• Asian Pacific Journal of Cancer Prevention
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• 제17권8호
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• pp.3929-3937
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• 2016

Gastric cancer (GC) is a major health problem worldwide and is one of the ten most commonly diagnosed cancers in Jordan. GC is usually diagnosed at late aggressive stages in which treatment options are limited. Recently, heat shock proteins (HSPs) were found to be overexpressed in a wide range of malignancies have been considered as promising candidate biomarkers for GC. The aim of this study was to investigate pathogenic roles of a panel of cytosolic HSPs including HSP90, HSP70, HSP60 and HSP27 in GC. Immunohistochemistry was used to assess the level of expression of these proteins in archived tumor samples (N=87) representing various pathological characteristics of GC. HSP90, HSP60 and HSP27 were expressed abundantly in gastric tumors. On the other hand, HSP70 was reduced significantly and also found to be associated with Helicobacter pylori infection in tissues collected from GC patients. Furthermore, HSP27 was found to be associated with the level of differentiation. Our findings indicate a role of HSP70 as a potential prognostic biomarker, patients harboring positive HSP70 expression displaying worse disease free survival than those with negative HSP70 expression. Differential expression of HSPs may play crucial roles in the initiation and progression of GC, and could be exploited as future therapeutic targets.

• BMB Reports
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• 제40권1호
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• pp.107-112
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• 2007

To study the functioning of HSP70 in Escherichia coli, we selected NtHSP70-2 (AY372070) from among three genomic clones isolated in Nicotiana tabacum. Recombinant NtHSP70-2, containing a hexahistidine tag at the amino-terminus, was constructed, expressed in E. coli, and purified by $Ni^{2+}$ affinity chromatography and Q Sepharose Fast Flow anion exchange chromatography. The expressed fusion protein, $H_6NtHSP70$-2 (hexahistidine-tagged Nicotiana tabacum heat shock protein 70-2), maintained the stability of E. coli proteins up to 90$^{\circ}C$. Measuring the light scattering of luciferase (luc) revealed that NtHSP70-2 prevents the aggregation of luc without ATP during high-temperature stress. In a functional bioassay (1 h at 50$^{\circ}C$) for recombinant $H_6NtHSP70$-2, E. coli cells overexpressing $H_6NtHSP70$-2 survived about seven times longer than those lacking $H_6NtHSP70$-2. After 2 h at 50$^{\circ}C$, only the E. coli overexpressing $H_6NtHSP70$-2 survived under such conditions. Our NtHSP70-2 bioassays, as well as in vitro studies, strongly suggest that HSP70 confers thermo-tolerance to E. coli.

• Journal of Animal Science and Technology
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• 제65권4호
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• pp.683-697
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• 2023

The threat posed by increased surface temperatures worldwide has attracted the attention of researchers to the reaction of animals to heat stress. Spermatogenesis in animals such as stallions is a temperature-dependent process, ideally occurring at temperatures slightly below the core body temperature. Thus, proper thermoregulation is essential, especially because stallion spermatogenesis and the resulting spermatozoa are negatively affected by increased testicular temperature. Consequently, the failure of thermoregulation resulting in heat stress may diminish sperm quality and increase the likelihood of stallion infertility. In this review, we emphasize upon the impact of heat stress on spermatogenesis and the somatic and germ cells and describe the subsequent testicular alterations. In addition, we explore the functions and molecular responses of heat shock proteins, including HSP60, HSP70, HSP90, and HSP105, in heat-induced stress conditions. Finally, we discuss the use of various therapies to alleviate heat stress-induced reproductive harm by modulating distinct signaling pathways.

