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.

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 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.

scholarly journals Genome-wide identification of heat shock factors and heat shock proteins in response to UV and high intensity light stress in lettuce

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Taehoon Kim ◽  
Shafina Samraj ◽  
Juan Jiménez ◽  
Celina Gómez ◽  
Tie Liu ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Light Stress ◽  
Stress Conditions ◽  
Heat Shock Factors ◽  
Genome Wide Analysis ◽  
Genome Wide ◽  
Shock Proteins ◽  
High Intensity Light

Abstract Background Heat shock factors (Hsfs) and Heat shock proteins (Hsps) belong to an essential group of molecular regulators involved in controlling cellular processes under normal and stress conditions. The role of Hsfs and Hsps is well known in model plant species under diverse stress conditions. While plants Hsfs are vital components of the signal transduction response to maintain cellular homeostasis, Hsps function as chaperones helping to maintain folding of damaged and newly formed proteins during stress conditions. In lettuce (Lactuca sativa), a highly consumed vegetable crop grown in the field and in hydroponic systems, the role of these gene families in response to artificial light is not well characterized. Results Using a genome-wide analysis approach, we identified 32 Hsfs and 22 small heat shock proteins (LsHsps) in lettuce, some of which do not have orthologs in Arabidopsis, poplar, and rice. LsHsp60s, LsHsp90s, and LsHsp100s are highly conserved among dicot and monocot species. Surprisingly, LsHsp70s have three times more members than Arabidopsis and two times more than rice. Interestingly, the lettuce genome triplication did not contribute to the increased number of LsHsp70s genes. The large number of LsHsp70s was the result of genome tandem duplication. Chromosomal distribution analysis shows larger tandem repeats of LsHsp70s genes in Chr1, Chr7, Chr8, and Chr9. At the transcriptional level, some genes of the LsHsfs, LsHsps, LsHsp60s, and LsHsp70s families were highly responsive to UV and high intensity light stress, in contrast to LsHsp90s and LsHsp100s which did not respond to a light stimulus. Conclusions Our genome-wide analysis provides a detailed identification of Hsfs and Hsps in lettuce. Chromosomal location and syntenic region analysis together with our transcriptional analysis under different light conditions provide candidate genes for breeding programs aiming to produce lettuce varieties able to grow healthy under hydroponic systems that use artificial light.

scholarly journals Developmental Expression and Functions of the Small Heat Shock Proteins in Drosophila

2018 ◽  
Vol 19 (11) ◽  
pp. 3441 ◽  
Author(s):  
Teresa Jagla ◽  
Magda Dubińska-Magiera ◽  
Preethi Poovathumkadavil ◽  
Małgorzata Daczewska ◽  
Krzysztof Jagla
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Large Family ◽  
Active Role ◽  
Stress Conditions ◽  
Developmental Expression ◽  
Shsp Gene ◽  
Time Specific ◽  
Shock Proteins ◽  
And Function

Heat shock proteins (Hsps) form a large family of evolutionarily conserved molecular chaperones that help balance protein folding and protect cells from various stress conditions. However, there is growing evidence that Hsps may also play an active role in developmental processes. Here, we take the example of developmental expression and function of one class of Hsps characterized by low molecular weight, the small Hsps (sHsps). We discuss recent reports and genome-wide datasets that support vital sHsps functions in the developing nervous system, reproductive system, and muscles. This tissue- and time-specific sHsp expression is developmentally regulated, so that the enhancer sequence of an sHsp gene expressed in developing muscle, in addition to stress-inducible elements, also carries binding sites for myogenic regulatory factors. One possible reason for sHsp genes to switch on during development and in non-stress conditions is to protect vital developing organs from environmental insults.

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