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Characterisation of HMGB1 interactome in PNT2 prostate cells

ABSTRACT: HMGB1 and HMGB2 are members of the High Mobility Group (HMG) protein superfamily that contain a DNA binding domain (HMG-Box), and their overexpression has been related to main cancer hallmarks, tumor progression, metastasis formation and bad prognosis. We have used yeast two hybrid and affinity purification-mass spectrometry to explore HMGB1 and HMGB2 protein interactions in prostate and ovarian epithelial cells.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Epithelial Cell, Cell Culture

SUBMITTER: James Wright

LAB HEAD: Jyoti Choudhary

PROVIDER: PXD007867 | Pride | 2018-05-07

REPOSITORIES: Pride

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			Action	DRS
	OT25cm_AB16B1.msf	Msf
	OT25cm_AB16B1.raw	Raw
	OT25cm_AB16Rb.msf	Msf
	OT25cm_AB16Rb.raw	Raw
	OT25cm_AB20B1.msf	Msf

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Publications

Delineating the HMGB1 and HMGB2 interactome in prostate and ovary epithelial cells and its relationship with cancer.

Barreiro-Alonso Aida A Lamas-Maceiras Mónica M García-Díaz Rosa R Rodríguez-Belmonte Esther E Yu Lu L Pardo Mercedes M Choudhary Jyoti S JS Cerdán María Esperanza ME

Oncotarget 20180410 27

High Mobility Group B (HMGB) proteins are involved in cancer progression and in cellular responses to platinum compounds used in the chemotherapy of prostate and ovary cancer. Here we use affinity purification coupled to mass spectrometry (MS) and yeast two-hybrid (Y2H) screening to carry out an exhaustive study of HMGB1 and HMGB2 protein interactions in the context of prostate and ovary epithelia. We present a proteomic study of HMGB1 partners based on immunoprecipitation of HMGB1 from a non-ca ...[more]

PMID: 29721183

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HMGB1 interactome in prostate and ovarian cancer cells

Project description:This study reports the interactome of HMGB1 in prostate and ovarian cancer cells, which includes a variety of proteins involved in diverse cellular processes. Subcellular fractionation is used to map the distribution of interacting proteins. In the nucleus, HMGB1 interacts directly with NuRD complex subunit RBBP7, as confirmed by yeast two-hybrid. Amongst HMGB1 interacting proteins are also subunits of the THOC complex and the septin complex. THOC5 IP-MS experiments confirmed that THOC proteins interact with septins and also with RAB11.

2022-02-17 | PXD026258 | Pride

HMGB1 interactome in prostate and ovarian cancer cells treated with cisplatin

Project description:Cisplatin is used in chemotherapy of prostate, ovary and other cancer types but unfortunately the efficiency of cisplatin treatment is frequently hampered by acquired resistance. The cytotoxic effect of cisplatin has been attributed to its binding to DNA. HMGB1 is able to bind to cisplatin-DNA adducts with high affinity and its expression levels are associated with cisplatin resistance. This study reports the interactome of HMGB1 in prostate and ovarian cancer cells treated with cisplatin.

2021-11-01 | PXD026309 | Pride

Chromatin IP sequencing of the nuclear factor HMGB1 in livers from mice after a metabolic stress either induced by a 12-week high fat diet consumption or a fasting (6hours)-refeeding (8hours) challenge.

Project description:To unveil HMGB1 DNA occupancy in livers of mice after a metabolic stress either induced by a 12-week high fat diet consumption or a fasting (6hours)-refeeding (8hours) challenge. Challenges known to generate a robust activation of hepatic lipogenesis and liver steatosis.

2022-03-31 | E-MTAB-11543 | biostudies-arrayexpress

Comparison of the transcriptomes of hmgb1 vs Col-0

Project description:Testing the consequences of the absence of the chromatin-associated HMGB1 protein on the transcriptome in Arabidopsis. Keywords: Comparison of mutant and wildtype samples. Four replicate RNA extractions were performed of each genotype using independent pools of plants. hmgb1#1 (Cy5) vs. Col-0#1 (Cy3) Col-0#2 (Cy5) vs. hmgb1#2 (Cy3) dye-swap hmgb1#3 (Cy5) vs. Col-0#3 (Cy3) Col-0#5 (Cy5) vs. hmgb1#4 (Cy3) dye-swap Samples were hybridized in two dye-swaps. The data were normalized over all 4 hybridizations to obtain one, single log-ratio(Sample/Reference). The raw data files of all four of the hybridizations are attached to the Sample.

2008-11-23 | E-GEOD-10638 | biostudies-arrayexpress

Tumor cells express and maintain HMGB1 in the reduced isoform to enhance CXCR4-mediated migration

Project description:During inflammation and tissue regeneration, the alarmin High Mobility Group Box 1 (HMGB1), in its reduced isoform, enhances the activity of the chemokine CXCL12, forming a heterocomplex that acts via the chemokine receptor CXCR4. Despite the established roles of both HMGB1 and CXCL12 in tumor progression and metastatic spread to distal sites, the role of the CXCL12/HMGB1 heterocomplex in cancer has never been investigated. By employing a newly established mass spectrometry protocol that allows an unambiguous distinction between reduced (red HMGB1) and oxidized (ox HMGB1) HMGB1 isoforms in cell lysates, we demonstrate that human epithelial cells derived from breast (MCF-7 and MDA-MB-231) and prostate (PC-3) cancer predominantly express red-HMGB1, while primary CD3+ T lymphocytes from peripheral blood express both HMGB1 isoforms. All these cancer cells release HMGB1 in the extracellular microenvironment together with varying concentrations of thioredoxin and thioredoxin reductase. The CXCL12/HMGB1 heterocomplex enhances, via CXCR4, the directional migration and invasiveness of cancer cells characterized by high metastatic potential that possess a fully active thioredoxin system, contributing to maintain red-HMGB1. On the contrary, cancer cells with low metastatic potential, lack thioredoxin reductase, promptly uptake CXCL12 and fail to respond to the heterocomplex. Our study demonstrates that the responsiveness of cancer cells to the CXCL12/HMGB1 heterocomplex, resulting in enhanced cell migration and invasiveness, depends on the maintenance of HMGB1 in its reduced isoform, and suggests disruption of the heterocomplex as a potential therapeutic target to inhibit invasion and metastatic spread in cancer therapies.