• Animal cells and systems
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• 제14권4호
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• pp.267-274
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• 2010

The decrease in sperm quality under heat stress causes a great loss in animal husbandry production. In order to reveal the mechanism underlying the sperm quality decrease caused by heat stress, we first established a mild heat-treated mouse model. Then, the sperm quality was identified. Further, the testicular proteome profile was mapped and compared with the control using 2D electrophoresis and mass spectrometry. Finally, the differential expressed proteins involved in the heat stress response were identified by real-time PCR and Western blotting. The results showed that heat stress caused a significant reduction in mouse sperm quality (P<0.05). Further, 52 protein spots on the 2D gel were found to differ between the heat-shocked tissues and the control. Of these spots, some repair proteins which might provide some explanation for the influence on sperm quality were found. We then focused on Bag-1, Hsp40, Hsp60 and Hsp70, which were found to be differently expressed after heat shock (P<0.05). Further analysis in this heat-shocked model suggests numerous potential mechanisms for heat shock-induced spermatogenic disorders.

• Toxicological Research
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• 제13권1_2호
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• pp.79-86
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• 1997

Inhibitory effects of tannic acid on skin toxicity and heat shock protein induced by UVB were investigated. Tannic acid was administered either topically or orally for 3 days to hairless mice, which were previously irradiated with UVB. UVB was found to cause skin erythema . However, the skin erythema was decreased when tannic acid was administered either topically or orally. The heat shock proteins, Hsp-78 kDa and 70 kDa, were induced by UVB irradiation, but the induction was decreased by treatment of tannic acid in both topically and orally administered groups. The hsp induction was more prominent in orally administered groups than in topically administerd groups. However, the difference between two groups was not statistically significant. The route of administrations, topical and oral, does not affect the activity of tannic acid. In the skin tissue observation, tannic acid regenerated the epithelial cells with 7-9 cell layers which were injured by UVB. In conclusion, tannic acid has an ability to protect against UVB irradiation and regenerate the skin.

• Animal Bioscience
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• 제36권12호
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• pp.1796-1805
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• 2023

Objective: This study aims to identify heat shock protein70-2 (HSP70-2) and protamine-1 (PRM1) mRNA and protein in Madura bull sperm and demonstrate their relation as bull fertility biomarkers. Methods: The Madura bull fertility rates were grouped based on the percentage of first service conception rate (%FSCR) as high fertility (HF) (79.04%; n = 4), and low fertility (LF) (65.84%; n = 4). mRNA of HSP70-2 and PRM1 with peptidylprolyl isomerase A (PPIA) as a housekeeping gene were determined by quantitative real-time polymerase chain reaction, while enzyme-linked immunoassay was used to measure protein abundance. In the post-thawed semen samples, sperm motility, viability, acrosome integrity, and sperm DNA fragmentation index were analyzed. Data analysis was performed on the measured parameters of semen quality, relative mRNA expression, and protein abundance of HSP70-2 and PRM1, among the bulls with various fertility levels (HF and LF) in a one-way analysis of variance analysis. The Pearson correlation was used to analyze the relationship between semen quality, mRNA, proteins, and fertility rate. Results: Relative mRNA expression and protein abundance of HSP70-2 and PRM1 were detected and were found to be highly expressed in bulls with HF (p<0.05) and were associated with several parameters of semen quality. Conclusion: HSP70-2 and PRM1 mRNA and protein molecules have great potential to serve as molecular markers for determining bull fertility.

• Molecules and Cells
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• 제19권3호
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• pp.328-333
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• 2005

Small heat shock proteins (sHSPs) are widely distributed, and their function and diversity of structure have been much studied in the field of molecular chaperones. In plants, which frequently have to cope with hostile environments, sHSPs are much more abundant and diverse than in other forms of life. In response to high temperature stress, sHSPs of more than twenty kinds can make up more than 1% of soluble plant proteins. We isolated a genomic clone, NtHSP18.3, from Nicotiana tabacum that encodes the complete open reading frame of a cytosolic class I small heat shock protein. To investigate the function of NtHSP18.3 in vitro, it was overproduced in Escherichia coli and purified. The purified NtHSP18.3 had typical molecular chaperone activity as it protected citrate synthase and luciferase from high temperature-induced aggregation. When E. coli celluar proteins were incubated with NtHSP18.3, a large proportion of the proteins remained soluble at temperatures as high as $70^{\circ}C$. Native gel analysis suggested that NtHSP18.3 is a dodecameric oligomer as the form present and showing molecular chaperone activity at the condition tested. Binding of bis-ANS to the oligomers of NtHSP18.3 indicated that exposure of their hydrophobic surfaces increased as the temperature was raised. Taken together, our data suggested that NtHSP18.3 is a molecular chaperone that functions as a dodecameric complex and possibly in a temperature-induced manner.

