Expression of heat shock protein genes Aaehsp26, Aaehsp83 and Aaehsc70 in response to thermal stress in Aedes aegypti larvae

2021 ◽  
Vol 30 (2) ◽  
pp. 233-241
Author(s):  
Hafisha Khatun Anee ◽  
Ashfaqul Muid Khandaker ◽  
Rowshan Ara Begum ◽  
Reza Md Shahjahan
Keyword(s):  
Climate Change ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Abiotic Factors ◽  
Shock Treatment ◽  
Heat Shock Treatment ◽  
Quantitative Real Time Pcr ◽  
Physiological Processes ◽  
Factors Influencing ◽  
Heat Shock Protein Genes

Climate change is responsible to a certain extent for the occurrence and spread of arboviral pathogens worldwide. Temperature is one of the crucial abiotic factors influencing the physiological processes of mosquitoes. Several genes of heat shock protein (AaeHsp26, AaeHsp83, and AaeHsc70) families are known to be expressed in mosquitoes, which aid in overcoming stress induced by elevated temperature. In this study, the relative expression of heat shock protein genes has been examined using Quantitative Real-time PCR (qPCR). The temperatures used for heat shock treatment were 27(control), 37, and 42°C for 1 hour heat shock period and applied to 3rd instar larvae. Significant up-regulation has been seen at 37, and 42°C. The highest expression level, about 82.43 fold, was reported for the AaeHsc70 gene at 42°C followed by 78.36 fold for AaeHsp26 at 37°C and 4.79 fold for AaeHsp83 at 42°C. The current study has shown that HSPs are important markers of stress and may function as critical proteins to protect and enhance the survival of Ae. aegypti larvae and pupae. Biological implications of these findings could impact the vector competencies Dhaka Univ. J. Biol. Sci. 30(2): 233-241, 2021 (July)

scholarly journals Characterization of the thermotolerant cell. II. Effects on the intracellular distribution of heat-shock protein 70, intermediate filaments, and small nuclear ribonucleoprotein complexes.

1988 ◽  
Vol 106 (4) ◽  
pp. 1117-1130 ◽  
Author(s):  
W J Welch ◽  
L A Mizzen
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Stress Proteins ◽  
Intracellular Distribution ◽  
Shock Treatment ◽  
Heat Shock Treatment ◽  
Ribonucleoprotein Complexes ◽  
Small Nuclear Ribonucleoprotein ◽  
Nuclear Ribonucleoprotein ◽  
In Cells

Here we further characterize a number of properties inherent to the thermotolerant cell. In the preceding paper, we showed that the acquisition of the thermotolerant state (by a prior induction of the heat-shock proteins) renders cells translationally tolerant to a subsequent severe heat-shock treatment and thereby results in faster kinetics of both the synthesis and subsequent repression of the stress proteins. Because of the apparent integral role of the 70-kD stress proteins in the acquisition of tolerance, we compared the intracellular distribution of these proteins in both tolerant and nontolerant cells before and after a severe 45 degrees C/30-min shock. In both HeLa and rat embryo fibroblasts, the synthesis and migration of the major stress-induced 72-kD protein into the nucleolus and its subsequent exit was markedly faster in the tolerant cells as compared with the nontolerant cells. Migration of preexisting 72-kD into the nucleolus was shown to be dependent upon heat-shock treatment and independent of active heat-shock protein synthesis. Using both microinjection and immunological techniques, we observed that the constitutive and abundant 73-kD stress protein similarly showed a redistribution from the cytoplasm and nucleus into the nucleolus as a function of heat-shock treatment. We show also that other lesions that occur in cells after heat shock can be prevented or at least minimized if the cells are first made tolerant. Specifically, the heat-induced collapse of the intermediate filament cytoskeleton did not occur in cells rendered thermotolerant. Similarly, the disruption of intranuclear staining patterns of the small nuclear ribonucleoprotein complexes after heat-shock treatment was less apparent in tolerant cells exposed to a subsequent heat-shock treatment.

Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein

1988 ◽  
Vol 8 (12) ◽  
pp. 5059-5071
Author(s):  
A P Arrigo ◽  
J P Suhan ◽  
W J Welch
Keyword(s):  
Molecular Weight ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Elevated Temperatures ◽  
Shock Treatment ◽  
Low Molecular Weight ◽  
C Cells ◽  
Heat Shock Treatment ◽  
Soluble Phase ◽  
In Cells

Mammalian cells grown at 37 degrees C contain a single low-molecular-weight heat shock (or stress) protein with an apparent mass of 28 kilodaltons (kDa) whose synthesis increases in cells after exposure to elevated temperatures or other forms of physiologic stress. Herein we present data demonstrating that heat shock protein 28 exists in a number of dynamic states depending upon the physiologic state of the cell. Biochemical fractionation of 37 degrees C cells in the absence of nonionic detergent revealed that the 28-kDa protein partitioned approximately equally between the soluble and insoluble fractions. The addition of detergent in the fractionation procedure resulted in all of the protein distributed within the soluble phase. In contrast, in cells first heat shocked and then fractionated in the presence of detergent, most of the 28-kDa protein was found within the insoluble fraction. These biochemical results appeared entirely consistent with indirect immunofluorescence experiments, demonstrating that the 28-kDa protein resided within the perinuclear region of 37 degrees C cells in close proximity to the Golgi complex. After heat shock treatment, the 28-kDa protein relocalized within the nucleus and resisted detergent extraction. The extent of 28-kDa protein redistribution into the nucleus and its detergent insolubility increased as a function of the severity of the heat shock treatment. With time of recovery from the heat treatment there occurred a gradual return of the 28-kDa protein into the detergent-soluble phase. Concomitant with these changes in 28-kDa protein solubility was a corresponding change in the apparent size of the protein as determined by gel filtration. While at 37 degrees C cells the protein exhibited a mass of 200 to 800 kDa; after heat shock the protein assumed sizes of 2 MDa or greater. Using immunoelectron microscopy, we show an accumulation of these aggregates of 28-kDa protein within the nucleus. Finally, we show that the heat-dependent redistribution of the 28-kDa protein from the cytoplasm into the nucleus was greatly diminished when the cells were first rendered thermotolerant, and we suggest that this simple assay (i.e., 28-kDa protein detergent solubility) may prove useful in evaluating the thermotolerant status of a cell or tissue.

scholarly journals Dynamic changes in the structure and intracellular locale of the mammalian low-molecular-weight heat shock protein.

1988 ◽  
Vol 8 (12) ◽  
pp. 5059-5071 ◽  
Author(s):  
A P Arrigo ◽  
J P Suhan ◽  
W J Welch
Keyword(s):  
Molecular Weight ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Elevated Temperatures ◽  
Shock Treatment ◽  
Low Molecular Weight ◽  
C Cells ◽  
Heat Shock Treatment ◽  
Soluble Phase ◽  
In Cells

