scholarly journals Roles of Hsp70s in Stress Responses of Microorganisms, Plants, and Animals

2015 ◽  
Vol 2015 ◽  
pp. 1-8 ◽  
Author(s):  
Anmin Yu ◽  
Ping Li ◽  
Ting Tang ◽  
Jiancai Wang ◽  
Yuan Chen ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Heat Shock ◽  
Virus Infection ◽  
Heat Shock Protein ◽  
Stress Responses ◽  
Molecular Chaperones ◽  
Neurological Disorders ◽  
Response To Stress ◽  
Cellular Development ◽  
Living Organisms

Hsp70s (heat shock protein 70s) are a class of molecular chaperones that are highly conserved and ubiquitous in organisms ranging from microorganisms to plants and humans. Most research on Hsp70s has focused on the mechanisms of their functions as molecular chaperones, but recently, studies on stress responses are coming to the forefront. Hsp70s play key roles in cellular development and protecting living organisms from environmental stresses such as heat, drought, salinity, acidity, and cold. Moreover, functions of human Hsp70s are related to diseases including neurological disorders, cancer, and virus infection. In this review, we provide an overview of the specific roles of Hsp70s in response to stress, particularly abiotic stress, in all living organisms.

Sequence analysis of Ricinus communis small heat-shock protein (sHSP) subfamily and its role in abiotic stress responses

2020 ◽  
Vol 152 ◽  
pp. 112541 ◽  
Author(s):  
Valdir G. Neto ◽  
Rhaissa R. Barbosa ◽  
Maria G.A. Carosio ◽  
Antônio G. Ferreira ◽  
Luzimar G. Fernandez ◽  
...  
Keyword(s):  
Abiotic Stress ◽  
Sequence Analysis ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Responses ◽  
Ricinus Communis ◽  
Small Heat Shock Protein

scholarly journals Heat Shock Protein 90 as Therapeutic Target for CVDs and Heart Ageing

2022 ◽  
Vol 23 (2) ◽  
pp. 649
Author(s):  
Siarhei A. Dabravolski ◽  
Vasily N. Sukhorukov ◽  
Vladislav A. Kalmykov ◽  
Nikolay A. Orekhov ◽  
Andrey V. Grechko ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Molecular Chaperones ◽  
Heat Shock Protein 90 ◽  
Misfolded Proteins ◽  
Heart Cells ◽  
Metabolic Demand ◽  
Heart Protection ◽  
High Metabolic Demand

Cardiovascular diseases (CVDs) are the leading cause of death globally, representing approximately 32% of all deaths worldwide. Molecular chaperones are involved in heart protection against stresses and age-mediated accumulation of toxic misfolded proteins by regulation of the protein synthesis/degradation balance and refolding of misfolded proteins, thus supporting the high metabolic demand of the heart cells. Heat shock protein 90 (HSP90) is one of the main cardioprotective chaperones, represented by cytosolic HSP90a and HSP90b, mitochondrial TRAP1 and ER-localised Grp94 isoforms. Currently, the main way to study the functional role of HSPs is the application of HSP inhibitors, which could have a different way of action. In this review, we discussed the recently investigated role of HSP90 proteins in cardioprotection, atherosclerosis, CVDs development and the involvements of HSP90 clients in the activation of different molecular pathways and signalling mechanisms, related to heart ageing.

scholarly journals Anticancer Effects of LBA-ST Yogurt Supernatant on HeLa Cells via Heat Shock Protein 27 Decrease In Vitro

2017 ◽  
Vol 6 (1) ◽  
pp. 16
Author(s):  
Liziyyannida Liziyyannida ◽  
Wibi Riawan
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Short Chain Fatty Acids ◽  
Heat Shock Protein 27 ◽  
Lactobacillus Bulgaricus ◽  
Culture Cells ◽  
Response To Stress ◽  
And Migration

Heat Shock Protein 27 (Hsp27) is overexpressed in cervical cancer as a response to stress conditions. Hsp27 overexpression increase invasion, migration, and adhesion pathways of cancer cells. The Yogurt supernatant contains Short-Chain Fatty Acids (SCFA) include acetate, lactate, and butyrate which have anticancer activity. This study aimed to investigate supernatant of LBA-ST (Lactobacillusbulgaricus-acidophilus, Streptococcusthermophillus) Yogurt can decrease the expression of Hsp27 in HeLa culture cells. The mechanism on how supernatant yogurt inhibit invasion, migration, and adhesion was studied by immunocytochemistry. The data was then collected and analyzed using One-Way ANOVA. From this study, it can be concluded that the expression of proteins that play a role in invasion, adhesion, and migration of the Hsp27 was proven to be decreased (p< 0.05 ± 0.005).Keywords: HeLa cells, yogurt supernatant, Lactobacillus bulgaricus-acidophilus, Streptococcus thermophillus, Hsp27

scholarly journals Small Molecule Inhibitors Targeting the Heat Shock Protein System of Human Obligate Protozoan Parasites

