The Prognostic Value of AT-Rich Interaction Domain (ARID) Family Members in Patients with Hepatocellular Carcinoma

Li, Siyi; Wu, Zhulin; Li, Qiuyue; Liang, Qiting; Zhou, Hengli; Shi, Yafei; Zhang, Rong; Pan, Huafeng

doi:10.1155/2022/1150390

Cited by 5 publications

(2 citation statements)

References 57 publications

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“…BAF plays role in remodelling chromatin structure by removing or deleting nucleosomes to create the space for transcription factor binding, which is crucial for gene regulation [ 3 , 4 ]. ARID1A gene also serves as a tumor suppressor and is frequently mutated in several cancers, including bladder [ 5 ], hepatic [ 6 ], colorectal [ 7 ] and renal [ 8 ] cancers. Besides, the decreased ARID1A expression correlates with the poor outcome of cancers [ 9 , 10 ].…”

Section: Introductionmentioning

confidence: 99%

Identification and characterization of ARID1A-interacting proteins in renal tubular cells and their molecular regulation of angiogenesis

Yoodee,

Peerapen,

Plumworasawat

et al. 2023

J Transl Med

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Background Defects and deficiency of AT-rich interactive domain-containing protein 1A (ARID1A) encoded by a tumor suppressor gene ARID1A have recently been suggested to get involved in angiogenesis, a crucial process in carcinogenesis. However, molecular mechanisms of ARID1A deficiency to induce angiogenesis in kidney cancer remain underinvestigated. Methods We performed large-scale identification of ARID1A protein interactors in renal tubular epithelial cells (RTECs) using immunoprecipitation (IP) followed by nanoLC-ESI-LTQ-Orbitrap tandem mass spectrometry (MS/MS). Their roles in angiogenesis were investigated using various assays. Results A total of 74 ARID1A-interacting proteins were identified. Protein–protein interactions analysis revealed that these identified proteins interacted directly or indirectly with ARID1A. Among them, the direct interaction between ARID1A and β-actin was validated by IP and reciprocal IP followed by Western blotting. Small interfering RNA (siRNA) was used for single and double knockdowns of ARID1A and ACTB. Semi-quantitative RT-PCR demonstrated that deficiency of ARID1A, but not ACTB, significantly affected expression of angiogenesis-related genes in RTECs (VEGF and FGF2 were increased, whereas PDGF and EGF were decreased). However, the knockdowns did not affect TGFB1 and FGF1 levels. The quantitative mRNA expression data of VEGF and TGFB1 were consistent with the secreted levels of their protein products as measured by ELISA. Only secreted products derived from ARID1A-deficient RTECs significantly increased endothelial cells (ECs) migration and tube formation. Some of the other carcinogenic features could also be confirmed in the ARID1A-deficient RTECs, including increased cell migration and chemoresistance. Double knockdowns of both ARID1A and ACTB did not enhance the effects of single ARID1A knockdown in all assays. Conclusions We report herein a large dataset of the ARID1A-interacting proteins in RTECs using an IP-MS/MS approach and confirm the direct interaction between ARID1A and β-actin. However, the role of ARID1A deficiency in angiogenesis is independent of β-actin.

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Section: Introductionmentioning

confidence: 99%

Identification and characterization of ARID1A-interacting proteins in renal tubular cells and their molecular regulation of angiogenesis

Yoodee,

Peerapen,

Plumworasawat

et al. 2023

J Transl Med

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“…Chen et al described the function of KDM5D in the development of cisplatin [CDDP, abbreviation for cisdiamino-dichloroplatinum (II)] tolerance in head and neck squamous cell carcinoma (HNSCC) (32). Decreased KDM5D expression was also observed in gastric, colorectal, and hepatocellular carcinomas (33)(34)(35). Moreover, in an analysis of the TCGA database, Duan et al showed that KDM5D was signi cantly downregulated in 24 different cancer types (e.g., breast, pancreatic, or prostate cancer) compared with adjacent tissues (36).…”

Section: Introductionmentioning

confidence: 99%

The Role of Kdm5d in the Development of Chemoresistance to Cisplatin Through Cul4a in Neuroblastoma

Podhorska,

Hrabeta,

Belhajova

et al. 2023

Preprint

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Chemoresistance is a major cause of cancer therapy failure. Increasing evidence points to the importance of histone lysine demethylase function, whose dysregulation has been described in many cancers. KDM5, a family of histone lysine demethylases, may play a critical role in downregulation of tumour-suppressors or upregulation of oncogenes and in the development of drug tolerance. In this study, we examined the expression of KDM5D in cell lines derived from high-risk neuroblastoma. We found that KDM5D expression was lost in all cisplatin-chemoresistant neuroblastoma cell lines compared with sensitive parental cells. In addition, we found that the cisplatin-chemoresistant neuroblastoma cell line had increased expression of the ubiquitin ligase cullin 4A (CUL4A) compared with the sensitive parental cells. CUL4A plays a role in cellular processes and its aberrant regulation has been observed in a number of cancers. We have shown that silencing of KDM5D causes a more aggressive phenotype of NBL by promoting cell proliferation and migration, evading cell death, promoting S phase of the cell cycle, and desensitizing sensitive cells to CDDP via the gene CUL4A. In addition, ectopic expression of KMD5D in a cisplatin-resistant cell line reversed these phenomena. Our results suggest that KDM5D and / or CUL4A may be a biomarkers of chemoresistance to cisplatin and a potential therapeutic target in NBL.

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Domain architecture and protein–protein interactions regulate KDM5A recruitment to the chromatin

Kataria,

Tyagi

2023

Epigenetics

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Tri-methylation of Histone 3 lysine 4 (H3K4) is an important epigenetic modification whose deposition and removal can affect the chromatin at structural and functional levels. KDM5A is one of the four known H3K4-specific demethylases. It is a part of the KDM5 family, which is characterized by a catalytic Jumonji domain capable of removing H3K4 di- and tri-methylation marks. KDM5A has been found to be involved in multiple cellular processes such as differentiation, metabolism, cell cycle, and transcription. Its link to various diseases, including cancer, makes KDM5A an important target for drug development. However, despite several studies outlining its significance in various pathways, our lack of understanding of its recruitment and function at the target sites on the chromatin presents a challenge in creating effective and targeted treatments. Therefore, it is essential to understand the recruitment mechanism of KDM5A to chromatin, and its activity therein, to comprehend how various roles of KDM5A are regulated. In this review, we discuss how KDM5A functions in a context-dependent manner on the chromatin, either directly through its structural domain, or through various interacting partners, to bring about a diverse range of functions.

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The Prognostic Value of AT-Rich Interaction Domain (ARID) Family Members in Patients with Hepatocellular Carcinoma

Cited by 5 publications

References 57 publications

Identification and characterization of ARID1A-interacting proteins in renal tubular cells and their molecular regulation of angiogenesis

Identification and characterization of ARID1A-interacting proteins in renal tubular cells and their molecular regulation of angiogenesis

The Role of Kdm5d in the Development of Chemoresistance to Cisplatin Through Cul4a in Neuroblastoma

Domain architecture and protein–protein interactions regulate KDM5A recruitment to the chromatin

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