Mammalian cells grown at 37 degrees C contain a single low-molecular-weight heat shock (or stress) protein with an apparent mass of 28 kilodaltons (kDa) whose synthesis increases in cells after exposure to elevated temperatures or other forms of physiologic stress. Herein we present data demonstrating that heat shock protein 28 exists in a number of dynamic states depending upon the physiologic state of the cell. Biochemical fractionation of 37 degrees C cells in the absence of nonionic detergent revealed that the 28-kDa protein partitioned approximately equally between the soluble and insoluble fractions. The addition of detergent in the fractionation procedure resulted in all of the protein distributed within the soluble phase. In contrast, in cells first heat shocked and then fractionated in the presence of detergent, most of the 28-kDa protein was found within the insoluble fraction. These biochemical results appeared entirely consistent with indirect immunofluorescence experiments, demonstrating that the 28-kDa protein resided within the perinuclear region of 37 degrees C cells in close proximity to the Golgi complex. After heat shock treatment, the 28-kDa protein relocalized within the nucleus and resisted detergent extraction. The extent of 28-kDa protein redistribution into the nucleus and its detergent insolubility increased as a function of the severity of the heat shock treatment. With time of recovery from the heat treatment there occurred a gradual return of the 28-kDa protein into the detergent-soluble phase. Concomitant with these changes in 28-kDa protein solubility was a corresponding change in the apparent size of the protein as determined by gel filtration. While at 37 degrees C cells the protein exhibited a mass of 200 to 800 kDa; after heat shock the protein assumed sizes of 2 MDa or greater. Using immunoelectron microscopy, we show an accumulation of these aggregates of 28-kDa protein within the nucleus. Finally, we show that the heat-dependent redistribution of the 28-kDa protein from the cytoplasm into the nucleus was greatly diminished when the cells were first rendered thermotolerant, and we suggest that this simple assay (i.e., 28-kDa protein detergent solubility) may prove useful in evaluating the thermotolerant status of a cell or tissue.

Heat-induced triploids in Brycon amazonicus: a strategic fish species for aquaculture and conservation

Zygote ◽  
2021 ◽  
pp. 1-5
Author(s):  
Nivaldo Ferreira do Nascimento ◽  
Rafaela Manchin Bertolini ◽  
Lucia Soares Lopez ◽  
Laura Satiko Okada Nakaghi ◽  
Paulo Sérgio Monzani ◽  
...  
Keyword(s):  
Flow Cytometry ◽  
Heat Shock ◽  
Early Development ◽  
Fish Species ◽  
Survival Rates ◽  
Shock Treatment ◽  
Hatching Rate ◽  
Heat Shock Treatment ◽  
Control Survival ◽  
Ploidy Status

Summary Triploidization plays an important role in aquaculture and surrogate technologies. In this study, we induced triploidy in the matrinxã fish (Brycon amazonicus) using a heat-shock technique. Embryos at 2 min post fertilization (mpf) were heat shocked at 38°C, 40°C, or 42°C for 2 min. Untreated, intact embryos were used as a control. Survival rates during early development were monitored and ploidy status was confirmed using flow cytometry and nuclear diameter analysis of erythrocytes. The hatching rate reduced with heat-shock treatment, and heat-shock treatments at 42°C resulted in no hatching events. Optimal results were obtained at 40°C with 95% of larvae exhibiting triploidy. Therefore, we report that heat-shock treatments of embryos (2 mpf) at 40°C for 2 min is an effective way to induce triploid individuals in B. amazonicus.

scholarly journals Characterization of the thermotolerant cell. I. Effects on protein synthesis activity and the regulation of heat-shock protein 70 expression.

1988 ◽  
Vol 106 (4) ◽  
pp. 1105-1116 ◽  
Author(s):  
L A Mizzen ◽  
W J Welch
Keyword(s):  
Protein Synthesis ◽  
Heat Shock ◽  
Stress Proteins ◽  
Stress Protein ◽  
Shock Treatment ◽  
Heat Shock Treatment ◽  
Normal Medium ◽  
Growth Environment ◽  
Mammalian Cell Lines ◽  
C 30