2019 ◽  
Vol 20 (23) ◽  
pp. 5930 ◽  
Author(s):  
Zininga ◽  
Shonhai
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Small Molecule ◽  
Molecular Chaperones ◽  
Small Molecule Inhibitors ◽  
Protozoan Parasites ◽  
Obligate Intracellular ◽  
Human Host ◽  
Shock Proteins

Obligate protozoan parasites of the kinetoplastids and apicomplexa infect human cells to complete their life cycles. Some of the members of these groups of parasites develop in at least two systems, the human host and the insect vector. Survival under the varied physiological conditions associated with the human host and in the arthropod vectors requires the parasites to modulate their metabolic complement in order to meet the prevailing conditions. One of the key features of these parasites essential for their survival and host infectivity is timely expression of various proteins. Even more importantly is the need to keep their proteome functional by maintaining its functional capabilities in the wake of physiological changes and host immune responses. For this reason, molecular chaperones (also called heat shock proteins)—whose role is to facilitate proteostasis—play an important role in the survival of these parasites. Heat shock protein 90 (Hsp90) and Hsp70 are prominent molecular chaperones that are generally induced in response to physiological stress. Both Hsp90 and Hsp70 members are functionally regulated by nucleotides. In addition, Hsp70 and Hsp90 cooperate to facilitate folding of some key proteins implicated in cellular development. In addition, Hsp90 and Hsp70 individually interact with other accessory proteins (co-chaperones) that regulate their functions. The dependency of these proteins on nucleotide for their chaperone function presents an Achille’s heel, as inhibitors that mimic ATP are amongst potential therapeutic agents targeting their function in obligate intracellular human parasites. Most of the promising small molecule inhibitors of parasitic heat shock proteins are either antibiotics or anticancer agents, whose repurposing against parasitic infections holds prospects. Both cancer cells and obligate human parasites depend upon a robust protein quality control system to ensure their survival, and hence, both employ a competent heat shock machinery to this end. Furthermore, some inhibitors that target chaperone and co-chaperone networks also offer promising prospects as antiparasitic agents. The current review highlights the progress made so far in design and application of small molecule inhibitors against obligate intracellular human parasites of the kinetoplastida and apicomplexan kingdoms.

scholarly journals Heat Shock Protein Genes Undergo Dynamic Alteration in Their Three-Dimensional Structure and Genome Organization in Response to Thermal Stress

2017 ◽  
Vol 37 (24) ◽  
Author(s):  
Surabhi Chowdhary ◽  
Amoldeep S. Kainth ◽  
David S. Gross
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Rna Polymerase Ii ◽  
De Novo ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Chromosome Conformation ◽  
Coding Regions ◽  
Response To Stress

ABSTRACT Three-dimensional (3D) chromatin organization is important for proper gene regulation, yet how the genome is remodeled in response to stress is largely unknown. Here, we use a highly sensitive version of chromosome conformation capture in combination with fluorescence microscopy to investigate Heat Shock Protein (HSP) gene conformation and 3D nuclear organization in budding yeast. In response to acute thermal stress, HSP genes undergo intense intragenic folding interactions that go well beyond 5′-3′ gene looping previously described for RNA polymerase II genes. These interactions include looping between upstream activation sequence (UAS) and promoter elements, promoter and terminator regions, and regulatory and coding regions (gene “crumpling”). They are also dynamic, being prominent within 60 s, peaking within 2.5 min, and attenuating within 30 min, and correlate with HSP gene transcriptional activity. With similarly striking kinetics, activated HSP genes, both chromosomally linked and unlinked, coalesce into discrete intranuclear foci. Constitutively transcribed genes also loop and crumple yet fail to coalesce. Notably, a missense mutation in transcription factor TFIIB suppresses gene looping, yet neither crumpling nor HSP gene coalescence is affected. An inactivating promoter mutation, in contrast, obviates all three. Our results provide evidence for widespread, transcription-associated gene crumpling and demonstrate the de novo assembly and disassembly of HSP gene foci.

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