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Expression data from isolated peritoneal macrophages treated with Histidine-rich glycoprotein

ABSTRACT: Histidine-rich glycoprotein (HRG) is a 75 kDa heparin-binding plasma protein which has been implicated in regulation of tumor angiogenesis and growth. To exert some of its biological functions, HRG acts on macrophages.This study was performed to assess changes in gene expression in peritoneal macrophages treated with HRG using oligonucleotide microarrays A total of 8 samples were analyzed. Peritoneal macrophages were pooled from 10 wt C57/BL6 mice and treated with recombinant HRG (1ug/ml) for 6 and 24 hours in duplicates

ORGANISM(S): Mus musculus

SUBMITTER: Sonia Tugues

PROVIDER: E-GEOD-34164 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Genetic deficiency in plasma protein HRG enhances tumor growth and metastasis by exacerbating immune escape and vessel abnormalization.

Tugues Sònia S Honjo Satoshi S König Christian C Noguer Oriol O Hedlund Marie M Botling Johan J Deschoemaeker Sofie S Wenes Mathias M Rolny Charlotte C Jahnen-Dechent Wilhelm W Mazzone Massimiliano M Claesson-Welsh Lena L

Cancer research 20120228 8

Histidine-rich glycoprotein (HRG) is a 75-kDa heparin-binding plasma protein implicated in the regulation of tumor growth and vascularization. In this study, we show that hrg(-/-) mice challenged with fibrosarcoma or pancreatic carcinoma grow larger tumors with increased metastatic properties. Compared with wild-type mice, fibrosarcomas in hrg(-/-) mice were more hypoxic, necrotic, and less perfused, indicating enhanced vessel abnormalization. HRG deficiency was associated with a suppressed anti ...[more]

PMID: 22374984

Similar Datasets

Expression data from isolated peritoneal macrophages treated with Histidine-rich glycoprotein

Project description:Histidine-rich glycoprotein (HRG) is a 75 kDa heparin-binding plasma protein which has been implicated in regulation of tumor angiogenesis and growth. To exert some of its biological functions, HRG acts on macrophages.This study was performed to assess changes in gene expression in peritoneal macrophages treated with HRG using oligonucleotide microarrays

2011-12-06 | GSE34164 | GEO

HUVEC Gene Regulation by Histidine-Rich Glycoprotein

Project description:HRG is a 75kDa heparin-binding protein non to extert gene regultaion changes on macropahges. To assess the effect of HRG on Enodothelial Cell gene regulation Human Umbilical Vein Endothelial Cells (HUVECs) were treated with Histidine-Rich Glycoprotein (HRG) 24 hour treatment with HRG. and examined for gene regulation changes versus untreated HUVECs after 6 and

2015-03-12 | GSE66768 | GEO

Genome-wide analysis of STAT3-binding and gene expression changes in peritoneal macrophages upon interleukin-10 stimulation

Project description:This SuperSeries is composed of the following subset Series: GSE31529: Genome-wide binding of STAT3 in peritoneal macrophages GSE31530: Transcriptome changes in IL-10 treated peritoneal macrophages Refer to individual Series

2012-02-13 | E-GEOD-31531 | biostudies-arrayexpress

Mouse peritoneal macrophages at 3.5 or 48 hours, 0,0.5 or 5 μg/ml Leukocyte cell-derived chemotaxin 2 (LECT2),gene expression array, two independent biological replicates

Project description:LECT2 is a liver derived cytokine and involved in many pathologic conditions, especially in immune regulation. To better understand cellular and molecular mechanisms of LECT2 in immune response, mouse peritoneal macrophages were isolated from mouse peritonaeum. After treatment with 0, 0.5 or 5 μg/ml of LECT2 for 3.5 or 48 hours, gene expression profile in mouse peritoneal macrophages was measured using gene expression array. Results showed that LECT2 treatment led to the enhancement of cytokines secretion and phagocytosis in peritoneal macrophages. Gene expression in mouse peritoneal macrophages isolated from mouse peritonaeum were measured after exposure to 0,0.5 or 5 μg/ml LECT2 for 3.5 or 48 hours using gene expression array. Two independent experiments were performed using different mice for each experiment for gene expression array analysis.

2011-12-13 | E-GEOD-33721 | biostudies-arrayexpress

Transcription profiling of mouse peritoneal macrophages treated with cholesterol

Project description:Peritoneal macrophages were extracted from 60 mice and then plated on tissue culture plates for treatment

2005-01-01 | E-TIGR-119 | biostudies-arrayexpress

MicroRNA expression in thioglycollate and alternatively activated

Project description:Macrophage activation must be tightly controlled to prevent overzealous responses that cause self-damage. MicroRNAs have been shown to promote classical macrophage activation by blocking concomitant anti-inflammatory signals and transcription factors, but can also place restraints on activation by preventing excessive TLR-signalling. In contrast, the microRNA profile associated with alternatively activated macrophages and their role in regulating wound-healing or anti-helminthic responses has not yet been described. Utilizing an in vivo model of alternative activation, in which adult Brugia malayi nematodes are surgically implanted in the peritoneal cavity of mice, we examined the profile of microRNA expression in these alternatively activated macrophages and compared this to alternatively activated IL-4 receptor knockout macrophages and thioglycollate elicited macrophages. Peritoneal macrophages from BALB/c wild type or IL-4 receptor knockout mice were elicited with thioglycollate or using nemtodes (peritoneal implant of Brugia malayi). The latter leads to a population of alternatively activated macrophages. Microarray analysis was used to examine the microRNA profile of WT alternatively activated macrophages (n = 4), IL-4 receptor knockout alternatively activated macrophages (n = 4), WT thioglycollate elicited macrophages (n = 3) and IL-4 receptor knockout thioglycollate elicited macrophages (n = 3).

