scholarly journals Melatonin and thermal stress regulate differential expression of heat shock proteins and melatonin receptors in spleen of mice

2015 ◽  
Vol 3 (01) ◽  
pp. 36-47 ◽  
Author(s):  
Samik Acharjee ◽  
Shiv Shankar Singh
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Receptor Expression ◽  
Melatonin Receptors ◽  
Hsp70 Expression ◽  
Immune Functions ◽  
Experimental Conditions ◽  
Shock Proteins ◽  
Thermally Stressed

Cellular defence by expression of heat shock proteins (Hsps) against stress stimulation is the most universal phenomenon in stress physiology. Melatonin is well known as an anti-stress molecule possessing hypothermic effects. It protects cells and tissues in stressed conditions. Individually, Hsp70 and melatonin shows its functional ability in stressed organisms as well as in immune functions. The aim of the present study was to determine the interaction of melatonin receptors (MT1/MT2) in exogenous melatonin modulated expression of heat shock proteins (Hsp70/Hsc70) in spleen of thermally stressed male mice. Results of the study showed thermal stress significantly increased the Hsp70/Hsc70 and melatonin receptor MT2 expression in spleen of mice. The administration of melatonin significantly increased Hsp70 expression, but decreased Hsc70 expression. Both MT1/MT2 receptor expressions increased after melatonin treatment, whereas thermal stress to melatonin treated mice showed decrease in MT1/MT2 receptor expression than the only melatonin treated mice. MT2 receptor is responding in all experimental conditions corresponding to changes in Hsp70 protein expression. Therefore, the present study might suggest that MT2 receptor is interacting in coordination of melatonin mediated heat shock proteins expression in mice spleen after thermally stressed conditions.

scholarly journals Expression pattern of heat shock proteins during acute thermal stress in the Antarctic sea urchin, Sterechinus neumayeri

2016 ◽  
Vol 89 (1) ◽  
Author(s):  
Karina González ◽  
Juan Gaitán-Espitia ◽  
Alejandro Font ◽  
César A. Cárdenas ◽  
Marcelo González-Aravena
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Expression Pattern ◽  
Sea Urchin ◽  
Sterechinus Neumayeri ◽  
Shock Proteins ◽  
The Antarctic

Expression of heat shock proteins in medulloblastoma

2013 ◽  
Vol 12 (5) ◽  
pp. 452-457 ◽  
Author(s):  
George A. Alexiou ◽  
George Vartholomatos ◽  
Kalliopi Stefanaki ◽  
Amalia Patereli ◽  
Lefkothea Dova ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Significant Positive Correlation ◽  
Large Cell ◽  
Hsp70 Expression ◽  
Ki 67 ◽  
Positive Correlation ◽  
Wide Range ◽  
Shock Proteins ◽  
Multiplex Bead

Object Medulloblastoma (MB) is the most common malignant brain tumor in children. Heat shock proteins (HSPs) comprise a superfamily of proteins that serve as molecular chaperones and are overexpressed in a wide range of human cancers. The purpose of the present study was to investigate the expression of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt by multiplex bead array assay of MBs. The results of HSP and Akt expression were correlated with MB subtype; immunohistochemical expression of Ki-67 index, bcl-2, and p53; and patients' prognosis. Methods The authors retrospectively evaluated 25 children with MB who underwent surgery. Immunohistochemical analysis of Ki-67, p53, and bcl-2 expression was performed in all cases. By using multiplex bead array assay, a simultaneous detection of HSP27 (pSer82), HSP27 (pSer15), HSP40, HSP60, HSP70, HSP90-α, Akt, and phospho-Akt was performed. Results Medulloblastoma with extensive nodularity had significantly lower HSP27 (pSer15) expression (p = 0.039) but significantly higher HSP60 expression (p = 0.021) than classic MB. Large-cell MB had significantly higher HSP70 expression (p = 0.028) than classic MB. No significant difference was found between HSP27 (pSer82), HSP40, HSP90-α, Akt, or phospho-Akt expression and MB subtype. Large-cell MBs had significantly higher Ki-67 index compared with classic MBs (p = 0.033). When analyzing all MBs, there was a significant negative correlation between HSP27 (pSer15) and Ki-67 index (r = −0.475, p = 0.016); a significant positive correlation between HSP70 expression and Ki-67 index (r = 0.407, p = 0.043); and a significant positive correlation between HSP70 expression and bcl-2 index (r = 0.491, p = 0.023). Patients with large-cell MB had a worse survival than those with classic MB, but the difference did not reach statistical significance (p = 0.076). Conclusions A substantial expression of several HSPs in MB was observed. Given that HSPs represent an attractive strategy for anticancer therapy, further studies, involving larger series of patients, are obviously necessary to clarify the relationship of HSPs with tumor aggressiveness and prognosis.

