scholarly journals Heat shock proteins expression during thermal risk exposure in the temperate xerothermic ant Formica cinerea

Sociobiology ◽  
2015 ◽  
Vol 62 (3) ◽  
pp. 457 ◽  
Author(s):  
Piotr Ślipiński ◽  
Jan Jakub Pomorski ◽  
Katarzyna Kowalewska
Keyword(s):  
Heat Shock ◽  
Effect Of Temperature ◽  
Temperate Climate ◽  
Control Group ◽  
Abiotic Conditions ◽  
Hot Days ◽  
Desert Habitat ◽  
Thermal Risk ◽  
Shock Proteins ◽  
Formica Cinerea

The abiotic conditions of the desert habitat fluctuate in a circadian rhythm of hot days and cold nights. Species living in desert habitats evolved many adaptations to increase their chances of survival. However, abiotic conditions in xerothermic habitats of a temperate climate are much different. Diurnal fluctuations are not as strong, but animals have to cope with seasonal changes and hibernate during the winter, which may potentially influence their adaptations to critical temperature conditions. We attempted to assess heat resistance adaptations using the example of a widely distributed xerothermic ant Formica cinerea. Using Real-Time PCR, we measured the expression of three heat shock protein genes (Hsp60, Hsp75, Hsp90) and assessed the adaptations of F. cinerea to enable foraging in risk prone conditions. The analysis of gene expression using the Generalized Linear Model surprisingly indicated that there was no significant effect of temperature when comparing workers from the control (23ºC) with workers foraging on the surface of hot sand (47-54ºC). As a next step we tried to estimate the threshold of a thermal resistance with the use of thermal chambers. Expression of all Hsps genes increase compare to the control group, expression of Hsp60 and Hsp90 continued up to 45ºC.

Short-term exercise training can improve myocardial tolerance to I/R without elevation in heat shock proteins

2001 ◽  
Vol 281 (3) ◽  
pp. H1346-H1352 ◽  
Author(s):  
Karyn L. Hamilton ◽  
Scott K. Powers ◽  
Takao Sugiura ◽  
Sunjoo Kim ◽  
Shannon Lennon ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Ischemia Reperfusion ◽  
Left Ventricular ◽  
Antioxidant Defenses ◽  
Control Group ◽  
Shock Proteins ◽  
Mnsod Activity ◽  
Over Time

We examined the effects of 3 days of exercise in a cold environment on the expression of left ventricular (LV) heat shock proteins (HSPs) and contractile performance during in vivo ischemia-reperfusion (I/R). Sprague-Dawley rats were divided into the following three groups ( n = 12/group): 1) control, 2) exercise (60 min/day) at 4°C (E-Cold), and 3) exercise (60 min/day) at 25°C (E-Warm). Left anterior descending coronary occlusion was maintained for 20 min, followed by 30 min of reperfusion. Compared with the control group, both the E-Cold and E-Warm groups maintained higher ( P < 0.05) LV developed pressure, first derivative of pressure development over time (+dP/d t), and pressure relaxation over time (−dP/d t) throughout I/R. Relative levels of HSP90, HSP72, and HSP40 were higher ( P < 0.05) in E-Warm animals compared with both control and E-Cold. HSP10, HSP60, and HSP73 did not differ between groups. Exercise increased manganese superoxide dismutase (MnSOD) activity in both E-Warm and E-Cold hearts ( P < 0.05). Protection against I/R-induced lipid peroxidation in the LV paralleled the increase in MnSOD activity whereas lower levels of lipid peroxidation were observed in both E-Warm and E-Cold groups compared with control. We conclude that exercise-induced myocardial protection against a moderate duration I/R insult is not dependent on increases in myocardial HSPs. We postulate that exercise-associated cardioprotection may depend, in part, on increases in myocardial antioxidant defenses.

scholarly journals Effects of transport stress on pathological injury and expression of main heat shock proteins in the caprine stomach

