Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

ORGANISM(S): Mus musculus

PROVIDER: GSE34164 | GEO | 2011/12/06

SECONDARY ACCESSION(S): PRJNA149709

REPOSITORIES: GEO

ACCESS DATA

Json Xml

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 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

2011-12-06 | E-GEOD-34164 | biostudies-arrayexpress

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

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

Mus musculus

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

| PRJNA149709 | ENA

Gene regulation in human lymphoma tissue

Project description:Among the different human lymphoma types, some express the soluble protein Histidine-rich glycorprotein (HRG) in CD20+ tumor cells. Normally HRG is expressed by hepatocytes. We were interested in comparing the gene expression patterns in lymphoma expressing HRG or not in marginal zone lymphomas, which was the lymphoma type with the highest prevalence f HRG (37%).

2021-05-25 | GSE151360 | GEO

Histidine-rich glycoprotein protects from systemic Candida infection.

Project description: Not available

| S-EPMC2537934 | biostudies-literature

Histidine-rich glycoprotein as a prognostic biomarker for sepsis.

Project description: Not available

| S-EPMC8119687 | biostudies-literature

WGS histidine overproducers

Project description:Whole genomes sequencing to determine mutations in histidine overproducers generated with a toxic histidine analog

| PRJEB45772 | ENA

Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1.

Project description: Not available

| S-EPMC198540 | biostudies-literature

Nickel Binding- and Histidine-Rich Proteins of Helicobacter species

Project description:The files in this archive examine six species within the genus Helicobacter to assay their histidine-rich proteins. They correspond to the manuscript "Expansion of nickel binding- and histidine-rich proteins during gastric adaptation of Helicobacter species" by Frederic Fischer, Egor Vorontsov, Evelyne Turlin, Christian Malosse, Camille Garcia, David L. Tabb, Julia Chamot-Rooke, Riccardo Percudani, Daniel Vinella and Hilde De Reuse. The sequence databases for the Helicobacter species are based on reference or complete UniProt proteomes in FASTA format, supplemented with reannotations of Hpn and Hpn2 protein products. The full list of RAW files, including their attribution to individual species and the type of experiment they represent, can be found in RAWs-Readme. We have included QuaMeter IDFree metrics to include basic statistics such as length of LC gradient, the number of MS/MS scans, etc.

2022-03-23 | MSV000089106 | MassIVE

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data