Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

DAA-IgA

ABSTRACT: D-amino acids control IgA production

PROVIDER: PRJEB35803 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	ERR3765020_1.fastq.gz	Fastqsanger.gz
	ERR3765020_2.fastq.gz	Fastqsanger.gz
	ERR3765030_1.fastq.gz	Fastqsanger.gz
	ERR3765030_2.fastq.gz	Fastqsanger.gz
	ERR3765021_1.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 44

Similar Datasets

murine jejunal and ileal epithelial tissue

Project description:Transcriptional profiling of mouse jejunal epithelia comparing Tcrbd-/-, DAOwt/wt mouse and Tcrbd-/-, DAOG181R/G181R Intestinal microbiota produce D-amino acids, which are bacteria-specific metabolites, for regulation of bacterial cell wall integrity. Host intestine releases D-amino acid oxidase (DAO) to degrade bacterial D-amino acids, which shapes gut microbial community. However, it is not clarified whether bacterial D-amino acids affect host s immunity. In the present study, we compared mRNA expression in ileal epithelial tissue of DAO null mice with that of control mice in the absence of both T cell receptor beta and delta (Tcrb/d). Transcriptome analysis revealed up-regulation of inflammatory cytokines such as TNFa, IL1b, and IFNg in the epithelial tissue. Up-regulation of such cytokines could promote survival of na ve B cells and increase IgA-producing plasma cells, which in turn results in enhancement of IgA production. These results indicate that DAO controls intestinal immune responses through regulation of na ve B cells and differentiation of mature B cells.

2020-08-31 | GSE142070 | GEO

IgA deglycosylation to identify glycosylation sites

Project description:In order to provide information on the peptide sequence of the IgA glycopeptides, a proteomics analysis was run on LC-MS/MS data of N-glycosidase F-digested IgA samples, in which the N-glycans had been released. The samples included IgA (isolated) from: 1) the saliva samples from two healthy donors, 2) a pooled-plasma standard from a minimum of 20 human donors (VisuCon-F Frozen Normal Control Plasma; Affinity Biologicals, Ancaster, Canada), 3) 10 μg of a human plasma-derived IgA standard (Lee Biosolutions, Maryland Heights, MO), and 4) a human colostrum-derived SIgA standard (Athens Research and Technology, Athens, GA).

2018-11-09 | PXD011228 | Pride

Gut IgA Enhances Systemic IgG Responses to Pneumococcal Vaccines Through the Commensal Microbiota

Project description:We set up to characterize the global transcriptome of splenic follicular (FO) B cells from control wild type (Wt) and Igha-deficient (IgAKO) mice with the aim of gaining new insights into how translocated gut antigens may impair IgG production to vaccines in the absence of IgA. Splenic Marginal zone (MZ) B cells were also included in this study, as IgA deficiency impaired IgG responses to T-independent immunogens as well.

2024-01-01 | GSE173361 | GEO

Gene expression on CD11b+ IgA and CD11b- IgA cells in the small intestine #01

Project description:To compare gene expression between CD11b+ IgA and CD11b- IgA cells in the small intestine, each cell population was isolated from the murine small intestine. Similar experiment with different sample was performed as described in Gene expression on CD11b+ IgA and CD11b- IgA cells in the small intestine #02

2013-04-01 | E-GEOD-37225 | biostudies-arrayexpress

IGA-BARIA

Project description:IGA-BARIA

| PRJEB47045 | ENA

Krüppel-like factor 2 controls IgA plasma cell compartmentalization and IgA responses

Project description:Krüppel-like factor 2 (KLF2) is a potent regulator of lymphocyte differentiation, activation and migration. However, its functional role in adaptive and humoral immunity remains elusive. Therefore, by using mice with a B cell-specific deletion of KLF2, we investigated plasma cell differentiation and antibody responses. We revealed that the deletion of KLF2 resulted in perturbed IgA plasma cell compartmentalization, characterized by the absence of IgA plasma cells in the bone marrow, their reductions in the spleen, the blood and the lamina propria of the colon and the small intestine, concomitant with their accumulation and retention in mesenteric lymph nodes and Peyer’s patches. Most intriguingly, secretory IgA in the intestinal lumen was almost absent, dimeric serum IgA was drastically reduced and antigen-specific IgA responses to soluble Salmonella flagellin were blunted in KLF2-deficient mice. Perturbance of IgA plasma cell localization was caused by deregulation of CCR9, Integrin chains αM, α4, β7, and sphingosine-1-phosphate receptors. Hence, KLF2 not only orchestrates the localization of IgA plasma cells by fine-tuning chemokine receptors and adhesion molecules but also controls IgA responses to Salmonella flagellin.

2022-07-13 | GSE160732 | GEO

Gene expression on CD11b+ IgA and CD11b- IgA cells in the small intestine #01

Project description:To compare gene expression between CD11b+ IgA and CD11b- IgA cells in the small intestine, each cell population was isolated from the murine small intestine.

2013-04-01 | GSE37225 | GEO

IgA transcytosis and tumor antigen recognition govern anti-tumor immunity in ovarian cancer

Project description:Although most ovarian cancers show prognostically relevant activated T-cell infiltrates, response rates to immune checkpoint inhibitors are very modest4. Memory B-cell and plasma cell infiltrates have been associated with better outcome in ovarian cancer, but the nature and functional relevance of these responses are controversial. Using 3 independent cohorts totaling 575 high-grade serous ovarian cancer (HGSOC) patients, we show that robust humoral responses are heavily dominated by the production of polyclonal IgA, which binds to Polymeric IgA Receptors universally expressed on ovarian cancer cells. Notably, all tertiary lymphoid structures identified in ~21% of HGSOCs contain IgA-producing oligoclonal B-cells. Strikingly, tumor Bcell-derived IgAs effectively target extracellular oncogenic drivers, whereas IgA transcytosis through malignant epithelial cells elicits transcriptional changes that antagonize the RAS pathway and that sensitize tumor cells to T-cell cytolytic killing, hindering malignant progression. Thus, tumor antigen-specific and antigen-independent IgA responses antagonize ovarian cancer growth by governing coordinated tumor cell, T-cell and B-cell responses. These findings provides a platform for the identification of novel targets spontaneously recognized by intratumoral B-cell-derived antibodies, and suggest that immunotherapies that augment B-cell responses may be more effective than T-cell-centric approaches, particularly for malignancies resistant to checkpoint inhibitors.

2020-12-01 | PXD018079 | Pride

Effect of perioperative dietary restriction strategy on intestinal IgA+ B cells in patients with colorectal cancer

Project description:Interventions: experimental group:fasting-mimicking diet;control group:none Primary outcome(s): IgA+ B cells Study Design: Parallel

| 41585 | ecrin-mdr-crc

Targeted transcriptional analysis of IgA vasculitis, IgA nephropathy, and IgA dominant infection related glomerulonephritis

Project description:This study identifies immune transcript signatures that may predict IgAV nephritis in skin biopsies and distinguish IgA-IRGN from IgAN and IgAV in kidney biopsies

2023-08-08 | GSE220100 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

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