2020 ◽  
Vol 16 (1) ◽  
Author(s):  
Wei Hu ◽  
Tian Ye ◽  
Yanzhen Yang ◽  
Ben Liu ◽  
Wenya Zheng
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Heat Shock Protein ◽  
Jiangxi Province ◽  
Control Group ◽  
Hsp70 Mrna ◽  
Stress Group ◽  
Protein Levels ◽  
Transport Stress ◽  
Shock Proteins

Abstract Background Transportation is necessary to introduce new breeds of goats to the farm and move the adult meat goat from the farm to the slaughterhouse. However, these actions may give rise to transport stress. Heat shock proteins (HSPs) are playing some important regulate roles during transport stress. The aim of this study was to evaluate the effects of transport stress on the pathological injury and HSPs expression in the stomach of goats. A total of three batches of Ganxi goats from western Jiangxi province were enrolled in this study. For each batch, twelve healthy adult male goats were randomly divided into three groups (four goats per batch and per group): Control group, stress group transported during 2 h and stress group transported during 6 h. Results Our results showed that the different degrees of stomach walls damage, with the change of expression levels of heat shock protein 27 (HSP27), heat shock protein 70 (HSP70) and heat shock protein 90 (HSP90), occurred after goats transportation. In rumen, the mRNA and protein expressions of HSP27 and HSP70 were increased after transport stress, but not HSP90. In reticulum, all three HSPs mRNA and protein levels were upregulated after 2 h transport, but decreased after 6 h transport. In omasum, HSP27 and HSP70 mRNA and protein were increased after transport stress, however, HSP90 mRNA level only had a slightly enhancement after transport stress. In abomasum, HSP70 and HSP90 mRNA and protein levels were increased after transport stress, but HSP27 was decreased after transport stress. Conclusions Taken together, these results revealed that the pathological changes in the gastric tissues and the stomach HSPs expression in goats are related to transport stress and duration. Moreover, this study also provides some new data to advocate reducing transport stress of goats and improving animal welfare.

T Cells Response and Autoantibodies to Human Heat Shock Proteins in Aplastic Anemia Patients.

Blood ◽  
2005 ◽  
Vol 106 (11) ◽  
pp. 2403-2403
Author(s):  
Yunfeng Cheng ◽  
Yong Tang ◽  
Neal S. Young
Keyword(s):  
Cell Proliferation ◽  
T Cells ◽  
T Cell ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Aplastic Anemia ◽  
T Cell Proliferation ◽  
Control Group ◽  
Cell Responses ◽  
Shock Proteins

Abstract Heat shock proteins (HSP) have been implicated in autoimmune diseases such as type I diabetes mellitus, systemic lupus erythematosus, and multiple sclerosis, in which T cell proliferative responses or autoantibodies towards endogenous HSP have been detected (Journal of Autoimmunity2003;20:313). HSP70 can function as an endogenous ‘danger’ signal, acting on antigen-presenting cells and critically influencing the decision between induction of tolerance and immunity upon antigen encounter (Millar et al. Nature Medicine2003; 9:1469). We studied T-cell proliferative responses and auto-antibodies to human HSP60, HSP70 and HSP90 proteins in 20 newly diagnosed aplastic anemia patients, peripheral blood was obtained (11 females, 9 males; age average 36.1±19 years). A non-isotopic immunoassay was used for BrdU incorporation into proliferative T cells and ELISA to measure HSP antibody titer. T cell proliferation was measured as the Eu-fluorescence in a time-resolved fluorometer. A positive result was defined as > 2 standard deviations (SD) from the mean of the controls. T-cell responses to HSP70 in the patient group (N=20; mean±SD Eu-fluorescence= 47,129±36,248) were significantly greater than those of the control group (N=18 healthy adult; mean Eu-fluorescence= 23,941±12,996; p=0.01). Fifty percent of the patients showed increased T cell proliferation after HSP70 stimulation compared to 5% in the control group (p=0.03). T-cell responses of the patient group to HSP90 and HSP60 were similar to those of the control group. Twenty percent of patients showed increased T cell proliferation to HSP 60 and HSP 90 stimulation compared to 5% in the control group (p=0.363). HSP antibody (IgG/A/M) seropositivity was 25% to HSP60, 50% to HSP70, and 5% to HSP90 in patients and 8% to HSP60, 0% to HSP70, and 0% to HSP90 in controls. Heightened autoimmunity to HSP70, but not to HSP60 and HSP90, is a feature of acquired aplastic anemia at presentation.