161; DISPARATE EXPRESSION OF HEAT SHOCK PROTEINS IN DIFFERENT ORGANS OF THERMALLY STRESSED RATS

Shock ◽  
1994 ◽  
Vol 1 (Supplement) ◽  
pp. 45 ◽  
Author(s):  
S. C. Beck ◽  
C. Paidas ◽  
H. Tan ◽  
J. Yang ◽  
M. Rodriguez-Ortega ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Shock Proteins ◽  
Thermally Stressed

scholarly journals Heat Shock Proteins 27, 70, and 110: Expression and Prognostic Significance in Colorectal Cancer

Cancers ◽  
2021 ◽  
Vol 13 (17) ◽  
pp. 4407
Author(s):  
Jan Hrudka ◽  
Karolína Jelínková ◽  
Hana Fišerová ◽  
Radoslav Matěj ◽  
Václav Mandys ◽  
...  
Keyword(s):  
Survival Analysis ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cox Regression ◽  
Prognostic Significance ◽  
Response To Therapy ◽  
Rank Test ◽  
Hsp70 Expression ◽  
Uicc Stage ◽  
Shock Proteins

Heat shock proteins (HSPs) are evolutionarily conserved chaperones occurring in virtually all living organisms playing a key role in the maintenance of cellular homeostasis. They are constitutively expressed to prevent and repair protein damage following various physiological and environmental stressors. HSPs are overexpressed in various types of cancers to provide cytoprotective function, and they have been described to influence prognosis and response to therapy. Moreover, they have been used as a tumor marker in blood serum biochemistry and they represent a potentially promising therapeutic target. To clarify prognostic significance of two canonical HSPs (27 and 70) and less known HSP110 (previously known as HSP105) in colorectal carcinoma (CRC), we retrospectively performed HSP immunohistochemistry on tissue microarrays from formalin-fixed paraffin-embedded tumor tissue from 297 patients with known follow-up. Survival analysis (univariate Kaplan–Meier analysis with the log-rank test and multivariate Cox regression) revealed significantly shorter overall survival (OS, mean 5.54 vs. 7.07, p = 0.033) and borderline insignificantly shorter cancer specific survival (CSS, mean 6.3 vs. 7.87 years, p = 0.066) in patients with HSP70+ tumors. In the case of HSP27+ tumors, there was an insignificantly shorter OS (mean 6.36 vs. 7.13 years, p = 0.2) and CSS (mean 7.17 vs. 7.95 years, p = 0.2). HSP110 showed no significant impact on survival. Using Pearson’s chi-squared test, there was a significant association of HSP27 and HSP70 expression with advanced cancer stage. HSP27+ tumors were more frequently mismatch-repair proficient and vice versa (p = 0.014), and they occurred more often in female patients and vice versa (p = 0.015). There was an enrichment of left sided tumors with HSP110+ compared to the right sided (p = 0.022). In multivariate Cox regression adjusted on the UICC stage, grade and right/left side; both HSPs 27 and 70 were not independent survival predictors (p = 0.616 & p = 0.586). In multivariate analysis, only advanced UICC stage (p = 0) and right sided localization (p = 0.04) were independent predictors of worse CSS. In conclusion, from all three HSPs examined in our study, only HSP70 expression worsened CRC prognosis, although stage-dependent. The contribution of this article may be seen as a large survival analysis of HSPs 27 and 70 and the largest analysis of HSP110 described in CRC.

scholarly journals Influence of Heating and Cyclic Tension on the Induction of Heat Shock Proteins and Bone-Related Proteins by MC3T3-E1 Cells

2014 ◽  
Vol 2014 ◽  
pp. 1-16 ◽  
Author(s):  
Eunna Chung ◽  
Alana Cherrell Sampson ◽  
Marissa Nichole Rylander
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Tensile Stress ◽  
Bone Cells ◽  
Cyclic Strain ◽  
Fold Increase ◽  
Shock Proteins ◽  
Related Proteins ◽  
The Impact

