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Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [thyroid]

ABSTRACT: Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [thyroid]

PROVIDER: PRJNA482447 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR7583890.fastq.gz	Fastqsanger.gz
	SRR7583891.fastq.gz	Fastqsanger.gz
	SRR7583892.fastq.gz	Fastqsanger.gz
	SRR7583893.fastq.gz	Fastqsanger.gz
	SRR7583894.fastq.gz	Fastqsanger.gz

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Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition

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Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [thyroid]

Project description:This study assessed tumor suppressor roles of CREBBP in SCLC and other neuroendocrine tumors. Genetically engineered mouse models were used to determine the tumor suppressor role of Crebbp in SCLC and other neuroendocrine tumors.

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Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [pituitary tumor]

Project description:Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [pituitary tumor]

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Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [preSC cell line]

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Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [SCLC]

2018-10-17 | GSE117547 | GEO

Crebbp loss drives small cell lung cancer and increases sensitivity to HDAC inhibition [pituitary tumor]

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CREBBP cooperates with cell cycle machinery to attenuate chidamide sensitivity in relapsed/refractory DLBCL

Project description:Frequent inactivating mutations of histone acetyltransferase CREBBP is a characteristic feature of diffuse large B-cell lymphoma (DLBCL), highlighting the attractiveness of targeting the CREBBP deficiency as a therapeutic strategy. In this study, we demonstrate that chidamide, a novel histone deacetylase (HDAC) inhibitor, is effective in treating a subgroup of relapsed/refractory DLBCL patients, achieving an overall response rate (ORR) of 25.0% and a complete response (CR) rate of 15.0%. However, the clinical response to chidamide remains poor as most patients exhibit resistance, hampering the clinical utility of the drug. Functional studies in both in vitro and in vivo models showed that CREBBP loss of function is correlated with chidamide sensitivity, which is associated with modulating cell cycle machinery. A combinatorial drug screening of 130 kinase inhibitors targeting cell cycle regulators identified AURKA inhibitors, which inhibited G2/M transition during cell cycling, as top candidates that synergistically enhanced antitumor effects of chidamide in CREBBP-proficient DLBCL cells. Our study demonstrated that CREBBP inactivation can serve as a potential biomarker to predict chidamide sensitivity, while a combination of AURKA inhibitor and chidamide provides a novel therapeutic strategy for the treatment of relapsed/refractory DLBCL.

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<i>Crebbp</i> Loss Drives Small Cell Lung Cancer and Increases Sensitivity to HDAC Inhibition.

Project description:CREBBP, encoding an acetyltransferase, is among the most frequently mutated genes in small cell lung cancer (SCLC), a deadly neuroendocrine tumor type. We report acceleration of SCLC upon Crebbp inactivation in an autochthonous mouse model. Extending these observations beyond the lung, broad Crebbp deletion in mouse neuroendocrine cells cooperated with Rb1/Trp53 loss to promote neuroendocrine thyroid and pituitary carcinomas. Gene expression analyses showed that Crebbp loss results in reduced expression of tight junction and cell adhesion genes, including Cdh1, across neuroendocrine tumor types, whereas suppression of Cdh1 promoted transformation in SCLC. CDH1 and other adhesion genes exhibited reduced histone acetylation with Crebbp inactivation. Treatment with the histone deacetylase (HDAC) inhibitor Pracinostat increased histone acetylation and restored CDH1 expression. In addition, a subset of Rb1/Trp53/Crebbp-deficient SCLC exhibited exceptional responses to Pracinostat in vivo Thus, CREBBP acts as a potent tumor suppressor in SCLC, and inactivation of CREBBP enhances responses to a targeted therapy.Significance: Our findings demonstrate that CREBBP loss in SCLC reduces histone acetylation and transcription of cellular adhesion genes, while driving tumorigenesis. These effects can be partially restored by HDAC inhibition, which exhibited enhanced effectiveness in Crebbp-deleted tumors. These data provide a rationale for selectively treating CREBBP-mutant SCLC with HDAC inhibitors. Cancer Discov; 8(11); 1422-37. ©2018 AACR. This article is highlighted in the In This Issue feature, p. 1333.

| S-EPMC6294438 | biostudies-literature

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