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

scholarly journals Studies of Heat shock protein 27 Interactions

2014 ◽  
Vol 70 (a1) ◽  
pp. C804-C804
Author(s):  
Adeleke Aguda ◽  
Nham Nguyen ◽  
Sami Caner ◽  
Susan Moore ◽  
Barbara Lelj-Garolla ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Actin Polymerization ◽  
Heat Shock Protein 27 ◽  
Actin Binding ◽  
Apoptotic Protein ◽  
Terminal Loop ◽  
Common Substrate ◽  
Partially Unfolded

Human heat shock protein 27 (Hsp27) is an oligomeric and cell survival protein that has been associated with several cancers including prostrate and breast cancer. It's a known anti-apoptotic protein that functions as a molecular chaperone for several proteins. Hsp27 characteristically binds and stabilizes numerous partially unfolded proteins preventing their degradation, and has been shown to prevent actin polymerization in vitro. Several actin-binding residues involved in this interaction have been identified at the N-terminal loop and highly conserved alpha crystallin domains of Hsp27. Multiple assays have demonstrated that this hydrophobic actin-binding site is also involved in other protein binding. We therefore propose a common substrate-binding region on Hsp27 and present a model of Hsp27 binding to actin.

Targeting heat-shock protein 27 enhances sensitivity to sorafenib treatment in renal cancer in vitro and in vivo

2017 ◽  
Vol 16 (3) ◽  
pp. e1480
Author(s):  
S. Frees ◽  
C. Chavez-Munoz ◽  
B. Zhou ◽  
P. Raven ◽  
L. Fazli ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Renal Cancer ◽  
Heat Shock Protein 27 ◽  
Sorafenib Treatment

scholarly journals Silencing Heat Shock Protein 27 Inhibits the Progression and Metastasis of Colorectal Cancer (CRC) by Maintaining the Stability of Stromal Interaction Molecule 1 (STIM1) Proteins

Cells ◽  
2018 ◽  
Vol 7 (12) ◽  
pp. 262 ◽  
Author(s):  
Chien-Yu Huang ◽  
Po-Li Wei ◽  
Wei-Yu Chen ◽  
Wei-Chiao Chang ◽  
Yu-Jia Chang
Keyword(s):  
Colorectal Cancer ◽  
Colon Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Calcium Influx ◽  
Heat Shock Protein 27 ◽  
Tissue Array ◽  
Migration And Invasion ◽  
Store Operated Calcium Entry

The incidence of colorectal cancer (CRC) has significantly increased in recent decades, and this disease has become an important health issue worldwide. Currently, there is no useful prognostic or diagnostic biomarker for CRC. Heat shock protein 27 (HSP27) is a chaperone that interacts with many proteins. HSP27 has been shown to be overexpressed in many cancers, including colon cancer, and its overexpression is related to poor disease outcome. Although the importance of HSP27 as a biomarker cannot be underrated, its detailed mechanisms in colon cancer are still unclear. In vitro studies have indicated that silencing HSP27 reduces the proliferation, migration and invasion of colon cancer cells, and xenograft models have shown that silencing HSP27 decreases tumor progression. Tissue array results showed that colon cancer patients with high expression of HSP27 exhibited poor prognosis. In addition, we found a reduction of calcium influx through a decrease in STIM1 protein after HSP27 was abolished. The formation of puncta was decreased in HSP27 knockdown (HSP27KD) cells after thapsigargin (TG) treatment. Finally, we confirmed that the reduction of STIM1 after HSP27 silencing may be due to a loss of STIM1 stability instead of transcription. HSP27 may interact with STIM1 but not Orai1, as shown by immunoprecipitation assays. HSP27 and STIM1 were co-expressed in CRC specimens. Our study showed that HSP27 is a key mediator in the progression and metastasis of CRC by regulating the store-operated calcium entry. This novel pathway may provide a new direction for development of therapeutic strategies for CRC.

scholarly journals Cytoprotective Effect of Heat Shock Protein 27 Against Lipopolysaccharide-Induced Apoptosis of Renal Epithelial HK-2 Cells

2017 ◽  
Vol 41 (6) ◽  
pp. 2211-2220 ◽  
Author(s):  
Chunmei Li ◽  
Jiang Wu ◽  
Yuan Li ◽  
Guangqun Xing
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cell Viability ◽  
Proinflammatory Cytokines ◽  
Mrna Level ◽  
Kidney Injury ◽  
Heat Shock Protein 27 ◽  
Survival Advantage ◽  
Inflammatory Factor

Background: In response to various stimuli, heat shock protein 27 (Hsp27) functions as an anti-apoptotic or/and anti-inflammatory factor which confers a survival advantage to cells. This study was aimed to explore whether Hsp27 also has a cytoprotective role in human renal tubular epithelial cells, and to evaluate its potential in treating septic acute kidney injury (septic AKI). Methods: HK-2 cells were subjected to different concentrations (0-10 µg/mL) of lipopolysaccharide (LPS) for various times (0-24 h) to establish a septic AKI model in vitro. Before LPS administration, HK-2 cells were transfected either with vectors or siRNA against Hsp27, and the changes in cell viability and apoptotic cells rate were assessed using CCK-8 and flow cytometry. The expression changes in apoptosis-related proteins, proinflammatory cytokines and chemokine, as well as main factors in NF-κB and JNK pathways were mainly determined by Western blotting. Besides, the relationship between Hsp27 and Bcl-2 was detected by co-immunoprecipitation. Results: LPS remarkably damaged HK-2 cells by reduction of cell viability, induction of apoptosis, and stimulation of proinflammatory cytokines and chemokine release. Hsp27 overexpression significantly impaired LPS-induced damage in HK-2 cells. Hsp27 overexpression couldn’t alter the mRNA level of Bcl-2, but could interact with Bcl-2 at an endogenous level. Both NF-κB and JNK pathways were activated by LPS, while were blocked in Hsp27-overexpressing cells. Conclusion: Hsp27 overexpression conferred a survival advantage to LPS-injured HK-2 cells by controlling cell viability, apoptosis and inflammation, possibly via interaction with Bcl-2 and modulation of NF-κB and JNK pathways.

scholarly journals Expression profiles of heat shock protein 27 and αB-crystallin and their effects on heat-stressed rat myocardial cells in vitro and in vivo

2015 ◽  
Vol 13 (2) ◽  
pp. 1633-1638 ◽  
Author(s):  
SHU TANG ◽  
HONGBO CHEN ◽  
YANFEN CHENG ◽  
MOHAMMAD ABDEL NASIR ◽  
NICOLE KEMPER ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Expression Profiles ◽  
Heat Shock Protein 27 ◽  
Myocardial Cells ◽  
Αb Crystallin

Effect of heat shock protein 27 on the in vitro degradation of myofibrils by caspase‐3 and μ‐calpain

2017 ◽  
Vol 53 (1) ◽  
pp. 121-128 ◽  
Author(s):  
Zhenjiang Ding ◽  
Feng Huang ◽  
Chunjiang Zhang ◽  
Liang Zhang ◽  
Hongxia Sun ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Caspase 3 ◽  
Heat Shock Protein 27 ◽  
In Vitro Degradation

Cholecystokinin stimulates heat shock protein 27 phosphorylation in rat pancreas both in vivo and in vitro

1997 ◽  
Vol 112 (4) ◽  
pp. 1354-1361 ◽  
Author(s):  
GE Groblewski ◽  
T Grady ◽  
N Mehta ◽  
H Lambert ◽  
CD Logsdon ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Heat Shock Protein 27 ◽  
Rat Pancreas
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