Stress conditioning (e.g., thermal, shear, and tensile stress) of bone cells has been shown to enhance healing. However, prior studies have not investigated whether combined stress could synergistically promote bone regeneration. This study explored the impact of combined thermal and tensile stress on the induction of heat shock proteins (HSPs) and bone-related proteins by a murine preosteoblast cell line (MC3T3-E1). Cells were exposed to thermal stress using a water bath (44°C for 4 or 8 minutes) with postheating incubation (37°C for 4 hours) followed by exposure to cyclic strain (equibiaxial 3%, 0.2 Hz, cycle of 10-second tensile stress followed by 10-second rest). Combined thermal stress and tensile stress induced mRNA expression of HSP27 (1.41 relative fold induction (RFI) compared to sham-treated control), HSP70 (5.55 RFI), and osteopontin (1.44 RFI) but suppressed matrix metalloproteinase-9 (0.6 RFI) compared to the control. Combined thermal and tensile stress increased vascular endothelial growth factor (VEGF) secretion into the culture supernatant (1.54-fold increase compared to the control). Therefore, combined thermal and mechanical stress preconditioning can enhance HSP induction and influence protein expression important for bone tissue healing.

scholarly journals Involvement of small heat shock proteins, trehalose, and lipids in the thermal stress management in Schizosaccharomyces pombe

2015 ◽  
Vol 21 (2) ◽  
pp. 327-338 ◽  
Author(s):  
Attila Glatz ◽  
Ana-Maria Pilbat ◽  
Gergely L. Németh ◽  
Katalin Vince-Kontár ◽  
Katalin Jósvay ◽  
...  
Keyword(s):  
Thermal Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Schizosaccharomyces Pombe ◽  
Stress Management ◽  
Small Heat Shock Proteins ◽  
Shock Proteins

scholarly journals Protective effect of Zingiber zerumbet Smith extract on thermotolerance

2021 ◽  
Vol 4 (1) ◽  
pp. 1
Author(s):  
Yasuhito Shirai ◽  
Hisakazu Kobayashi ◽  
Shuji Ueda ◽  
Yun Sang Soon ◽  
Akiho Kushiya ◽  
...  
Keyword(s):  
Heat Treatment ◽  
Growth Rate ◽  
Heat Stress ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Hsp70 Expression ◽  
Heat Shock Treatment ◽  
Zingiber Zerumbet ◽  
Murine Liver ◽  
Shock Proteins

Background: Global warming causes severe heat conditions. Heat stress contributes to higher morbidity of heatstroke in human and mortality in livestock. To protect them from heat stress, thermotolerance mechanisms were widely studied, and some studies suggest relationship between heat shock proteins (HSPs) and thermotolerance. HSPs were not induced by only heat shock but also some stimulations including bioactive compounds from plants. Zingiber zerumbet is a perennial herb found in many tropical countries, including Thailand. The rhizome of Zingiber zerumbet contains zerumbone that is a bioactive compound to induce HSPs expression in animal cells.Objective: To prevent higher morbidity of heatstroke in human and mortality in livestock by the heat stress, we investigated the effect of zerumbone, the extract of Zingiber zerumbet Smith, on thermotolerance, using a cell line and mice.Methods: The murine liver hepatoma cell line, Hepa1c1c7 cells, were incubated in medium supplemented with extract from rhizome of Zingiber zerumbet Simith containing zerumbone, and then the expression of heat shock proteins (HSP) 40, 70 and 90 were investigated by western blotting. Furthermore, we established the evaluation system of thermotolerance using mice, and studied the effect of the extract on the growth rate of mice under the heat shock treatment. Briefly, 4 weeks old C57BL6 mice were fed that with the extract (or vehicle) for a week before the first heat shock treatment (38 °C for an hour). Before and after five days heat treatment, body weights were measured. The protein expressions of heat shock proteins in liver were measured by western blotting using HSPs antibodies.Results: The extract of Zingiber zerumbet rhizome, equivalent to 50 μM zerumbone, significantly increased the expression of heat shock proteins (HSP40, HSP70, HSP90). The growth rate of the mice under the heat treatment were lower than control. The feeding with the extract containing 25 ppm zerumbone have significantly attenuated the decline of the growth rate led by the heat treatment, whereas there was little effect on mouse growth rate grown under normal conditions. The protein expression of HSP70 in the liver of zerumbone-fed mice was upregulated compared with control mice, equivalent to heat treatment without zerumbone. On the other hand, both treatments of zerumbone and heat resulted in highest HSP70 expression among four groups.Conclusion: Our study demonstrated that oral administration of the extract of Zingiber zerumbet Smith led to the attenuation of decline of growth rate induced by heat treatment. HSP70 expression in murine liver was enhanced by either feeding the extract or heat treatment. More interestingly, HSP70 expression was further enhanced by both treatments of zerumbone and heat. These results suggested that zerumbone may contribute to thermotolerance via, at least, HSP70 expression.Keywords: Zingiber zerumbet, thermotolerance, heat shock protein

Sign in / Sign up

Export Citation Format

Share Document