scholarly journals Heat Treatment at an Early Age Has Effects on the Resistance to Chronic Heat Stress on Broilers

Animals ◽  
2019 ◽  
Vol 9 (12) ◽  
pp. 1022 ◽  
Author(s):  
Darae Kang ◽  
JinRyong Park ◽  
KwanSeob Shim
Keyword(s):  
Heat Stress ◽  
High Temperature ◽  
Heat Shock ◽  
Stress Hormones ◽  
Heat Exposure ◽  
Control Group ◽  
Heat Shock Factors ◽  
Gene Expressions ◽  
Stressed Group ◽  
Shock Proteins

This study was conducted to investigate the effects of early heat conditioning on growth performance, liver-specific enzymes (GOT and GPT), neuro-hormones (dopamine and serotonin), stress hormones (corticosterone), and the expression of HSPs (heat shock proteins), HSFs (heat shock factors), and pro-inflammatory cytokines under chronic high temperature. Broilers were raised with commercial feed and supplied with water ad libitum under conventional temperature. We separated the broilers into three groups: the control without any heat exposure (C), chronic heat-stressed group (CH), and early and chronic heat-stressed group (HH). At 5 days of age, the HH group was exposed to high temperatures (40 °C for 24 h), while the remaining groups were raised at a standard temperature. Between days 6 and 20, all three groups were kept under optimal temperature. From 21 to 35 days, the two heat-stressed groups (CH and HH) were exposed to 35 °C. Groups exposed to high temperature (CH and HH) showed significantly lower body weight and feed intake compared to the control. GOT and GPT were lower expressed in the CH and HH groups than the control group. In addition, the protein expressions of HSPs were down-regulated by chronic heat stress (CH and HH groups). The gene expressions of HSP60 and HSF3 were significantly down-regulated in the CH and HH groups, while HSP70 and HSP27 genes were up-regulated only in the HH group compared with the control group. The expression of pro-inflammatory cytokine genes was significantly up-regulated in the HH group compared with the control and CH groups. Thus, exposure of early Heat stress (HS) to broilers may affect the inflammatory response; however, early heat exposure did not have a positive effect on chronic HS of liver enzymes and heat shock protein expression.

scholarly journals The Mitochondrial Small Heat Shock Protein HSP22 from Pea is a Thermosoluble Chaperone Prone to Co-Precipitate with Unfolding Client Proteins

2019 ◽  
Vol 21 (1) ◽  
pp. 97
Author(s):  
Marie-Hélène Avelange-Macherel ◽  
Aurélia Rolland ◽  
Marie-Pierre Hinault ◽  
Dimitri Tolleter ◽  
David Macherel
Keyword(s):  
Heat Shock ◽  
Recombinant Protein ◽  
Quaternary Structure ◽  
Small Heat Shock Protein ◽  
Effect Of Temperature ◽  
Molar Ratio ◽  
Client Proteins ◽  
Shock Proteins ◽  
Cellular Compartments

The small heat shock proteins (sHSPs) are molecular chaperones that share an alpha-crystallin domain but display a high diversity of sequence, expression, and localization. They are especially prominent in plants, populating most cellular compartments. In pea, mitochondrial HSP22 is induced by heat or oxidative stress in leaves but also strongly accumulates during seed development. The molecular function of HSP22 was addressed by studying the effect of temperature on its structural properties and chaperone effects using a recombinant or native protein. Overexpression of HSP22 significantly increased bacterial thermotolerance. The secondary structure of the recombinant protein was not affected by temperature in contrast with its quaternary structure. The purified protein formed large polydisperse oligomers that dissociated upon heating (42 °C) into smaller species (mainly monomers). The recombinant protein appeared thermosoluble but precipitated with thermosensitive proteins upon heat stress in assays either with single protein clients or within complex extracts. As shown by in vitro protection assays, HSP22 at high molar ratio could partly prevent the heat aggregation of rhodanese but not of malate dehydrogenase. HSP22 appears as a holdase that could possibly prevent the aggregation of some proteins while co-precipitating with others to facilitate their subsequent refolding by disaggregases or clearance by proteases.

