Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Genome-wide analysis of primary intestinal epithelial cells with or without Cosmc from 2-month-old mice

ABSTRACT: Analysis of mucin-type O-glycan regulation of gene expression in murine intestinal epithelial cells isolated from a mouse. The hypothesis tested in the current study was that loss of Cosmc (by Cre/Lox: Vil-Cre+ X Cosmcflox/+), which is required for core 1-based O-glycan extension, influences gene expression. Transcripts from colorectum and from small intestine were compared to also evaluate whether O-glycans control different genes in different regions of the gut. We had particular interest in identifying transcripts or pathways important in regulating the microbiota or influencing intestinal inflammation. Results provide important information on how cell surface glycosylation controls gene transcription in in vivo.

ORGANISM(S): Mus musculus

PROVIDER: GSE84416 | GEO | 2016/12/18

SECONDARY ACCESSION(S): PRJNA329110

REPOSITORIES: GEO

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

proteome sequencing for the colon tissues of mice with ckmt1 knockout

Project description:We here performed a proteomics study on the colon tissues of ckmt1 KOIEC or. WT (flox+/+) mice after DSS treatment for 8 days (n=3). KOIEC mice (Ckmt1flox/flox, Vil-Cre) means mice with intestinal epithelial conditional knockout (C57BL/6J). Cre-negative Ckmt1 flox/flox littermates were used as controls. Group 1: DSSCKO (Ckmt1flox/flox, Vil-Cre) Group 2: DSSflox (Cre-negative Ckmt1 flox/flox littermates)

2025-05-07 | PXD057053 | Pride

A mucin-regulated adhesin determines the spatial organization and inflammatory character of a bacterial symbiont in the vertebrate gut

Project description:In a healthy gut, microbes are often aggregated with host mucus, yet the molecular basis for this organization and its impact on intestinal health are unclear. Mucus is a viscous physical barrier separating resident microbes from epithelia, but also provides glycan cues that regulate microbial behaviors. Here, we describe a mucin-sensing pathway in an Aeromonas symbiont of zebrafish, Aer01. In response to the mucin-associated glycan N-acetylglucosamine, a sensor kinase regulates expression of an aggregation-promoting adhesin we named MbpA. Upon MbpA disruption, Aer01 colonizes to normal levels, but is largely planktonic and more immunogenic. Increasing cell surface MbpA rescues these traits. MbpA-like adhesins are common in human-associated bacteria and expression of an Akkermansia muciniphila MbpA-like adhesin in MbpA-deficient Aer01 restores lumenal aggregation and reverses its pro-inflammatory character. Our work demonstrates how resident bacteria use mucin glycans to modulate behaviors congruent with host health.

2023-07-03 | GSE236092 | GEO

RHOA inactivation enhances Wnt signaling and promotes colorectal cancer

Project description:Microarray transcriptomic analysis of formalin-fixed, paraffin-embedded small intestinal tumors from control (Apcmin/+;Vil-Cre-/-;RhoADN/-) and DN-RhoA (Apcmin/+;Vil-CreTG/-;RhoADN/-) mice.

2014-11-21 | E-MTAB-2981 | biostudies-arrayexpress

Ruminococcus torques is a keystone degrader of intestinal mucin glycoprotein, releasing oligosaccharides used by Bacteroides thetaiotaomicron

Project description:Symbiotic interactions between humans and our communities of resident gut microbes (microbiota) play many roles in health and disease. Some gut bacteria utilize mucus as a nutrient source and can under certain conditions damage the protective barrier it forms, increasing disease susceptibility. We investigated how Ruminococcus torques—a known mucin-degrader that remains poorly studied despite its implication in inflammatory bowel diseases (IBDs)— degrades mucin glycoproteins or their component O-linked glycans to understand its effects on the availability of mucin-derived nutrients for other bacteria. We found that R. torques utilizes both mucin glycoproteins and released oligosaccharides from gastric and colonic mucins, degrading these substrates with a panoply of mostly constitutively expressed, secreted enzymes. Investigation of mucin oligosaccharide degradation by R. torques revealed strong fucosidase, sialidase and b1,4-galactosidase activities. There was a lack of detectable sulfatase and weak β1,3-galactosidase degradation, resulting in accumulation of glycans containing these structures on mucin polypeptides. While the Gram-negative symbiont, Bacteroides thetaiotaomicron grows poorly on mucin glycoproteins, we demonstrate a clear ability of R. torques to liberate products from mucins, making them accessible to B. thetaiotaomicron. This work underscores the diversity of mucin-degrading mechanisms in different bacterial species and the probability that some species are contingent on others for the ability to more fully access mucin-derived nutrients. The ability of R. torques to directly degrade a variety of mucin and mucin glycan structures and unlock released glycans for other species suggests that it is a keystone mucin degrader, which may contribute to its association with IBD.

