary atherosclerosis, is establish. Conclusion. The revealed threshold of chaperone activity can be considered as a possible marker of the severity of coronary atherosclerosis.

The role of heat shock proteins in ER export mechanisms of the human serotonin transporter

2013 ◽  
Vol 1 (Suppl. 1) ◽  
pp. A3.17
Author(s):  
Ali El-Kasaby
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Serotonin Transporter ◽  
Shock Proteins ◽  
Er Export

Regulatory Role of Heat Shock Proteins in the Pathogenesis of Type 1 and Type 2 Diabetes

2017 ◽  
Vol 13 (1) ◽  
Author(s):  
Christiane Habich ◽  
Henrike Sell ◽  
Volker Burkart
Keyword(s):  
Type 2 Diabetes ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Regulatory Role ◽  
Shock Proteins

ATPase inhibition by omeprazole reveals role of heat shock proteins on testicular torsion

Andrologia ◽  
2020 ◽  
Author(s):  
Cengiz Güney ◽  
Kübra Açıkalın Coşkun ◽  
Yusuf Tutar
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Testicular Torsion ◽  
Shock Proteins ◽  
Atpase Inhibition

Role of heat shock proteins in the formation of stress resistance in different animal strains

1994 ◽  
Vol 118 (1) ◽  
pp. 689-691 ◽  
Author(s):  
E. V. Malysheva ◽  
A. V. Zamotrinskii ◽  
I. Yu. Malyshev
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Resistance ◽  
Shock Proteins ◽  
Animal Strains

The Unique Role of Heat Shock Proteins in Infections

2020 ◽  
pp. 27-51
Author(s):  
Bernd Schoel ◽  
Stefan H. E. Kaufmann
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Unique Role ◽  
Shock Proteins
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