scholarly journals Changed content of heat shock proteins and antibodies to them in blood and nasal mucosa cells in rhinites and rhinosinusites of different etiology

2018 ◽  
Vol 35 (6) ◽  
pp. 23-28
Author(s):  
M. O. Ivanov ◽  
N. M. Ivanova ◽  
M. V. Maksimenya ◽  
T. M. Karavaeva ◽  
E. V. Egorova ◽  
...  
Keyword(s):  
Allergic Rhinitis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Blood Serum ◽  
Nasal Secretion ◽  
Control Group ◽  
Hsp 70 ◽  
Immunological Effect ◽  
Shock Proteins ◽  
Age Range

Aim. To determine the content of heat shock proteins with molecular weight 70 kDa (HSP 70) and antibo dies to them in blood and nasal secretion in patients with allergic rhinites and infectious rhinosinusites of different etiology. Materials and methods. The paper presents the results of examination of 10 patients with allergic rhinitis and 30 patients, infected with rhinosinusites(the age range 25–35 years). The patients with infectious rhinosinusites were divided into 3 groups according to nosologic form of disease. The control group included 10 practically healthy persons in the ratio, comparable by their gender and age with sick persons. Results.The analysis showed that in the nasal secretion of all patients, HSP 70 level significantly raised compared to the control. Maximum values were registered in patients with bacterial rhinosinusitis and were higher than in patients with viral and fungous ones by 1.9 times (p = 0.015) and 2.9 times (p = 0.001), respectively. In blood serum, HSP 70 concentration compared with the control increased in patients with allergic rhinitis and bacterial rhinosinusitis by 103.67 % (p = 0.015) and 32.11 % (p = 0.049), respectively; these values in the last two groups exceeded the latter in patients with fungous RS by 2.37 times (p = 0.01) and by 1.54 times (p = 0.035). Conclusions. It was detected that in the group of patients with allergic rhinitis and chronic bacterial rhinosinusitis in the nasal secretion and blood serum, HSP 70 values were the highest. In the nasal secretion, HSP 70 level was higher than in blood. The amount of autoantibodies to HSP 70 in blood grew in allergic rhinitis, fungous and viral forms of rhinosinusites that reflects the immunological effect of chaperone proteins.

scholarly journals Melatonin mitigates cisplatin-induced acute kidney injury through regulation of the heat shock proteins expressions

2021 ◽  
Author(s):  
Ali Tuğrul Akin ◽  
Murat Unsal ◽  
Tayfun Ceylan ◽  
Emin Kaymak ◽  
Emel Ozturk ◽  
...  
Keyword(s):  
Acute Kidney Injury ◽  
Uric Acid ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Blood Serum ◽  
Renal Cortex ◽  
Kidney Injury ◽  
Control Group ◽  
Albino Rats ◽  
Shock Proteins

Abstract Purpose. To determine the protective effects of melatonin (MEL) in acute kidney injury (AKI) induced by Cisplatin (CP), widely used as a chemotherapeutic in the treatment of many cancer types, via assessment of heat-shock proteins (HSPs) levels in rats. Methods. Total 40 Wistar albino rats were divided into four groups: Control (n = 10), MEL (n = 10, 10 mg/kg/i.p melatonin for 8 days), CP (n = 10, 7 mg/kg/i.p cisplatin at the 5th day), and CP + MEL (n = 10, 10 mg/kg/i.p melatonin for 8 days and 7 mg/kg/i.p cisplatin at the 5th day). After administrations, animals were sacrificed, and kidney tissues were extracted. Histopathological changes were evaluated and glomerular and tubular immunoreactivities of HSP47, HSP60, HSP7, and HSP90 in renal cortex were detected by immunohistochemistry. Moreover, blood serum BUN, creatinine and uric acid levels were measured to assess of kidney function. Results. CP group showed histopathological deterioration compared to Control group and MEL treatment attenuated this damage. When compared with Control and MEL groups, an increase in HSPs immunoreactivities in renal cortex and blood serum BUN, creatinine and uric acid levels were observed in the CP group. Furthermore, an improvement was observed in the CP + MEL in terms of these parameters compared to the CP group. Conclusion. According to our results, MEL could exert a significant protective effect to ameliorate CP-induced AKI via regulation of heat-shock protein expressions.