Exposure of mammalian cells to a nonlethal heat-shock treatment, followed by a recovery period at 37 degrees C, results in increased cell survival after a subsequent and otherwise lethal heat-shock treatment. Here we characterize this phenomenon, termed acquired thermotolerance, at the level of translation. In a number of different mammalian cell lines given a severe 45 degrees C/30-min shock and then returned to 37 degrees C, protein synthesis was completely inhibited for as long as 5 h. Upon resumption of translational activity, there was a marked induction of heat-shock (or stress) protein synthesis, which continued for several hours. In contrast, cells first made thermotolerant (by a pretreatment consisting of a 43 degrees C/1.5-h shock and further recovery at 37 degrees C) and then presented with the 45 degrees C/30-min shock exhibited considerably less translational inhibition and an overall reduction in the amount of subsequent stress protein synthesis. The acquisition and duration of such "translational tolerance" was correlated with the expression, accumulation, and relative half-lives of the major stress proteins of 72 and 73 kD. Other agents that induce the synthesis of the stress proteins, such as sodium arsenite, similarly resulted in the acquisition of translational tolerance. The probable role of the stress proteins in the acquisition of translational tolerance was further indicated by the inability of the amino acid analogue, L-azetidine 2-carboxylic acid, an inducer of nonfunctional stress proteins, to render cells translationally tolerant. If, however, analogue-treated cells were allowed to recover in normal medium, and hence produce functional stress proteins, full translational tolerance was observed. Finally, we present data indicating that the 72- and 73-kD stress proteins, in contrast to the other major stress proteins (of 110, 90, and 28 kD), are subject to strict regulation in the stressed cell. Quantitation of 72- and 73-kD synthesis after heat-shock treatment under a number of conditions revealed that "titration" of 72/73-kD synthesis in response to stress may represent a mechanism by which the cell monitors its local growth environment.

scholarly journals DNA damage and heat shock dually regulate genes in Saccharomyces cerevisiae.

1986 ◽  
Vol 6 (1) ◽  
pp. 90-96 ◽  
Author(s):  
T McClanahan ◽  
K McEntee
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Dna Damage ◽  
Heat Shock ◽  
Shock Treatment ◽  
Northern Hybridization ◽  
Heat Shock Treatment ◽  
Base Pairs ◽  
S1 Nuclease ◽  
Hsp70 Family ◽  
Transcriptional Start Sites

Two Saccharomyces cerevisiae genes isolated in a differential hybridization screening for DNA damage regulation (DDR genes) were also transcriptionally regulated by heat shock treatment. A 0.45-kilobase transcript homologous to the DDRA2 gene and a 1.25-kilobase transcript homologous to the DDR48 gene accumulated after exposure of cells to 4-nitroquinoline-1-oxide (NQO; 1 to 1.5 microgram/ml) or brief heat shock (20 min at 37 degrees C). The DDRA2 transcript, which was undetectable in untreated cells, was induced to high levels by these treatments, and the DDR48 transcript increased more than 10-fold as demonstrated by Northern hybridization analysis. Two findings argue that dual regulation of stress-responsive genes is not common in S. cerevisiae. First, two members of the heat shock-inducible hsp70 family of S. cerevisiae, YG100 and YG102, were not induced by exposure to NQO. Second, at least one other DNA-damage-inducible gene, DIN1, was not regulated by heat shock treatment. We examined the structure of the induced RNA homologous to DDRA2 after heat shock and NQO treatments by S1 nuclease protection experiments. Our results demonstrated that the DDRA2 transcript initiates equally frequently at two sites separated by 5 base pairs. Both transcriptional start sites were utilized when cells were exposed to either NQO or heat shock treatment. These results indicate that DDRA2 and DDR48 are members of a unique dually regulated stress-responsive family of genes in S. cerevisiae.

scholarly journals Perturbation of chromatin architecture on ecdysterone induction of Drosophila melanogaster small heat shock protein genes.

1989 ◽  
Vol 9 (1) ◽  
pp. 332-335 ◽  
Author(s):  
S E Kelly ◽  
I L Cartwright
Keyword(s):  
Drosophila Melanogaster ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Intergenic Region ◽  
Small Heat Shock Protein ◽  
Dnase I ◽  
Developmentally Regulated ◽  
Regulatory Interactions ◽  
Chromatin Architecture ◽  
Heat Shock Protein Genes

Alterations in the pattern of DNase I hypersensitivity were observed on ecdysterone-stimulated transcription of Drosophila melanogaster small heat shock protein genes. Perturbations were induced near hsp27 and hsp22, coupled with an extensive domain of chromatin unfolding in the intergenic region between hsp23 and the developmentally regulated gene 1. These regions represent candidates for ecdysterone regulatory interactions.

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