Tracking the Dynamic Histone Methylation of H3K27 in Live Cancer Cells

ACS Sensors ◽  
2021 ◽  
Author(s):  
Ya Gong ◽  
Chujun Wei ◽  
Leonardo Cheng ◽  
Fengyi Ma ◽  
Shaoying Lu ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Histone Methylation

scholarly journals Direct regulation of E-cadherin by targeted histone methylation of TALE-SET fusion protein in cancer cells

Oncotarget ◽  
2015 ◽  
Vol 6 (27) ◽  
pp. 23837-23844 ◽  
Author(s):  
Hyun-Soo Cho ◽  
Jeong Gu Kang ◽  
Jae-Hye Lee ◽  
Jeong-Ju Lee ◽  
Seong Kook Jeon ◽  
...  
Keyword(s):  
Fusion Protein ◽  
Cancer Cells ◽  
Histone Methylation ◽  
Direct Regulation ◽  
E Cadherin

UHRF1-KAT7-mediated regulation of TUSC3 expression via histone methylation/acetylation is critical for the proliferation of colon cancer cells

Oncogene ◽  
2019 ◽  
Vol 39 (5) ◽  
pp. 1018-1030 ◽  
Author(s):  
Kenzui Taniue ◽  
Tomoatsu Hayashi ◽  
Yuki Kamoshida ◽  
Akiko Kurimoto ◽  
Yasuko Takeda ◽  
...  
Keyword(s):  
Colon Cancer ◽  
Cancer Cells ◽  
Histone Methylation ◽  
Colon Cancer Cells

scholarly journals ASXL2 promotes proliferation of breast cancer cells by linking ERα to histone methylation

Oncogene ◽  
2015 ◽  
Vol 35 (28) ◽  
pp. 3742-3752 ◽  
Author(s):  
U-H Park ◽  
M-R Kang ◽  
E-J Kim ◽  
Y-S Kwon ◽  
W Hur ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cells ◽  
Histone Methylation ◽  
Breast Cancer Cells

scholarly journals Exosomal lncRNA UCA1 Derived From Pancreatic Stellate Cells Promotes Gemcitabine Resistance in Pancreatic Cancer via the SOCS3/EZH2 Axis

2021 ◽  
Vol 11 ◽  
Author(s):  
Yuan Chi ◽  
He Xin ◽  
Zhaoyu Liu
Keyword(s):  
Pancreatic Cancer ◽  
Cancer Cells ◽  
Mtt Assay ◽  
Histone Methylation ◽  
Methylation Level ◽  
Stellate Cells ◽  
Pancreatic Stellate Cells ◽  
Gene Region ◽  
Cancer Resistance ◽  
Pancreatic Cancer Cells

ObjectivePancreatic cancer is associated with poor prognosis and dismal survival rates. This study aims to investigate roles of lncRNA UCA1-loaded exosomes secreted by pancreatic stellate cells (PSCs) in Gemcitabine (Gem) resistance of pancreatic cancer under hypoxia, which involves the methylation of SOCS3 and EZH2 recruitment.MethodsThe exosomes were isolated from PSCs and hypoxic PSCs (HPSCs), and co-cultured with pancreatic cancer cells transduced with manipulated lncRNA UCA1, EZH2, and SOCS3. The interaction among lncRNA UCA1, EZH2, and SOCS3 was characterized by RIP and ChIP assays. Next, MTT assay, flow cytometry and TUNEL staining and Transwell assay were used to detect cell viability, apoptosis, invasion, and migration. Gem-resistant pancreatic cancer cell line (GemMIA-R3) was established, which was applied in a mouse xenograft model of pancreatic cancer, with MTT assay to determine Gem sensitivity.ResultsLncRNA UCA1 was highly expressed, while SOCS3 was poorly expressed in pancreatic cancer tissues. Hypoxia induced activation of PSCs and promoted release of exosomes. LncRNA UCA1 delivered by hypoxic PSC-derived exosomes (HPSC-EXO) regulated histone methylation level in SOCS3 gene region through recruitment of EZH2. In vitro and in vivo experimental results confirmed that lncRNA UCA1-loaded HPSC-EXO promoted malignant phenotypes, inhibited apoptosis, and promoted Gem resistance of pancreatic cancer cells as well as tumorigenesis in mice.ConclusionUnder hypoxic conditions, exosomes secreted by hypoxia-induced PSCs deliver lncRNA UCA1 into pancreatic cancer cells, where lncRNA UCA1 recruits EZH2 and regulates histone methylation level in SOCS3 gene region, thereby augmenting pancreatic cancer resistance to Gem.

scholarly journals Sulforaphane influences histone methylation in advanced prostate cancer cells (1045.15)

2014 ◽  
Vol 28 (S1) ◽  
Author(s):  
G Watson ◽  
S Wickramasekara ◽  
Z Palomera‐Sanchez ◽  
C Black ◽  
C Maier ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Histone Methylation ◽  
Advanced Prostate Cancer ◽  
Prostate Cancer Cells

scholarly journals A Key Silencing Histone Mark on Chromatin Is Lost When Colorectal Adenocarcinoma Cells Are Depleted of Methionine by Methionine γ-Lyase

2021 ◽  
Vol 8 ◽  
Author(s):  
Samanta Raboni ◽  
Serena Montalbano ◽  
Stephanie Stransky ◽  
Benjamin A. Garcia ◽  
Annamaria Buschini ◽  
...  
Keyword(s):  
Cancer Cells ◽  
Histone Methylation ◽  
Colorectal Adenocarcinoma ◽  
Cancer Cell Line ◽  
Histone Mark ◽  
Systemic Delivery ◽  
Total Histone ◽  
Major Satellite

Methionine is an essential amino acid used, beyond protein synthesis, for polyamine formation and DNA/RNA/protein methylation. Cancer cells require particularly high methionine supply for their homeostasis. A successful approach for decreasing methionine concentration is based on the systemic delivery of methionine γ-lyase (MGL), with in vitro and in vivo studies demonstrating its efficacy in cancer therapy. However, the mechanisms explaining how cancer cells suffer from the absence of methionine more significantly than non-malignant cells are still unclear. We analyzed the outcome of the human colorectal adenocarcinoma cancer cell line HT29 to the exposure of MGL for up to 72 h by monitoring cell viability, proteome expression, histone post-translational modifications, and presence of spurious transcription. The rationale of this study was to verify whether reduced methionine supply would affect chromatin decondensation by changing the levels of histone methylation and therefore increasing genomic instability. MGL treatment showed a time-dependent cytotoxic effect on HT29 cancer cells, with an IC50 of 30 µg/ml, while Hs27 normal cells were less affected, with an IC50 of >460 µg/ml. Although the levels of total histone methylation were not altered, a loss of the silencing histone mark H3K9me2 was observed, as well as a decrease in H4K20me3. Since H3K9me2/3 decorate repetitive DNA elements, we proved by qRT-PCR that MGL treatment leads to an increased expression of major satellite units. Our data indicate that selected histone methylation marks may play major roles in the mechanism of methionine starvation in cancer cells, proving that MGL treatment directly impacts chromatin homeostasis.

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