MBD2

Last update 08 May 2025

Basic Info

Synonyms

Demethylase, DMTase, MBD2

+ [3]

Introduction

Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides (PubMed:9774669). Binds hemimethylated DNA as well (PubMed:10947852, PubMed:24307175). Recruits histone deacetylases and DNA methyltransferases to chromatin (PubMed:10471499, PubMed:10947852). Acts as a component of the histone deacetylase NuRD complex which participates in the remodeling of chromatin (PubMed:16428440, PubMed:28977666). Acts as a transcriptional repressor and plays a role in gene silencing (PubMed:10471499, PubMed:10947852, PubMed:16415179). Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression (PubMed:16415179). May enhance the activation of some unmethylated cAMP-responsive promoters (PubMed:12665568).

100 Clinical Results associated with MBD2

100 Translational Medicine associated with MBD2

0 Patents (Medical) associated with MBD2

982

Literatures (Medical) associated with MBD2

31 Dec 2025·Annals of Medicine

The methyl-CpG binding domain 2 regulates peptidylarginine deiminase 4 expression and promotes neutrophil extracellular trap formation via the Janus kinase 2 signaling pathway in experimental severe asthma

Article

Author: Peng, Biao ; Xiang, Xu-Dong ; Liu, Da ; Sun, Fei ; Yan, Mu-Yun ; Chen, Yun-Rong

OBJECTIVEThe prognosis for severe asthma is poor, and the current treatment options are limited. The methyl-CpG binding domain protein 2 (MBD2) participates in neutrophil-mediated severe asthma through epigenetic regulation. Neutrophil extracellular traps (NETs) play a critical role in the pathogenesis of severe asthma. This study aims to detect if MBD2 can reduce NETs formation and the potential mechanism in severe asthma.METHODSA severe asthma model was established in C57BL/6 wild-type mice exposure to house dust mite (HDM), ovalbumin (OVA), and lipopolysaccharide (LPS). Enzyme-linked immunosorbent assay was used to measure the concentrations of IL-4, IL-17A, and IFN-γ in lung tissues. Flow cytometry was employed to determine the percentages of Th2, Th17, and Treg cells in lung tissues. Quantitative real-time polymerase chain reaction was utilized to assess the mRNA expression levels of MBD2, JAK2, and PAD4. Western blotting and immunofluorescence were conducted to detect the protein of MBD2, JAK2, PAD4, and CitH3. HL-60 cells were differentiated into neutrophil-like cells by culturing in a medium containing dimethyl sulfoxide and then stimulated with LPS. KCC-07, Ruxolitinib, and Cl-amidine were used to inhibit the expressions of MBD2, JAK2, and PAD4, respectively.RESULTSSevere asthma mice were characterized by pulmonary neutrophilic inflammation and increased formation of neutrophil extracellular traps (NETs). The expression of MBD2, JAK2, and PAD4 was elevated in severe asthma mice. Inhibiting the expression of MBD2, JAK2, and PAD4 reduced NETs formation and decreased airway inflammation scores, total cell counts and neutrophil counts in BALF, and percentage of Th2 and Th17 cell in lung tissues, whereas increasing Treg cell counts. In both severe asthma mice and HL-60-differentiated neutrophil-like cells in vitro, inhibiting MBD2 reduced the mRNA and protein expression of JAK2 and PAD4, and inhibiting JAK2 reduced the expression of PAD4 mRNA and protein.CONCLUSIONMBD2 regulates PAD4 expression through the JAK2 signaling pathway to promote NETs formation in mice with severe asthma. Further bench-based and bedside-based studies targeting the MBD2, PAD4, and JAK2 signaling pathways will help open new avenues for drug development of severe asthma.

31 Dec 2025·Gut Microbes

Novel role of FTO in regulation of gut–brain communication via Desulfovibrio fairfieldensis -produced hydrogen sulfide under arsenic exposure

Article

Author: Zhou, Lixiao ; Chen, Chengzhi ; Jiang, Xuejun ; Wang, Ruonan ; Zhang, Hongyang ; Lv, Bo ; Chen, Ruonan ; Zhao, Feng ; Zhou, Tianxiu ; Qiu, Jingfu ; Zou, Zhen ; Mao, Lejiao ; Tian, Xin ; Zhang, Jun ; Chai, Xiaoqin ; Hu, Jun ; Zhang, Yunxiao ; Xia, Yinyin

Fat mass and obesity-associated protein (FTO) is the key demethylase that reverses the abnormally altered N6-methyladenosine (m6A) modification in eukaryotic cells under environmental pollutants exposure. Arsenic is an environmental metalloid and can cause severe symptoms in human mainly through drinking water. However, there is no specific treatment for its toxic effects due to the uncovered mechanisms. We previously revealed that exposure to arsenic increased the level of m6A via down-regulation of FTO, which might serve as a potential target for intervention against arsenic-related disorders. In this study, our results demonstrated that chronic exposure to arsenic significantly disrupted the intestinal barrier and microenvironment. Also, this administration resulted in the enhancement of m6A modification and the reduction of FTO expression in the intestine. By using both CRISPR/Cas9-based FTO knock-in strategy and adeno-associated virus (AAV)-mediated overexpression of FTO in the intestine, we established for the first time that up-regulation of FTO remarkably ameliorated arsenic-induced disruption of intestinal barriers and altered microenvironment of mice. We also firstly identified a dominant gut microbial species, Desulfovibrio fairfieldensis, which was sharply reduced in arsenic-exposed mice, was able to proceed arsenic-induced neurobehavioral impairments by declining the levels of its major metabolite hydrogen sulfide. Administration of Desulfovibrio fairfieldensis could significantly alleviate the neurotoxicity of arsenic. Intriguingly, the beneficial effects of FTO against arsenic neurotoxicity possibly occurred through a novel gut-brain communication via Desulfovibrio fairfieldensis and its produced hydrogen sulfide. Collectively, these findings will provide new ideas for understanding the mechanisms of arsenic-induced toxic effects from a gut-brain communication perspective, and will assist the development of explicit intervention strategy via regulation of a new potential target FTO for prevention and treatment against arsenic-related both intestinal and neurological disorders.

01 Dec 2025·Molecular Biology Reports

Versatile functions of methyl-CpG-binding domain 2 (MBD2) in cellular characteristics and differentiation

Review

Author: Koca, Kasım Kağan ; Kugu, Gizem ; Lekesiz, Rabia Tuana ; Çalışkaner, Zihni Onur

Cellular differentiation is a vital process that results in cell specialization and functionalization, synchronized with the development and growth in multicellular organisms. Any fault in this process can bring about the emergence of various diseases. Gene expression controls cellular differentiation, but various epigenetic mechanisms play a pivotal role as well. For instance, DNA methylation and combined histone modifications, such as histone acetylation/deacetylation, are crucial in cellular differentiation. Methyl-CpG-Binding Domain 2 (MBD2), a highly conserved member of the MBD protein family, is considered a reader of DNA methylation and drives the crosstalk between DNA methylation and histone deacetylation. It can functionally recruit the nucleosome remodeling and deacetylase (NuRD) complex to the CpG-methylated promoters of the genes, which will be silenced during the cell fate determination. This review focuses on the cell-specific functions of MBD2 isoforms (MBD2a, MBD2b, and MBD2c(t)) in cellular differentiation, reprogramming, and the immune system. Furthermore, the relevance between MBD2 and certain cancers was discussed for the first time in this paper. Thus, we provide a comprehensive review about the significance of MBD2 in various cellular mechanisms.

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MBD2

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