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HMGB1 interactome in prostate and ovarian cancer cells

ABSTRACT: 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.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: James Wright

LAB HEAD: Jyoti Choudhary

PROVIDER: PXD026258 | Pride | 2022-02-17

REPOSITORIES: Pride

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Dataset's files

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			Action	DRS
	OT25cm_AB06_Rb1.msf	Msf
	OT25cm_AB06_Rb1.raw	Raw
	OT25cm_AB07_B1.msf	Msf
	OT25cm_AB07_B1.raw	Raw
	OT25cm_AB07_Rb1.msf	Msf

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Publications

HMGB1 Protein Interactions in Prostate and Ovary Cancer Models Reveal Links to RNA Processing and Ribosome Biogenesis through NuRD, THOC and Septin Complexes.

Barreiro-Alonso Aida A Lamas-Maceiras Mónica M Lorenzo-Catoira Lidia L Pardo Mercedes M Yu Lu L Choudhary Jyoti S JS Cerdán M Esperanza ME

Cancers 20210918 18

This study reports the HMGB1 interactomes in prostate and ovary cancer cells lines. Affinity purification coupled to mass spectrometry confirmed that the HMGB1 nuclear interactome is involved in HMGB1 known functions such as maintenance of chromatin stability and regulation of transcription, and also in not as yet reported processes such as mRNA and rRNA processing. We have identified an interaction between HMGB1 and the NuRD complex and validated this by yeast-two-hybrid, confirming that the RB ...[more]

PMID: 34572914

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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

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

Characterisation of HMGB1 interactome in PNT2 prostate cells

Project description: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.

2018-05-07 | PXD007867 | Pride

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

Quantitative analysis of septin Cdc10 & Cdc3-associated proteome during stress response in the fungal pathogen Cryptococcus neoformans

Project description:Cryptococcus neoformans is a type of pathogenic fungi that can cause infections in people with weakened immune systems. This fungal pathogen can survive in the body by growing at the host's body temperature (37\'b0C), forming a carbohydrate capsule, and producing melanin. When Cryptococcus neoformans strains lack certain septin proteins, they cannot grow at 37\'b0C and are not able to cause infections in mice. However, it is not yet clear how septins help the yeast to grow at the host's body temperature. Septins are a group of proteins that are important for cell division and morphogenesis. In the model organism, Saccharomyces cerevisiae septins are essential. S. cerevisiae septins form a higher-order complex at the mother bud-neck to scaffold over 80 proteins, including those involved in cell wall organization, cell polarity, and cell cycle control. In C. neoformans, septins also form a complex at the mother bud neck but the septin interacting proteome in this species remains largely unknown. In this study, the entire septin complex in C. neoformans was uncovered as downregulated during the stationary growth phase and heat stress. In addition, we investigated the septin interactome in C. neoformans, shedding light on the proteins that interact with septins Cdc3 and Cdc10 under ambient temperature and heat stress, respectively. Our findings unveiled a diverse array of interacting proteins, including components of Golgi to plasma membrane transport, cell division, and single-stranded DNA binding. \'a0Overall, this study delineates septins in C. neoformans as part of the cytoskeleton and cytoskeleton-dependent cytokinesis and provides a landscape of septin interactors to investigate and further understand septin biology in fungal systems.

2024-10-28 | PXD052407 | 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

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

Identification of cell cycle dependent interaction partners of the septins by quantitative mass spectrometry

Project description:The septins are a conserved family of GTP-binding proteins that, in the baker's yeast, assemble into a highly ordered array of filaments at the mother bud neck. These filaments undergo dramatic structural rearrangements during the cell cycle which are mechanistically not yet understood. We aimed at identifying key components that are involved in the transitions of the septins. Combining cell synchronization and quantitative affinity-purification mass-spectrometry (AP-MS), we identified interaction partners of the septins at three distinct stages of the cell cycle. A total of 83 interaction partners of the septins were assigned. We detected DNA-interacting/nuclear proteins and proteins involved in ribosome biogenesis and protein synthesis predominantly present in G1 arrested cells without an assembled septin structure. In addition, two distinct sets of regulatory proteins that are specific for cells at S-phase with a stable septin collar or at mitosis with split septin rings were identified. Complementary methods such as the SPLIFF method allowed us to more exactly define the spatial and temporal characteristics of selected candidate proteins of the AP-MS screen.

2016-01-28 | PXD002561 | Pride

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

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-49855 | biostudies-arrayexpress

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