Mus musculus
Ontology highlight
ABSTRACT:
PROVIDER: PRJNA145167 | ENA |
REPOSITORIES: ENA
Similar Datasets
Project description:The purpose of this experiment is to respond to the NIGMS mandate to screen Core F generated glycosyltransferase KO mice in Core E and Core C. The goal is to screen several tissues for gene expression changes in ST6GalNAc2 KO mice and B4GalNT1/B4GalNT2 double KO mice relative to C75 Wild Type controls. Tissues for Core E analysis were selected by mining public databases including the NIH GEO database for tissues that expressed the KO genes at moderate to high levels.
2011-09-08 | GSE31993 | GEO
Project description:The purpose of this experiment is to respond to the NIGMS mandate to screen Core F generated glycosyltransferase KO mice in Core E and Core C. The goal is to screen several tissues for gene expression changes in ST6GalNAc2 KO mice and B4GalNT1/B4GalNT2 double KO mice relative to C75 Wild Type controls. Tissues for Core E analysis were selected by mining public databases including the NIH GEO database for tissues that expressed the KO genes at moderate to high levels. Results from Core E gene expression analysis are then used to help Core C select tissues to follow up with glycan analysis on in each of the KO mice. For the ST6GalNAc2 KO mouse we selected: Brain, Small Intestine, Lymph Node and Thyroid for analysis. For the B4GalNT1/B4GalNT2 double KO mouse we selected: Kidney, Mammary Gland, Thymus and Testes for analysis. Wild type tissues were analyzed in parellel.
2011-09-07 | E-GEOD-31993 | biostudies-arrayexpress
Project description:The Sda histo-blood group antigen [GalNAcβ1-4(NeuAcα2-3)Galβ-R] is present in colon, kidney and body fluids among 96-98% of Europeans whilst 90% have Sda-positive erythrocytes. Sda is implicated in various infections and constitutes a potential biomarker for colon cancer. The 2-4% truly Sd(a‒) individuals may produce anti-Sda, which can lead to incompatible blood transfusions, especially if donors with the high-expressing Sda phenotype, Sd(a++) or Cad, are involved. It was hypothesized that defects in the B4GALNT2-encoded β4GalNAc-T2 glycosyltransferase underlies the null phenotype. We recently reported the association of B4GALNT2 mutations with the Sd(a‒) phenotype, which formally established the SID blood-group system. In the present study, we provide causal proof and glycoprotein profiling underpinning this correlation. Phenotypically Sd(a‒) HEK293 cells were transfected with different B4GALNT2 constructs and evaluated by immunostaining and LC-MS/MS-based glycoproteomics. The pre¬dominant SIDnull allele with SNP rs7224888:T>C (p.Cys406Arg) abolished Sda synthesis, while this antigen was detectable as N- or O-glycans on multiple glycoproteins following transfection of wildtype B4GALNT2. Surprisingly, two rare missense SNPs, rs148441237:A>G and rs61743617:C>T, found in a Sd(a‒) compound heterozygote gave results similar to wildtype. To elucidate if Sd(a++)/Cad is also due to B4GALNT2 alterations, its coding region and 2 kbp upstream were sequenced in five Cad individuals. No genetic changes were associated with this phenotype but a detailed erythroid Cad glycoprotein profile was obtained, especially for GLPA (O-glycosylation) and, for the first time, B3AT (N-glycosylation). In conclusion, the p.Cys406Arg β4GalNAc-T2 variant causes Sda-deficiency in humans, while the enigmatic Cad phenotype remains unresolved, albeit further characterized.
2022-04-07 | PXD023943 | Pride
Project description:SILAC analysis to comparing mitotic chromosome between Wild type and BAZ1B KO (or BAZ1A/B double KO)
| PXD008696 | JPOST Repository
Project description:Peroxisomes are versatile single membrane-enclosed cytoplasmic organelles, involved in reactive oxygen species (ROS) and lipid metabolism and diverse other metabolic processes. Peroxisomal disorders result from mutations in Pex genes-encoded proteins named peroxins (PEX proteins) and single peroxisomal enzyme deficiencies. The PEX11 protein family (α, β, and γ isoforms) plays an important role in peroxisomal proliferation and fission. However, their specific functions and the metabolic impact caused by their deficiencies have not been precisely characterized. To understand the systemic molecular alterations caused by peroxisomal defects, here we utilized untreated peroxisomal biogenesis factor 11α knockout (Pex11α KO) mouse model and performed serial relative-quantitative lipidomic, metabolomic, and proteomic analyses of serum, liver, and heart tissue homogenates. We demonstrated significant specific changes in the abundances of multiple lipid species, polar metabolites, and proteins and dysregulated metabolic pathways in distinct biological specimens of the Pex11α KO adult mice in comparison to the wild type (WT) controls. Overall, the present study reports comprehensive semi-quantitative molecular omics information of the Pex11α KO mice, which might serve in the future as a reference for a better understanding of the roles of Pex11α and underlying pathophysiological mechanisms of peroxisomal biogenesis disorders.
