scholarly journals 75-kDa glucose-regulated protein (GRP75) is a novel molecular signature for heat stress response in avian species

2020 ◽  
Vol 318 (2) ◽  
pp. C289-C303 ◽  
Author(s):  
Ahmed Edan Dhamad ◽  
Elizabeth Greene ◽  
Marites Sales ◽  
Phuong Nguyen ◽  
Lesleigh Beer ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Cell Viability ◽  
Stress Responses ◽  
3D Structure ◽  
Avian Species ◽  
Molecular Signature ◽  
Hsp70 Family ◽  
Avian Cell ◽  
Glucose Regulated Protein

Glucose-regulated protein 75 (GRP75) was first characterized in mammals as a heat shock protein-70 (HSP70) family stress chaperone based on its sequence homology. Extensive studies in mammals showed that GRP75 is induced by various stressors such as glucose deprivation, oxidative stress, and hypoxia, although it remained unresponsive to the heat shock. Such investigations are scarce in avian (nonmammalian) species. We here identified chicken GRP75 by using immunoprecipitation assay integrated with LC-MS/MS, and found that its amino acid sequence is conserved with high homology (52.5%) to the HSP70 family. Bioinformatics and 3D-structure prediction indicate that, like most HSPs, chicken GRP75 has two principal domains (the NH2-terminal ATPase and COOH-terminal region). Immunofluorescence staining shows that GRP75 is localized predominantly in the avian myoblast and hepatocyte mitochondria. Heat stress exposure upregulates GRP75 expression in a species-, genotype-, and tissue-specific manner. Overexpression of GRP75 reduces avian cell viability, and blockade of GRP75 by its small molecular inhibitor MKT-077 rescues avian cell viability during heat stress. Taken together, this is the first evidence showing that chicken GRP75, unlike its mammalian ortholog, is responsive to heat shock and plays a key role in cell survival/death pathways. Since modern avian species have high metabolic rates and are sensitive to high environmental temperature, GRP75 could open new vistas in mechanistic understanding of heat stress responses and thermotolerance in avian species.

scholarly journals Cold and Heat Stress Diversely Alters Both Cauliflower Respiration and Distinct Mitochondrial Proteins Including OXPHOS Components and Matrix Enzymes

2018 ◽  
Author(s):  
Michał Rurek ◽  
Magdalena Czołpińska ◽  
Tomasz Andrzej Pawłowski ◽  
Włodzimierz Krzesiński ◽  
Tomasz Spiżewski
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Stress Responses ◽  
Protein Import ◽  
Plant Mitochondria ◽  
Complex Model ◽  
Mitochondrial Proteome ◽  
Metabolism Enzymes ◽  
Shock Proteins

Complex proteomic and physiological approaches to study cold and heat stress responses in plant mitochondria are still limited. Variations in the mitochondrial proteome of cauliflower (Brassica oleracea var. botrytis) curds after cold and heat and after stress recovery were assayed by 2D PAGE in relation to respiratory parameters. Quantitative analysis of the mitochondrial proteome revealed numerous stress-affected protein spots. In cold alternative oxidase isoforms were extensively upregulated; major downregulations in the level of photorespiratory enzymes, porine isoforms, oxidative phosphorylation (OXPHOS) and some low-abundant proteins were observed. On the contrary, distinct proteins, including carbohydrate metabolism enzymes, heat-shock proteins, translation, protein import, and OXPHOS components were involved in heat response and recovery. Few metabolic regulations were suggested. Cauliflower plants appeared less susceptible to heat; closed stomata in heat stress resulted in moderate photosynthetic, but only minor respiratory impairments, however photosystem II performance was unaffected. Decreased photorespiration corresponded with proteomic alterations in cold. Our results show that cold and heat stress not only operate in diverse mode (exemplified by cold-specific accumulation of some heat shock proteins), but exert some associations on molecular and physiological levels. This implies more complex model of action of investigated stresses on plant mitochondria.

