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 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 Angiopoietin1 Deficiency in Hepatocytes Affects the Growth of Colorectal Cancer Liver Metastases (CRCLM)

Cancers ◽  
2019 ◽  
Vol 12 (1) ◽  
pp. 35
Author(s):  
Nisreen S. Ibrahim ◽  
Anthoula Lazaris ◽  
Miran Rada ◽  
Stephanie K. Petrillo ◽  
Laurent Huck ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Colon Cancer ◽  
Liver Metastases ◽  
Poor Response ◽  
Growth Patterns ◽  
Migration And Invasion ◽  
Colorectal Cancer Liver Metastases ◽  
Angiogenic Therapy ◽  
Tumor Region

Colorectal cancer liver metastases (CRCLM) that receive their blood supply via vessel co-option are associated with a poor response to anti-angiogenic therapy. Angiopoietins (Ang1 and Ang2) with their Tyrosine-protein kinase receptor (Tie2) have been shown to support vessel co-option. We demonstrate significantly higher expression of Ang1 in hepatocytes adjacent to the tumor region of human chemonaïve and treated co-opting (replacement histopathological growth patterns: RHGP) tumors. To investigate the role of the host Ang1 expression, Ang1 knockout (KO) mice were injected intra-splenically with metastatic MC-38 colon cancer cells that develop co-opting liver metastases. We observed a reduction in the number of liver metastases and interestingly, for the first time, the development of angiogenic driven desmoplastic (DHGP) liver metastases. In addition, in-vitro, knockout of Ang1 in primary hepatocytes inhibited viability, migration and invasion ability of MC-38 cells. We also demonstrate that Ang 1 alone promotes the migration and growth of both human and mouse colon cancer cell lines These results provide evidence that high expression of Ang1 in the host liver is important to support vessel co-option (RHGP lesions) and when inhibited, favours the formation of angiogenic driven liver metastases (DHGP lesions).

scholarly journals Suppression of heat shock protein 27 expression promotes 5-fluorouracil sensitivity in colon cancer cells in a xenograft model

2012 ◽  
Vol 28 (4) ◽  
pp. 1269-1274 ◽  
Author(s):  
RYOHEI HAYASHI ◽  
YOSHIYUKI ISHII ◽  
HIROKI OCHIAI ◽  
ATSUSHI MATSUNAGA ◽  
TAKASHI ENDO ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Xenograft Model ◽  
Heat Shock Protein 27 ◽  
Colon Cancer Cells

Heat shock protein 27 is associated with irinotecan resistance in human colorectal cancer cells

FEBS Letters ◽  
2007 ◽  
Vol 581 (8) ◽  
pp. 1649-1656 ◽  
Author(s):  
Dae Hwa Choi ◽  
Jin Sook Ha ◽  
Won Hyuck Lee ◽  
Jeong Kee Song ◽  
Gyu Yeol Kim ◽  
...  
Keyword(s):  
Colorectal Cancer ◽  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Heat Shock Protein 27 ◽  
Human Colorectal Cancer ◽  
Colorectal Cancer Cells ◽  
Human Colorectal Cancer Cells

Effect of Heat Shock Protein 90 (Hsp90) on Migration and Invasion of Human Cancer Cells in Vitro

2014 ◽  
Vol 157 (4) ◽  
pp. 476-478 ◽  
Author(s):  
A. V. Snigireva ◽  
V. V. Vrublevskaya ◽  
Yu. Yu. Skarga ◽  
Yu. V. Evdokimovskaya ◽  
O. S. Morenkov
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Cancer Cells ◽  
Human Cancer ◽  
Heat Shock Protein 90 ◽  
Migration And Invasion ◽  
Human Cancer Cells

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.

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