Small heat shock proteins translocate to the cytoskeleton in human skeletal muscle following eccentric exercise independently of phosphorylation

2014 ◽  
Vol 116 (11) ◽  
pp. 1463-1472 ◽  
Author(s):  
Noni T. Frankenberg ◽  
Graham D. Lamb ◽  
Kristian Overgaard ◽  
Robyn M. Murphy ◽  
Kristian Vissing
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Eccentric Exercise ◽  
Vastus Lateralis ◽  
Small Heat Shock Proteins ◽  
Control Group ◽  
Vastus Lateralis Muscle ◽  
Partial Redistribution ◽  
Αb Crystallin ◽  
Shock Proteins

Small heat shock proteins (sHSPs) are a subgroup of the highly conserved family of HSPs that are stress inducible and confer resistance to cellular stress and injury. This study aimed to quantitatively examine whether type of contraction (concentric or eccentric) affects sHSPs, HSP27 and αB-crystallin, localization, and phosphorylation in human muscle. Vastus lateralis muscle biopsies from 11 healthy male volunteers were obtained pre- and 3 h, 24 h, and 7 days following concentric (CONC), eccentric (ECC1), and repeated bout eccentric (ECC2) exercise. No changes were apparent in a control group ( n = 5) who performed no exercise. Eccentric exercise induced muscle damage, as evidenced by increased muscle force loss, perceived muscle soreness, and elevated plasma creatine kinase and myoglobin levels. Total HSP27 and αB-crystallin amounts did not change following any type of exercise. Following eccentric exercise (ECC1 and ECC2) phosphorylation of HSP27 at serine 15 (pHSP27-Ser15) was increased approximately 3- to 6-fold at 3 h, and pαB-crystallin-Ser59 increased ∼10-fold at 3 h. Prior to exercise most of the sHSP and psHSP pools were present in the cytosolic compartment. Eccentric exercise resulted in partial redistribution of HSP27 (∼23%) from the cytosol to the cytoskeletal fraction (∼28% for pHSP27-Ser15 and ∼7% for pHSP27-Ser82), with subsequent full reversal within 24 h. αB-crystallin also showed partial redistribution from the cytosolic to cytoskeletal fraction (∼18% of total) 3 h post-ECC1, but not after ECC2. There was no redistribution or phosphorylation of sHSPs with CONC. Eccentric exercise results in increased sHSP phosphorylation and translocation to the cytoskeletal fraction, but the sHSP translocation is not dependent on their phosphorylation.

Anti Hsp70 Antibodies in Untreated Patients with Chronic Lymphocytic Leukaemia

Blood ◽  
2008 ◽  
Vol 112 (11) ◽  
pp. 4191-4191
Author(s):  
Jaroslaw Piszcz ◽  
Edyta Cichocka ◽  
Lukasz Bolkun ◽  
Marzenna Galar ◽  
Katarzyna Mazgajska-Barczyk ◽  
...  
Keyword(s):  
Prognostic Factors ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Chronic Lymphocytic Leukaemia ◽  
Lymphocytic Leukaemia ◽  
Surface Expression ◽  
Control Group ◽  
Antibody Concentration ◽  
Neoplastic Processes ◽  
Shock Proteins

