Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Exposure of human cholangiocytes to 1,2-dichloropropane in the presence of macrophages induces base-excision repair-related genes in vitro

ABSTRACT: Exposure of human cholangiocytes to 1,2-dichloropropane in the presence of macrophages induces base-excision repair-related genes in vitro

PROVIDER: PRJNA817201 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR18369410.fastq.gz	Fastqsanger.gz
	SRR18369411.fastq.gz	Fastqsanger.gz
	SRR18369412.fastq.gz	Fastqsanger.gz
	SRR18369413.fastq.gz	Fastqsanger.gz
	SRR18369414.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 18

Similar Datasets

Exposure of human cholangiocytes to 1,2-dichloropropane in the presence of macrophages induces base-excision repair-related genes in vitro

Project description:1,2-dichloropropane (1,2-DCP), a synthetic organic solvent, has been implicated in causality of cholangiocarcinoma. 1,2-DCP from Group 3 to Group 1. 1,2-DCP-induced occupational cholangiocarcinoma show a different carcinogenic process compared to common cholangiocarcinoma. However, the mechanism of 1,2-DCP induced carcinogenicity in cholangiocytes remains elusive. We reported previously that exposure of MMNK-1 cholangiocytes co-cultured with THP-1 macrophages, but not monocultured MMNK-1 cholangiocytes to 1,2-DCP induced activation-induced cytidine deaminase (AID) expression, DNA damage and ROS production. The aim of this study was to identify relevant biological processes or target genes expressed in response to 1,2-DCP, using an in vitro system where cholangiocytes are co-cultured with macrophages. The co-cultured cells were exposed to 1,2-DCP at 0, 0.1, and 0.4 mM for 24 hours and the cell lysates, assessed by transcriptome analysis. 1,2-DCP upregulated the expression of base excision repair genes in MMNK-1 cholangiocytes in the co-cultures, whereas it upregulated the expression of cell cycle-related genes in THP-1 macrophages. Activation of the base excision repair pathway might result from the previously observed DNA damage in MMNK-1 cholangiocytes co-cultured with THP-1 macrophages. Cross talk interactions between cholangiocytes and macrophages could explain the observed increase in DNA damage in the cholangiocytes.

2025-03-17 | GSE198858 | GEO

Transcription profiling of S. cerevisiae with modulated expression of base excision repair players

Project description:We are investigating the transcriptional response of yeast to modulation of the expression of base excision repair players, these generate different dna lesions of abasic sites of strand breaks; We used microarrays to detail the global programme of gene expression underlying the DNA damage response in yeast Experiment Overall Design: Yeaststrains with different expression levels of players in base excision repair (in biological triplicate) were grown to mid log phase. The expression responses were compared to each other and we have deciphered a gene expression profile that is specific for DNA damage in yeast.

2008-06-16 | E-GEOD-9295 | biostudies-arrayexpress

Lamin A/C promotes DNA base excision repair

Project description:Lamin A/C promotes DNA base excision repair

| PRJNA512097 | ENA

Expression data from yeast with modulated expression of base excision repair players

2007-11-30 | GSE9295 | GEO

Lamin A/C promotes DNA base excision repair (mouse arrays)

Project description:Lamin A/C promotes DNA base excision repair (mouse arrays)

| PRJNA492926 | ENA

Lamin A/C promotes DNA base excision repair (human arrays)

Project description:Lamin A/C promotes DNA base excision repair (human arrays)

| PRJNA512096 | ENA

Acetylation of p62 regulates base excision repair through interaction with APE1

Project description:p62, a well-known adaptor of autophagy, plays multiple functions in response to various stresses. Here, we report a function for p62 in base excision repair that is distinct from its known functions. Loss of p62 impairs BER capacity and increases the sensitivity of cancer cells to alkylating and oxidizing agents. In response to alkylative and oxidative damage, p62 is accumulated in the nucleus，acetylated by hMOF， deacetylated by SIRT7, and acetylated p62 is recruited to chromatin. The chromatin-enriched p62 directly interacts with APE1, a key enzyme of the BER pathway, and promotes its endonuclease activity, which facilitates BER and cell survival. Collectively, our findings demonstrate that p62 is a regulator of BER, and provide further rationale for targeting p62 as a cancer therapeutic strategy.

2022-07-19 | PXD034899 | Pride

Acetylation of p62 regulates base excision repair through interaction with APE1

2022-07-19 | PXD034901 | Pride

Covalent PARylation of DNA base excision repair proteins regulates DNA demethylation

Project description:Covalent PARylation of DNA base excision repair proteins regulates DNA demethylation

| PRJNA702477 | ENA

PARP1 gene knockout suppresses expression of DNA Base Excision Repair genes

Project description:PARP1 gene knockout suppresses expression of DNA Base Excision Repair genes

| PRJNA906061 | ENA