Repression of Cell Cycle Progression by Antisense HMG2 RNA

Yamazaki, Fuminori; Nagatsuka, Yasuko; Shirakawa, Hitoshi; Yoshida, Michiteru

doi:10.1006/bbrc.1995.1762

Cited by 19 publications

(15 citation statements)

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“…5E). This observation is in agreement with data from COS-1 cells, in which Hmgb2 knockdown suppresses cell division (46). Furthermore, the cell type-specific lethality of Ctcf levels is also in agreement with data showing that Ctcf knockout is embryonic lethal in mice (47,48).…”

Section: 6supporting

confidence: 91%

Reciprocal Regulation of the Cardiac Epigenome by Chromatin Structural Proteins Hmgb and Ctcf

Monte

Rosa‐Garrido

Karbassi

et al. 2016

Journal of Biological Chemistry

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Transcriptome remodeling in heart disease occurs through the coordinated actions of transcription factors, histone modifications, and other chromatin features at pathology-associated genes. The extent to which genome-wide chromatin reorganization also contributes to the resultant changes in gene expression remains unknown. We examined the roles of two chromatin structural proteins, Ctcf (CCCTC-binding factor) and Hmgb2 (high mobility group protein B2), in regulating pathologic transcription and chromatin remodeling. Our data demonstrate a reciprocal relationship between Hmgb2 and Ctcf in controlling aspects of chromatin structure and gene expression. Both proteins regulate each others' expression as well as transcription in cardiac myocytes; however, only Hmgb2 does so in a manner that involves global reprogramming of chromatin accessibility. We demonstrate that the actions of Hmgb2 on local chromatin accessibility are conserved across genomic loci, whereas the effects on transcription are loci-dependent and emerge in concert with histone modification and other chromatin features. Finally, although both proteins share gene targets, Hmgb2 and Ctcf, neither binds these genes simultaneously nor do they physically colocalize in myocyte nuclei. Our study uncovers a previously unknown relationship between these two ubiquitous chromatin proteins and provides a mechanistic explanation for how Hmgb2 regulates gene expression and cellular phenotype. Furthermore, we provide direct evidence for structural remodeling of chromatin on a genome-wide scale in the setting of cardiac disease.

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Section: 6supporting

confidence: 91%

Reciprocal Regulation of the Cardiac Epigenome by Chromatin Structural Proteins Hmgb and Ctcf

Monte

Rosa‐Garrido

Karbassi

et al. 2016

Journal of Biological Chemistry

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“…First, HMGB2 is necessary for cell survival, proliferation and growth signal transduction to nucleus. HMGB2 inhibition by antisense RNA repressed cell cycle progression in COS-1 cells 34 and HMGB2 knockdown by siRNA inhibited cell proliferation in rat HCC cells. 16 Additionally, IHC study of HCC showed that positivity of HMGB2 was correlated with PCNA, a known marker of cell proliferation.…”

Section: Methodsmentioning

confidence: 95%

High-mobility group box 2 (HMGB2) modulates radioresponse and is downregulated by p53 in colorectal cancer cell

Shin

Kim

et al. 2012

Cancer Biology & Therapy

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“…The amount of HMG2 protein parallels the proliferative activity of cells in various organs [30]. The level of HMG2 mRNA is enhanced in cells transformed with various viral genes [31], and cell growth is repressed by expression of antisense HMG2 RNA [31]. These findings indicate that HMG2 protein must be closely related to cell proliferation.…”

Section: Discussionmentioning

confidence: 99%

Novel autoantigens of perinuclear anti-neutrophil cytoplasmic antibodies (P-ANCA) in ulcerative colitis: non-histone chromosomal proteins, HMG1 and HMG2

Sobajima

Ozaki

Osakada

et al. 1997

Clinical and Experimental Immunology

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SUMMARYAnti-neutrophil cytoplasmic antibodies (ANCA) in sera from ulcerative colitis (UC) patients have been described as reacting with proteins in the granules of human neutrophils such as cathepsin G and lactoferrin and with yet unidentified antigens. Here we report the existence of a new member of perinuclear ANCA (P-ANCA) in UC patients. In the previous study, we found that UC patients had a novel P-ANCA against neutrophil 28-kD protein. In this study, we purified the same antigens from HL-60 lysates by using reversed phase high-performance liquid chromatography, and revealed that the 28-kD antigen consisted of two different proteins. The N-terminus amino acids of these proteins are identical with those of high mobility group (HMG) non-histone chromosomal proteins HMG1 and HMG2. Immunoblotting analysis of human neutrophil lysates using rabbit anti-HMG1/2 antisera revealed a single band of 28 kD, and the 28-kD band detected by immunoblotting analysis using patient's serum IgG completely disappeared after preincubation with a mixture of HMG1 and HMG2. Furthermore, rabbit anti-HMG1/2 antisera showed a perinuclear staining pattern in indirect immunofluorescence studies using ethanol-fixed neutrophils. These data demonstrate that HMG1 and HMG2 are novel target antigens of P-ANCA. HMG1 and HMG2 are distributed in the nuclei and cytoplasm of eukaryotic cells and act as transcription factors. Their intracellular localization and functions are distinct from those of the previously reported granular antigens of P-ANCA.

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Repression of Cell Cycle Progression by Antisense HMG2 RNA

Cited by 19 publications

References 0 publications

Reciprocal Regulation of the Cardiac Epigenome by Chromatin Structural Proteins Hmgb and Ctcf

Reciprocal Regulation of the Cardiac Epigenome by Chromatin Structural Proteins Hmgb and Ctcf

High-mobility group box 2 (HMGB2) modulates radioresponse and is downregulated by p53 in colorectal cancer cell

Novel autoantigens of perinuclear anti-neutrophil cytoplasmic antibodies (P-ANCA) in ulcerative colitis: non-histone chromosomal proteins, HMG1 and HMG2

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