Identification and characterisation of heat shock protein gene (HSP70) family and its expression in Agave sisalana under heat stress

2019 ◽  
Vol 95 (4) ◽  
pp. 470-482
Author(s):  
Anicet Agossa Batcho ◽  
Muhammad Bilal Sarwar ◽  
Leeza Tariq ◽  
Bushra Rashid ◽  
Sameera Hassan ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Gene ◽  
Heat Shock Protein Gene ◽  
Hsp70 Family ◽  
Agave Sisalana

scholarly journals The heat shock protein family gene Hspa1l in male mice is dispensable for fertility

PeerJ ◽  
2020 ◽  
Vol 8 ◽  
pp. e8702 ◽  
Author(s):  
Xin Wang ◽  
Wenxiu Xie ◽  
Yejin Yao ◽  
Yunfei Zhu ◽  
Jianli Zhou ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Responses ◽  
Sperm Count ◽  
Protein Family ◽  
Apoptotic Cells ◽  
Significant Difference ◽  
Family Gene ◽  
Conserved Gene

Background Heat shock protein family A member 1 like (Hspa1l) is a member of the 70kD heat shock protein (Hsp70) family. HSPA1L is an ancient, evolutionarily conserved gene with a highly conserved domain structure. The gene is highly abundant and constitutively expressed in the mice testes. However, the role of Hspa1l in the testes has still not been elucidated. Methods Hspa1l-mutant mice were generated using the CRISPR/Cas9 system. Histological and immunofluorescence staining were used to analyze the phenotypes of testis and epididymis. Apoptotic cells were detected through TUNEL assays. Fertility and sperm motilities were also tested. Quantitative RT-PCR was used for analyzing of candidate genes expression. Heat treatment was used to induce heat stress of the testis. Results We successfully generated Hspa1l knockout mice. Hspa1l-/- mice exhibited normal development and fertility. Further, Hspa1l-/- mice shown no significant difference in spermatogenesis, the number of apoptotic cells in testes epididymal histology, sperm count and sperm motility from Hspa1l+/+ mice. Moreover, heat stress does not exacerbate the cell apoptosis in Hspa1l-/- testes. These results revealed that HSPA1L is not essential for physiological spermatogenesis, nor is it involved in heat-induced stress responses, which provides a basis for further studies.

Heat acclimation increases the basal HSP72 level and alters its production dynamics during heat stress

1999 ◽  
Vol 276 (5) ◽  
pp. R1506-R1515 ◽  
Author(s):  
Alina Maloyan ◽  
Aaron Palmon ◽  
Michal Horowitz
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Mrna Level ◽  
Heat Acclimation ◽  
Heat Strain ◽  
Continuous Exposure ◽  
Hsp70 Family ◽  
Before And After ◽  
Gene Transcripts

It has been previously shown that heat acclimation leads to an elevated basal level of 72-kDa heat shock protein (HSP72). Augmented expression of HSP72 is considered as a cytoprotective response. This led us to hypothesize that alterations in the heat shock protein (HSP) defense pathway are an integral part of the heat acclimation repertoire. To investigate this, we studied the temporal profile of basal HSP expression upon acclimation and the dynamics of their accumulation subsequent to acute heat stress (HS). In parallel, HSP72 mRNA level before and after HS was measured. For comparison, HSC mRNA [the constitutive member of 70-kDa HSP (HSP70) family] was measured in similar conditions. Heat acclimation was attained by continuous exposure of rats to 34°C for 0, 1, 2, and 30 days. HS was attained by exposure to 41 or 43°C for 2 h. Thermoregulatory capacity of the rats was defined by rectal temperature, heating rate, and the cumulative heat strain invoked during HS. HSP72 and HSP70 gene transcripts were measured in the left ventricle of the heart by means of Western immunoblotting and semiquantitative RT-PCR, respectively. The resultant acclimatory change comprised a higher resting level of the encoded 72-kDa protein (Δ175%, P < 0.0001). After HS, peak HSP72 mRNA level was attained, 40 and 20 min post-HS at 41 and 43°C, respectively, vs. 60 and 40 min in the nonacclimated group. The subsequent HSP synthesis, however, was dependent on the severity of the cumulative heat strain. At the initial phase of heat acclimation, augmented HSP72 transcription unaccompanied by HSP synthesis was observed. It is concluded that upon heat acclimation, the HSP defense pathway is predisposed to a faster response. At the initial phases of heat acclimation, inability to elevate the HSP cytosolic level rules out their direct cytoprotective role.