2024-05-02 | PXD048091 | Pride

A monoclonal anti-HMGB1 antibody attenuates neurodegeneration in an experimental animal model of glaucoma

Project description:Neuroinflammation is a crucial process for the loss of retinal ganglion cells (RGC), a major characteristic of glaucoma. High expression of high mobility group box protein 1 (HMGB1) plays a detrimental role in inflammatory processes and is elevated in the retinas of glaucoma patients. Therefore, this study aimed to investigate the effects of intravitreal injection of an anti-HMGB1 monoclonal antibody (anti-HMGB1 Ab) in an experimental animal model of glaucoma. Two groups of Spraque Dawley rats received episcleral vein occlusion to chronically elevate intraocular pressure (IOP): (1) IgG group, intravitreal injection of an unspecific IgG as a control, n=5, (2) HMGB1 group, intravitreal injection of an anti-HMGB1 Ab, n=6. IOP, retinal nerve fiber layer thickness (RNFLT), and the retinal flash response was monitored longitudinally. Post-mortem examinations included immunohistochemistry, microarray, and mass spectrometric analysis. RNFLT was significantly increased in the HMGB1 group compared to the IgG group (p<0.001). RGC density showed improved neuronal cell survival in the retina in HMGB1 compared to the IgG group (p<0.01). Mass spectrometric proteomic analysis of retinal tissue showed increased abundance of RNA metabolism-associated heterogeneous nuclear ribonucleoproteins (hnRNPs), such as hnRNP U, D, and H2, in animals injected with the anti-HMGB1 Ab, indicating that application of the antibody may cause increased gene expression. Microarray analysis showed significantly decreased expression of C-X-C motif chemokine ligand 8 (CXCL8, p<0.05) and connective tissue growth factor (CTGF, p<0.01) in the HMGB1 group. Thus, these data suggest that intravitreal injection of anti-HMGB1 Ab reduced HMGB1-dependent inflammatory signaling and mediated RGC neuroprotection.

2022-05-20 | PXD031987 | Pride

HuR and miR-1192 regulate myogenesis by modulating the translation of HMGB1 mRNA (mRNA)

Project description:Upon muscle injury the high mobility group box 1 (HMGB1) protein is up-regulated and secreted to initiate reparative responses. Here we show that HMGB1 controls myogenesis both in vitro and in vivo, during development and after adult muscle injury. HMGB1 expression in muscle cells is regulated at the translational level: the miRNA miR-1192 inhibits HMGB1 translation and the RNA-binding protein HuR promotes it. HuR binds to a cis-element, HuRBS, located in the 3'UTR of the HMGB1 transcript, and at the same time miR-1192 is recruited to an adjacent seed element. The binding of HuR to the HuRBS prevents the recruitment of Argonaute 2 (Ago2), overriding miR-1192-mediated translation inhibition. Depleting HuR reduces myoblast fusion and silencing miR-1192 re-establishes the fusion potential of HuR-depleted cells. We propose that HuR promotes the commitment of myoblasts to myogenesis by enhancing the translation of HMGB1 and suppressing the translation inhibition mediated by miR-1192. RNA content was extracted following immunoprecipitation of HuR using a monoclonal antibody (3A2) and the levels of mRNA were compared to an IgG control in order to determine which transcripts were enriched in the HuR ribonucleoprotein complex.

2013-08-14 | E-GEOD-49856 | biostudies-arrayexpress

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [HiC]

Project description:The mutually exclusive expression of virulence genes is critical for the immune evasion and pathogenesis of malaria parasites, Plasmodium falciparum, in human host. The three-dimensional genome structure has emerged as a new factor involved in transcriptional regulation of virulence gene families in the parasites. However, the mechanism controlling this epigenetic regulation pathway remains elusive. Here, we have identified the highly conserved high mobility group protein HMGB1 as a critical architectural regulator in establishment of high-order genome structure via interaction with centromeres in P. falciparum. Genetic manipulation of Pfhmgb1 gene and Hi-C analysis showed that the boundary of telomere and centromere clusters in an opposite spatial relationship in the nucleus was disrupted upon hmgb1 knockout. The collapse of euchromatic centromere cluster from nuclear periphery towards the opposite heterochromatic telomere cluster triggered relocation of the original active var gene, which resulted in complete silence of the entire repertoire of var gene family. ChIP-seq and fluorescence assay analysis confirmed the specific interaction between PfHMGB1 and centromeres. Meanwhile, as in other eukaryotes, PfHMGB1 was also widely present on the promoter regions of a variety of genes and co-regulated transcription, including other non-var variant gene families, suggesting multiple dimensions of epigenetic gene regulation by PfHMGB1. Finally, the natural genome organization could be reconstructed by hmgb1 gene complementation, which rescued the mutually exclusive expression of virulence genes. Taken together, our work provides new insight into the evolution of biological functions of the HMG architectural superfamily in eukaryotes.

2021-04-14 | GSE141759 | GEO

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [RNA-seq]

2021-04-14 | GSE141758 | GEO

HMGB1 is required for virulence gene expression via configuration of genome architecture in Plasmodium falciparum [TF ChIP]

2021-04-14 | GSE141761 | GEO