2012-08-07 | E-GEOD-35047 | biostudies-arrayexpress

Polymorphic Histidine-rich Glycoprotein LC-MS/MS

Project description:Histidine-rich glycoprotein (HRG) HRG is a liver-produced protein circulating in human plasma serum at high concentrations of around 125 ug/mL. HRG belongs to the family of type-3 cystatins and has been implicated in a plethora of biological processes, albeit its precise function is still not well understood. Human HRG is a highly polymorphic protein, with at least 5 variants with minor allele frequencies (MAF) of more than 10%, variable in populations from different parts of the world. Considering these 5 mutations we can expect already 35 = 243 possible possibly genetic HRG variants in the population. Here, we purified HRG from serum of 44 individual donors and investigated by proteomics the occurrence of different allotypes, each being either homozygote or heterozygote for each of the 5 mutation sites. We observed that some mutational combinations in HRG were highly favored, while others were apparently missing, although they ought to be present based on the stochastic independent assembly of these 5 mutation sites. To further explore this behavior, we extracted data from the 1000 genome project (n ~ 2500 genomes) and assessed the frequency of different HRG mutants in this larger dataset, observing a prevailing agreement with our proteomics data. From all the proteogenomic data we conclude that the 5 different (frequent) mutations sites in HRG are not occurring independently, but some mutational variants at different sites are fully mutually exclusive, whereas other are highly intwined. Specific mutations also affect HRG abundance and its glycosylation. As the levels of HRG have been suggested as a protein biomarker in a variety of biological processes (e.g., aging, COVID-19 severity, severity of bacterial infections), we here conclude that the highly polymorphic nature of the protein needs to be considered in such evaluations, as these mutations affect HRG’s abundance, structure, post-translational modifications, and function.

2023-10-24 | PXD040914 | Pride

Deep sequencing analysis of the murine transcriptome response to different virulent parenthood B. melitensis infection

Project description:In this study, we employed the Illumina Genome Analyzer platform to perform a Digital Gene Expression (DGE) analysis of the peritoneal macrophages genome-wide transcriptome response to B.melitensis infection. Common changes in gene expression were observed among Brucella app. infected macrophages suggesting similar strategies were employed for their survival and replication, inducing anti-inflammatory and anti-apoptotic. A total of 1019 differentially expressed (DE) transcripts were identified in the macrophages 4 hours after differ virluent B.melitensis infection, especially genes participated lysosome pathway and MAPK pathway. Our findings demonstrate previously unrecognized changes in gene transcription that are associated with B.melitensis infection in the macrophages, and many significant pathways (cascades) identified in the study clearly merit further investigation. Our data provide new clues to understand the molecular attenuation mechanism of M5-90 and a firm foundation for reducing vaccine residual virulence, enhancing vaccine efficacy. Examination oftwo peritoneal macrophages infected brucella and one blank control.

2012-12-01 | E-GEOD-26337 | biostudies-arrayexpress

Transcription profiling of murine macrophages after infection with Paracoccidioides brasiliensis

Project description:Identification of transcripts in mouse peritoneal macrophages infected by P. brasiliensis yeasts cells

2007-08-31 | E-MEXP-1093 | biostudies-arrayexpress

HDX-MS of Human Histidine Rich Glycoprotein (HRG)

Project description:Histidine rich glycoprotein (HRG) is a multi-domain plasma glycoprotein, which is implicated in numerous biological processes including immune regulation, angiogenesis, coagulation and fibrinolysis. Despite a diverse role of biological functions, structural investigations into HRG have yielded only limited information, and there are no 3-dimensional structures of the intact protein. Current computational modelling suggests that HRG exhibits a large degree of conformational flexibility, which likely contributes to its well-documented multifunctionally. Here, utilising amide hydrogen-deuterium exchange mass spectrometry (HDX-MS), and combining insights from AlphaFfold, we investigate the conformational landscape of HRG. Overall, our data reveal a high degree of H/D exchange within the HRR, PRR and C terminal domains, indicating these regions are exposed to the aqueous environment surrounding the HRG surface, and provides the strongest evidence yet that these are largely disordered in vivo. Overall, this investigation lays the foundation for understanding the conformational architecture of HRG and paves the way for future studies aimed at elucidating how the interactions between HRG and other molecules are mediated, potentially revealing new mechanisms of its biological activity.

2025-11-06 | PXD065786 | Pride

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