The repeated bout effect and heat shock proteins: intramuscular HSP27 and HSP70 expression following two bouts of eccentric exercise in humans

2002 ◽  
Vol 174 (1) ◽  
pp. 47-56 ◽  
Author(s):  
H. S. Thompson ◽  
P. M. Clarkson ◽  
S. P. Scordilis
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Eccentric Exercise ◽  
Hsp70 Expression ◽  
Repeated Bout Effect ◽  
Shock Proteins ◽  
Exercise In Humans ◽  
Repeated Bout

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.

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 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

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.

scholarly journals Modulation of thermal induction of hsp70 expression by Ku autoantigen or its individual subunits.

1996 ◽  
Vol 16 (7) ◽  
pp. 3799-3806 ◽  
Author(s):  
S H Yang ◽  
A Nussenzweig ◽  
L Li ◽  
D Kim ◽  
H Ouyang ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cell Lines ◽  
Heat Shock Response ◽  
Hsp70 Expression ◽  
Shock Response ◽  
Ku Protein ◽  
Shock Proteins ◽  
Ku Autoantigen ◽  
Thermal Induction

Previously, we proposed a dual control mechanism for the regulation of the heat shock response in mammalian cells: a positive control mediated by the heat shock transcription factor HSF1 and a negative control mediated by the constitutive heat shock element-binding factor (CHBF). To study the physiological role of CHBF in the regulation of heat shock response, we purified CHBF to apparent homogeneity and showed it to be identical to the Ku autoantigen, a heterodimer consisting of 70-kDa (Ku-70) and 86-kDa (Ku-80) polypeptides. To study further the functional significance of Ku/CHBF in the cellular response to heat shock, we established rodent cell lines that stably and constitutively overexpressed one or both subunits of the human Ku protein, and examined the thermal induction of hsp70 and other heat shock proteins in these Ku-overexpressing ing cells. We show that expression of the human Ku-70 and Ku-80 subunits jointly or of the Ku-70 subunit alone specifically inhibits heat-induced hsp70 expression. Conversely, expression of human Ku-80 alone does not have this effect. Thermal induction of other heat shock proteins in all of the Ku-overexpressing cell lines appears not to be significantly affected, nor is the state of phosphorylation or the DNA-binding ability of HSF1 affected. These findings support a model in which hsp70 expression is controlled by a second regulatory factor in addition to the positive activation of HSF1. The Ku protein, specifically the Ku-70 subunit, is involved in the regulation of hsp70 gene expression.

Heat shock proteins (HSP70) expression in primary non-small cell lung carcinomas

Lung Cancer ◽  
1999 ◽  
Vol 25 ◽  
pp. S27 ◽  
Author(s):  
Ewa Malusecka ◽  
Anna Zborek ◽  
Stefania Krzyċwska-Gruca ◽  
Zdzislaẃ Krawczyk
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Small Cell ◽  
Hsp70 Expression ◽  
Small Cell Lung ◽  
Lung Carcinomas ◽  
Shock Proteins

scholarly journals Generation of tumors in wing imaginal discs of Drosophila melanogaster third instar larvae to study temporal and spatial patterns of expression of major heat shock proteins

2021 ◽  
Author(s):  
Gunjan Singh ◽  
Subhash C. Lakhotia
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Cancer Cells ◽  
Spatial Patterns ◽  
Hsp70 Expression ◽  
Loss Of Function ◽  
Temporal And Spatial Patterns ◽  
Early Stages ◽  
Temporal And Spatial ◽  
Shock Proteins

Cancer cells experience a variety of stresses like hypoxia, lack of nutrients, DNA damage and immune responses, which trigger several processes to drive genomic instability and mutation, alterations in gene expression programs, and reprogramming of the metabolic pathways to escape growth inhibition signaling, and acquire resistance to the immune surveillance. Different heat shock proteins are expressed at elevated levels in cancer cells. However, their specific roles in initiation, establishment and progression of cancers are still not clear. Here using the loss of function allele of the apico-basal polarity gene, lgl, we have established models for induction of tumorous somatic clones of different genetic constitutions at defined developmental times for examination of temporal and spatial patterns of expression of the major heat shock protein families, namely Hsp83, Hsp70, Hsp60 and Hsp27. The Hsp83, Hsp60 and Hsp27 begin to express in all cells of the tumor at high levels since early stages (48hr after tumor induction) and continue their high expression at later stages when the tumorous clones accumulate F-actin and get transformed. Levels of the heat shock cognate Hsc70 proteins also follow the same pattern as the other Hsps. However, the major stress-inducible Hsp70 is not expressed at early stages of tumor growth, but expresses at a later stage only in a few cells in a given lgl loss of function clone, which also shows high F-actin aggregates. Thus, the major Hsps, except the Hsp70, seems to be involved in early as well as late stages of epithelial tumors induced by loss of the Lgl cell polarity protein, while the Hsp70 expression in a few cells coincides with their getting transformed. This model will be useful for further genetic studies to dissect specific roles of different Hsps in tumor development and their therapeutic manipulation.

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.

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