2022-02-02 | MTBLS1887 | MetaboLights
Project description:To investigate the molecular mechanisms by which KIBRA regulates exosome secretion, we performed mass spectral (MS) analysis and an isobaric tag for relative and absolute quantitation (iTRAQ) assay to screen the differentially-expressed proteins in the brains of KIBRA-KO mice compared with their WT littermates.
2019-04-02 | PXD012430 | Pride
Project description:Abstract Aim: Circulating triglyceride and triglyceride-rich lipoprotein (TRL) accumulation is increasingly recognized as a residual atherosclerotic risk, but their specific effect in cardiac remodeling and heart failure (HF) remain largely unexplored. Here we investigated this issue in Gpihbp1 knockout (KO) mice, which develop severe hyperchylomicronemia due to disruption of intravascular TRL hydrolysis . Methods: Cardiac lipid metabolism and remodeling were evaluated in 10-month-old Gpihbp1 KO mice and wild-type littermates under physiological conditions. Mice were also subjected to transverse aortic constriction (TAC) to evaluate the impact of severe hyperchylomicronemia on pressure overload-induced remodeling and HF. Furthermore, Gpihbp1 KO mice were crossed into Ldlr KO background to study hyperchylomicronemia’s effects on hemorheology and high-fat diet (HFD)-induced cardiac pathology. Results: Untargeted cardiac lipidomics revealed 214 differentially regulated lipid species specifically enriched in glycerophospholipids, fatty acid (FA) and diacylglycerol subclasses. qPCR confirmed down-regulated FA oxidation genes and upregulated glucose utilization genes. Electron microscopy showed swollen mitochondria with fragmented cristae, and RNA-seq demonstrated reduced respiratory-chain gene expression. These derangements culminated in impaired cardiac contractile performance in 10-month-old Gpihbp1 KO mice without inducing hypertrophy or fibrosis. After TAC, Gpihbp1 KO hearts exhibited exaggerated diastolic dysfunction, increased myocyte hypertrophy, and fibrosis. In Gpihbp1/Ldlr double knockout (dKO) mice, reduced erythrocyte deformability and increased whole blood viscosity were observed and worsened post-HFD. Additionally, HFD feeding precipitated significant diastolic impairment, cardiac hypertrophy and fibrosis in dKO mice. Conclusion: Severe hyperchylomicronemia due to GPIHBP1 deficiency sensitizes the heart to pathological remodeling and HF. These findings indicate a potential pathogenic contribution of HTG and TRL accumulation to cardiac disease.
2026-06-11 | MTBLS14749 | MetaboLights
Project description:GBA variants are among the most significant genetic risk factors for synucleinopathies including Parkinson’s disease and dementia with Lewy bodies. The GBA gene encodes the lysosomal enzyme glucocerebrosidase (GBA), which is essential for glycosphingolipid catabolism. There is a reciprocal relationship between GBA and -synuclein ( -syn), in which reduced GBA levels lead to elevated -syn. To explore this relationship specifically within neurons in vivo, we have introduced a human pathogenic variant of -syn, A53T, into a neuron-specific Gba-KO mouse. This double variant mouse exhibited a reduced lifespan relative to the neuron-specific Gba-KO mouse and more pronounced weight loss, demonstrating a faster disease course and more severe phenotype than neuron-specific Gba-KO mice. Additionally, their brains showed elevated levels of glucosylceramide (GlcCer) and phosphorylated -syn compared to the single-variant mice. Surprisingly, glucosylsphingosine (GlcSph) levels were comparable between double-variant and neuron-specific Gba-KO mice, suggesting impaired GlcSph generation. A small number of genes were significantly different between double variant and neuron-specific Gba-KO mice. These findings suggest that GlcCer accumulation, due to GBA loss, interacts with -syn in neurons, driving increased pathogenic -syn levels and modulating GlcCer metabolism.
2026-02-01 | GSE289837 | GEO
Project description:Liver gene expression profile of wild type, liver-specific PTEN KO, SCAP KO and PTEN/SCAP double KO mice.
| PRJNA715216 | ENA