Metal ions induced heat shock protein response by elevating superoxide anion level in HeLa cells transformed by HSE-SEAP reporter gene

Toxicology ◽  
2006 ◽  
Vol 223 (1-2) ◽  
pp. 1-8 ◽  
Author(s):  
Zhanjiang Yu ◽  
Xiaoda Yang ◽  
Kui Wang
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Metal Ions ◽  
Reporter Gene ◽  
Hela Cells ◽  
Superoxide Anion ◽  
Protein Response

Effect of atrazine and chlorpyrifos exposure on heat shock protein response in the brain of common carp (Cyprinus carpio L.)

2013 ◽  
Vol 107 (2) ◽  
pp. 277-283 ◽  
Author(s):  
Tao Liu ◽  
Ziwei Zhang ◽  
Dechun Chen ◽  
Liangliang Wang ◽  
Haidong Yao ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Common Carp ◽  
Cyprinus Carpio ◽  
Common Carp Cyprinus Carpio ◽  
Carp Cyprinus Carpio ◽  
Protein Response ◽  
The Brain

scholarly journals Anticancer Effects of LBA-ST Yogurt Supernatant on HeLa Cells via Heat Shock Protein 27 Decrease In Vitro

2017 ◽  
Vol 6 (1) ◽  
pp. 16
Author(s):  
Liziyyannida Liziyyannida ◽  
Wibi Riawan
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Short Chain Fatty Acids ◽  
Heat Shock Protein 27 ◽  
Lactobacillus Bulgaricus ◽  
Culture Cells ◽  
Response To Stress ◽  
And Migration

Heat Shock Protein 27 (Hsp27) is overexpressed in cervical cancer as a response to stress conditions. Hsp27 overexpression increase invasion, migration, and adhesion pathways of cancer cells. The Yogurt supernatant contains Short-Chain Fatty Acids (SCFA) include acetate, lactate, and butyrate which have anticancer activity. This study aimed to investigate supernatant of LBA-ST (Lactobacillusbulgaricus-acidophilus, Streptococcusthermophillus) Yogurt can decrease the expression of Hsp27 in HeLa culture cells. The mechanism on how supernatant yogurt inhibit invasion, migration, and adhesion was studied by immunocytochemistry. The data was then collected and analyzed using One-Way ANOVA. From this study, it can be concluded that the expression of proteins that play a role in invasion, adhesion, and migration of the Hsp27 was proven to be decreased (p< 0.05 ± 0.005).Keywords: HeLa cells, yogurt supernatant, Lactobacillus bulgaricus-acidophilus, Streptococcus thermophillus, Hsp27

A stress-inducible 40 kDa protein (hsp40): purification by modified two-dimensional gel electrophoresis and co-localization with hsc70(p73) in heat-shocked HeLa cells

1993 ◽  
Vol 104 (3) ◽  
pp. 629-638 ◽  
Author(s):  
H. Hattori ◽  
T. Kaneda ◽  
B. Lokeshwar ◽  
A. Laszlo ◽  
K. Ohtsuka
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells ◽  
Gel Electrophoresis ◽  
Recovery Period ◽  
Chinese Hamster ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis ◽  
Terminal Amino ◽  
Kinetics Of

We have previously reported that a novel 40 kDa protein is induced by heat shock and several environmental stresses in mammalian and avian cells and that the N-terminal amino acid sequence of this 40 kDa protein has homology with the bacterial DnaJ heat-shock protein. We have purified this protein (40 kDa heat-shock protein, hsp40) from HeLa cells by modified two-dimensional gel electrophoresis and generated a polyclonal antibody against hsp40. This antibody was highly specific for human hsp40 and cross-reacted weakly with rat and Chinese hamster hsp40. Indirect immunofluorescence revealed that the hsp40 in HeLa cells accumulates in the nucleus, especially in the nucleolus, during heat shock and returns to the cytoplasm during the recovery period. The kinetics of the accumulation in the nucleoli and subsequent return to the cytoplasm of hsp40 was similar to that of hsp70. In addition, hsp40 was co-localized with hsc70(p73) in heat-shocked HeLa cells as demonstrated by double immunofluorescence staining. These results suggest that hsp40 (a DnaJ homologue) and hsp70 (a DnaK homologue) may act in concert to repair (refold) denatured proteins and protein aggregates in the nuclei and nucleoli of heat-shocked HeLa cells.