Abstract Background: Chronic lymphocytic leukaemia (CLL) is one of the diseases in which processes of proliferation and apoptosis are altered. It has been intensely studied in the recent years in order to understand the mechanisms of neoplastic development. Hsps or heat shock proteins are molecular chaperones involved in a number of cellular functions in stress conditions. Feng et al. (2002) have reported that heat-stressed apoptotic 12B1-D1 leukaemia cells (BCR-ABL(+)) express Hsp70 on their surface. It has also been suggested that an increased surface expression of heat shock proteins on apoptotic tumour cells results in the generation of potent antitumour T-cell responses. Furthermore, different hsps including Hsp70 have been discovered in indolent lymphoma cells. Anti Hsp70 antibodies are known to play a role in immunological and neoplastic processes. It has been well documented that this antibodies level tends to increase with age likewise an incidence of CLL. However their significance in CLL has not been clearly understood. Aims: The aim of our study was the assessment of the anti Hsp70 antibody concentration in the patients with CLL. Material and methods: We assessed 60 peripheral blood samples from the patients with newly diagnosed CLL. (aged 40–77), including 31 males and 29 females. A group of 20 healthy age matched subjects were used as a control group. The patients were in A-C stages of CLL according to Binet scale. Quantitative determination of anti-human Hsp70 antibodies in the serum was done using commercial test (anti Hsp70 Elisa Kits, Stressgen). The results are presented as mean ± SEM. Statistical analysis was done using Shapiro-Wilk, Mann-Whitney and Spearman’s tests. Results: The levels of anti Hsp70 antibodies were significantly lower in the group of patients with CLL in comparison to healthy controls (105,70±16,86 ng/ml vs.243,71±60,36 ng/ml; p=0,0027). In our analysis there was no association between the levels of antibodies and the stage of the disease. There were no statistically significant correlations between the levels of anti Hsp antibodies and other parameters such as age, gender and some prognostic factors (LDH, β2-microglobulin, and lymphocyte doubling time) in the studied group. Conclusions: The significantly lower concentrations of anti Hsp70 antibodies in CLL patients suggest that these molecules may play a role in the biology of the disease. Our study revealed lack of correlation between the level of antibodies and the disease prognostic factors. However, further studies utilizing new discovered factors are required to elucidate the role of these proteins in leukaemic biology. The encouraging results from our study suggest that it might be interesting to assess their level in CLL patient after chemotherapy.

Early-Phase Detection of Heat Shock Proteins (Hsp27 and Hsp40) in Extruded Earthworm Tissue after Dermal Exposure to Herbicides

2011 ◽  
Vol 343-344 ◽  
pp. 1140-1151
Author(s):  
Chang E Liu ◽  
Chang Qun Duan ◽  
Fei Liu ◽  
Xing Peng
Keyword(s):  
Heat Shock ◽  
Imaging System ◽  
General Trend ◽  
The Body ◽  
Control Group ◽  
Phase Detection ◽  
Relative Expression ◽  
High Concentrations ◽  
Shock Proteins ◽  
Good Exposure

Samples on a regular basis, and the use of SDSPAGE and Western Blotting methods was inspected to express situation in the induction of heat shock protein (both Hsp27 and Hsp40) of the body tissue of earthworms (Eisenia foetide) exposed in the soil by respectively adding Atrazine, Chlorotoluron; Acetochlor, Butachlor. According to the gel imaging system for gray-scale scanner, with the increase of the concentration of herbicides, the relative expression of both Hsps showed the phenomenon of induction in low concentration and suppression in high concentrations within the range of tested concentration. With the extension of the processing time, both Hsps were first induced suppression of the general trend and there was good exposure time – coercing effect relationship. The relative expression of HSP27 and HSP40 exposed by Atrazine, Chlorotoluron, Acetochlor and Butachlor were 2.21, 1.98, 2.06, 2.11 times and 2.32, 1.99, 2.15, 2.24 times of the control group. The sensitive ability of the organization of HSP27 and HSP40 to four herbicides was in the order of Atrazine > Butachlor > Acetochlor > Chlorotoluron. The relative expression of Hsp40 slightly was a little bit larger than Hsp27.

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