2024-06-19 | GSE262875 | GEO

Mucosal Glycan Foraging Enhances the Fitness and Transmission of a Saccharolytic Human Distal Gut Symbiont

Project description:Gene expression profiles of Bacteroides thetaiotaomicron in vitro during growth on host mucosal polysaccharides as sole carbon sources. All substrates in this series are derived from porcine gastric mucin and include mucin O-glycans and glycosaminoglycans. Two different culture formats used: 800ml batch-culture bioreactors and 5ml tube cultures (format is indicated within each sample title). Each set of growths was referenced to a minimal medium glucose reference corressponding to the same culture format. Unfractionated porcine mucosal glycan (PMG) growths were compared to previously published in vivo datasets, which were referenced to the 800ml minimal medium glucose reference dataset.

2008-11-20 | E-GEOD-11944 | biostudies-arrayexpress

Epithelial Muscarinic Receptor 3 Ablation Induces Sex-Specific Modulation of Colonic Intestinal Progenitor Cells and Response to Intestinal Injury [586CW]

Project description:In this study, we investigated regional and sex differences in the cholinergic modulation of intestinal epithelial cells in homeostasis and regeneration. Genetic intestinal epithelial ablation of the M3R employing Vil-Cre x M3R fl/fl mice interestingly resulted in the prominent reduction in Lgr5-expressing progenitor cells in male tissues, contrasting an expansion of these cells in the female intestinal epithelium. This prominent difference showed abrogated in young female mice with reduced circulating sex hormone levels. M3R ablation further induced the expansion of pEGFR+ tuft cells and induced the activation of the PI3K/Akt pathway. Importantly, sex-specific differences in Lgr5-expressing progenitor cells translated into the development of severe inflammation in male Vil-Cre x M3R fl/fl mice subjected to an acute colitis model, which did almost not affect female Vil-Cre x M3R fl/fl mice. In addition, sex-specific effects of modulations of cholinergic signaling on epithelial cells could be corroborated in murine and human colonoids. Collectively, our data reveal regional and sex differences in the cholinergic, muscarinic modulation of intestinal epithelial cells.

2025-02-28 | GSE286190 | GEO

Epithelial Muscarinic Receptor 3 Ablation Induces Sex-Specific Modulation of Colonic Intestinal Progenitor Cells and Response to Intestinal Injury [JW468]

2025-02-28 | GSE286189 | GEO

Binding of Akkermansia muciniphila to mucin is O-glycan specific

Project description:The intestinal anaerobic bacterium Akkermansia muciniphila is specialized in the degradation of mucins, which are heavily O-glycosylated proteins that constitute the major components of the mucus lining the intestine. Despite that adhesion to mucins is considered critical for the persistence of A. muciniphila in the human intestinal tract, our knowledge of how this intestinal symbiont recognizes and binds to mucins is still limited. Here, we first show that the mucin-binding properties of A. muciniphila are independent of environmental oxygen concentrations and not abolished by pasteurization. We then dissected the mucin-binding properties of pasteurized A. muciniphila by use of a recently developed cell-based mucin array that enables display of the tandem repeats of human mucins with distinct O-glycan patterns and structures. We found that A. muciniphila recognizes the unsialylated LacNAc (Galβ1-4GlcNAc1-R) disaccharide selectively on core2 and core3 O-glycans. This disaccharide epitope is abundantly found on human colonic mucins capped by sialic acids, and we demonstrated that endogenous A. muciniphila neuraminidase activity can uncover the epitope and promote binding. In summary, our study provides insights into the mucin-binding properties important for colonization of a key mucin-foraging bacterium.

2024-05-30 | PXD051738 | Pride

Transcriptome study of colon epithelial cells in Reg3a-transgenic mice

Project description:The human C-type lectin Reg3a (HIP/PAP) is an antimicrobial peptide that kills Gram-positive bacteria. Reg3a preserves gut microbiota homeostasis, reinforces intestinal barrier function and thereby helps to fight induced colitis in mice. Transcriptomic data revealed an upregulation of numerous genes involved in the robustness of the intestinal barrier, and the biosynthesis pathway of mucin core 1 and 3 O-glycans.

2018-01-31 | GSE64932 | GEO

Host-derived O-glycans inhibit toxigenic conversion by a virulence-encoding phage in Vibrio cholerae

Project description:Pandemic and endemic strains of Vibrio cholerae arise from toxigenic conversion by the CTXφ bacteriophage, a process by which CTXφ infects non-toxigenic strains of V. cholerae. CTXφ encodes the cholera toxin, an enterotoxin responsible for the watery diarrhea associated with cholera infections. Despite the critical role of CTXφ during infections, signals that affect CTXφ-driven toxigenic conversion or expression of the CTXφ-encoded cholera toxin remain poorly characterized, particularly in the context of the gut mucosa. Here, we identify mucin polymers as potent regulators of CTXφ-driven pathogenicity in V. cholerae. Our results indicate that mucin-associated O-glycans block toxigenic conversion by CTXφ and suppress the expression of CTXφ-related virulence factors, including the toxin co-regulated pilus and cholera toxin, by interfering with the TcpP/ToxR/ToxT virulence pathway. By synthesizing individual mucin glycan structures de novo, we identify the Core 2 motif as the critical structure governing this virulence attenuation. Overall, our results highlight a novel mechanism by which mucins and their associated O-glycan structures affect CTXφ-mediated evolution and pathogenicity of V. cholerae, underscoring the potential regulatory power housed within mucus.

2022-12-01 | GSE213598 | 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