• The Journal of Korean Physical Therapy
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• 제12권1호
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• pp.147-151
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• 2000

Heat shock protein 70(HSP70) is induced by elevated temperature and many other types of stresses in cell. HSP70 ensures cell survival under stressful condition that would lead to irreversible cell damage and ultimately to cell death. HSP70 plays essential role in the synthesis, transport, and folding of proteins and is often refferred to as molecular chaperones. Increased levels of HSPs occur after arthritis, infection, imflammation, autoimmune disease and CNS injury such as infarction, ischemia, seizure and Alzheimer's disease. Also, HSP70 increases resistance to apoptosis. The recent studies that the expression of the HSP has been processed at various field. However, they an still relatively line studied in clinically application. This review summarizes the fundamental knowledge of HSP.

• Genomics & Informatics
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• 제11권1호
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• pp.52-54
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• 2013

Proteins in DNAJ/K families are ubiquitous, from prokaryotes to eukaryotes, and function as molecular chaperones. For systematic phylogenomics of the DNAJ/K families, we developed the Eukaryotic DNAJ/K Database (EDD). A total of 12,908 DNAJs and 4,886 DNAKs were identified from 339 eukaryotic genomes in the EDD. Kingdom-wide comparison of DNAJ/K families provides new insights on the evolutionary relationship within these families. Empowered by 'class', 'cluster', and 'taxonomy' browsers and the 'favorite' function, the EDD provides a versatile platform for comparative genomic analyses of DNAJ/K families.

• 대한약리학회지
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• 제31권3호
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• pp.323-331
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• 1995

사구체내 단핵구의 침윤은 면역학적뿐 아니라 비면역학적 사구체 질환 발생 초기에 특징적으로 관찰된다. 단핵구에서 합성되는 대표적인 사이토 카인인 tumor necrosis factor $(TNF){\alpha}$의 합성이 각종 사구체 질환과 관련되어 증가할 뿐 아니라 외부에서 투여한 $TNF{\alpha}$는 사구체 질환의 발생과 진행에 수반된 유사한 증세를 초래한다. 따라서 본 연구에서는 사구체 질환의 표적세포인 혈관간 세포를 이용하여 $TNF{\alpha}$에 의한 세포독성 기전을 검색하고자 하였다. 표준화된 체걸름법을 이용하여 사구체를 분리한후 collagenase로 처리하여 배양하므로써 혈관간 세포의 특징을 지닌 일차 배양 혈관간 세포계를 수립하였다. 세포독성의 지표로서 지질과산화물을 측정했을때, $TNF{\alpha}$는 용량의존적으로 배양 혈관간 세포의 지질과산화를 증가시켰다. 배양혈관간 세포를 $45^{\circ}C$에서 30분간 처리했을 때 heat shock protein 70의 합성이 증가함을 western 분석으로 확인하였을 뿐 아니라, $TNF{\alpha}$에 의한 지질과산화 증가를 효과적으로 억제함을 관찰하였다. 이상의 결과는 $TNF{\alpha}$에 의한 지질과산화 증가가 사구체 질환의 발생이나 진행에 관하여할 수 있음과 고온 전처리에 의해서 heat shock 반응을 초래하므로써 $TNF{\alpha}$에 의한 사구체 손상을 보호할 수 있음을 시사하였다.