Different Induction of 70,000-Da Heat Shock Protein and Metallothionein in HeLa Cells by Copper1

1991 ◽  
Vol 110 (5) ◽  
pp. 726-731 ◽  
Author(s):  
Takumi Hatayama ◽  
Yasohiro Tsukimi ◽  
Tohru Wakatsuki ◽  
Teruko Kitamura ◽  
Hirotsugu Imahara
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Hela Cells

The heat shock protein response following eccentric exercise in human skeletal muscle is unaffected by local NSAID infusion

2013 ◽  
Vol 113 (7) ◽  
pp. 1883-1893 ◽  
Author(s):  
U. R. Mikkelsen ◽  
G. Paulsen ◽  
P. Schjerling ◽  
I. C. Helmark ◽  
H. Langberg ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Eccentric Exercise ◽  
Human Skeletal Muscle ◽  
Protein Response

scholarly journals Comparative inhibition by hard and soft metal ions of steroid-binding capacity of renal mineralocorticoid receptor cross-linked to the 90-kDa heat-shock protein heterocomplex

1999 ◽  
Vol 341 (3) ◽  
pp. 585-592 ◽  
Author(s):  
Mario D. GALIGNIANA ◽  
Graciela PIWIEN-PILIPUK
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Metal Ions ◽  
Mineralocorticoid Receptor ◽  
Binding Capacity ◽  
Toxic Effects ◽  
Chemical Hardness ◽  
Activation Process ◽  
Steroid Binding

We analysed the inhibitory effectsin vitro and in vivo of several metal ions on aldosterone binding to the rat kidney mineralocorticoid receptor with the purpose of assessing possible toxic effects of those ions on sodium retention, as well as to obtain information on receptor structural requirements for ligand binding. For the assaysin vitro, the inhibitory effects of 20 metal ions were analysed on steroid-binding capacity for renal receptor cross-linked to 90-kDa heat-shock protein (hsp90) by pretreatment with dimethyl pimelimidate. Cross-linking prevented the artifactual dissociation of hsp90 (and, consequently, the loss of steroid binding) from the mineralocorticoid receptor due to the presence of high concentrations of salt in the incubation medium. Cross-linked heterocomplex showed no difference in ligand specificity and affinity with respect to native receptor, but increased stability upon thermal- or ionic-strength-induced destabilization was observed. Treatments in vitro with metal ions in the range 10-8-10-1 M resulted in a differential inhibitory effect for each particular ion on aldosterone binding. Using the negative logarithm of metal concentration for 50% inhibition, the ions could be correlated with their Klopman hardness constants. The analysis of this relationship led us to postulate three types of reaction: with thiol, imidazole and carboxyl groups. The essential role played by these residues in steroid binding was confirmed by chemical modification of cysteines with dithionitrobenzoic acid, histidines with diethyl pyrocarbonate and acidic amino acids with Woodward's reagent (N-ethyl-5-phenylisoxazolium-3′-sulphonate). Importantly, the toxic effects of some metal ions were also observed by treatments in vivo of adrenalectomized rats on both steroid-binding capacity and aldosterone-dependent sodium-retaining properties. We suggest that those amino acid residues are involved in the activation process of the mineralocorticoid receptor upon steroid binding. Thus toxic effects observed with these metal ions may be a consequence of modifications of those essential groups. Our results support the notion that toxicity of metals on renal mineralocorticoid function may be predicted according to their chemical hardness.

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