scholarly journals Persistent Borna Disease Virus Infection Confers Instability of HSP70 mRNA in Glial Cells during Heat Stress

2005 ◽  
Vol 79 (4) ◽  
pp. 2033-2041 ◽  
Author(s):  
Makiko Yamashita ◽  
Wataru Kamitani ◽  
Hideyuki Yanai ◽  
Naohiro Ohtaki ◽  
Yohei Watanabe ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Disease Virus ◽  
Glial Cells ◽  
Stress Responses ◽  
Borna Disease Virus ◽  
Hsp70 Mrna ◽  
Persistently Infected ◽  
Infected Cells ◽  
Borna Disease

ABSTRACT Borna disease virus (BDV) is a highly neurotropic RNA virus that causes neurological disorders in many vertebrate species. Although BDV readily establishes lasting persistence, persistently infected cells maintain an apparently normal cell phenotype in terms of morphology, viability, and proliferation. In this study, to understand the regulation of stress responses in BDV infection, we investigated the expression of heat shock proteins (HSPs) in glial cells persistently infected with BDV. Interestingly, we found that BDV persistence did not upregulate HSP70 expression even in cells treated with heat stress. Furthermore, BDV-infected glial cells exhibited rapid rounding and detachment from the culture plate under various stressful conditions. Immunofluorescence analysis demonstrated that heat stress rapidly disrupts the cell cytoskeleton only in persistently infected cells, suggesting a lack of thermotolerance. Intriguingly, we found that although persistently infected glial cells expressed HSP70 mRNA after heat stress, its expression rapidly disappeared during the recovery period. These observations indicated that persistent BDV infection may affect the stability of HSP70 mRNA. Finally, we found that the double-stranded RNA-dependent protein kinase (PKR) is expressed at a constant level in persistently infected cells with or without heat shock. Considering the interrelationship between HSP70 and PKR production, our data suggest that BDV infection disturbs the cellular stress responses to abolish antiviral activities and maintain persistence.

scholarly journals Direct exposure to mild heat stress stimulates cell viability and heat shock protein expression in primary cultured broiler fibroblasts

2020 ◽  
Vol 25 (6) ◽  
pp. 1033-1043
Author(s):  
Sharif Hasan Siddiqui ◽  
Sivakumar Allur Subramaniyan ◽  
Darae Kang ◽  
Jinryong Park ◽  
Mousumee Khan ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Protein Expression ◽  
Cell Viability ◽  
Mild Heat ◽  
Direct Exposure ◽  
Heat Shock Protein Expression

Molecular cloning and characterization of genes encoding Pennisetum glaucum ascorbate peroxidase and heat-shock factor: Interlinking oxidative and heat-stress responses

2009 ◽  
Vol 166 (15) ◽  
pp. 1646-1659 ◽  
Author(s):  
Ramesha A. Reddy ◽  
Bhumesh Kumar ◽  
Palakolanu Sudhakar Reddy ◽  
Rabi N. Mishra ◽  
Srikrishna Mahanty ◽  
...  
Keyword(s):  
Heat Stress ◽  
Heat Shock ◽  
Molecular Cloning ◽  
Ascorbate Peroxidase ◽  
Stress Responses ◽  
Pennisetum Glaucum ◽  
Heat Shock Factor ◽  
Genes Encoding
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