Adult versus P7 mouse brain gene expression
Ontology highlight
ABSTRACT:
ORGANISM(S): Mus musculus
SUBMITTER: Steven Head
PROVIDER: E-GEOD-27348 | biostudies-arrayexpress |
REPOSITORIES: biostudies-arrayexpress
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Project description:Dr. Schwarting's research is focused on the analysis of developmentally regulated cell surface molecules and their role in axon guidance and neuronal migration, using the olfactory system as a model. The interaction of cell surface glycans with endogenous lectins in the extracellular matrix provides one mechanism by which axons can utilize specific pathways as they grow towards their targets. We have a mutant mouse (b3GNT2 KO) that up-regulates the expression of lactosamine containing glycans in a subset of olfactory neurons. Gene expression profiling was performed using control and mutant mice that up-regulate the expression of lactosamine containing glycans in a subset of olfactory neurons. Glycosyltransferase expression that differed between control and mutant mice were identified.
2011-03-02 | E-GEOD-27590 | biostudies-arrayexpress
Project description:Dr. Stanley's laboratory is interested in 1) understanding the biological roles of specific classes of N-glycan in development and immunity through studies of glycosyltransferase mutant mice, 2) identifying complex binding specificities of galectins using a panel of CHO glycosylation mutants, and 3) determining how O-fucose glycans function in Notch receptor signaling and in modulating the interaction of Notch receptors with their ligands. The bisecting GlcNAc on N-glycans inhibits ricin binding and enhances E-PHA binding. It is expected that mammalian CBP's, including galectins, may have their binding affected positively or negatively by the presence of the bisecting GlcNAc. In fact unpublished experiments have identified reduced binding of at least one galectin to LEC10 CHO cells that express GlcNAc-TIII compared to CHO cells that do not. We have shown that the Mgat3 gene that encodes GlcNAc-TIII, the glycosyltransferase that adds the bisecting GlcNAc, is barely expressed in E9.5 mouse embryos and robustly expressed in E10.5 embryos (J. Biol. Chem. 277, 26300-26309; 2002). We wish to compare glycosylation and lectin genes that are expressed at E10.5 in the brain of embryos from wild type and Mgat3 knockout embryos. RNA samples were prepared from several embryo heads (3) from Mgat3+/+ and Mgat3-/- E10.5 embryos. We hybridized the RNA to glyco-chips (in triplicate per sample for a total of 6) so we can detect changes in the expression of glyco-genes as well as signaling pathway genes that may be affected.
2011-02-04 | E-GEOD-27055 | biostudies-arrayexpress
Project description:This laboratory focuses on the interactions of murine CD4+CD25+ regulatory T cells (Tregs) with CD4+CD25- T cells, both from a fundamental biological point of view, and in the context of a murine model of lupus. This study characterized the surface glycans expressed by CD25 and CD25- CD4 T cells selected from lupus-prone (systemic lupus erythematosus or SLE) mouse strains MRL/Mp and NZB/W F1 and two control strains, CBA/Ca (haplotype-matched with the MRL/Mp; H-2k) and BALB/c. A transcriptomic survey of freshly isolated and bead-activated CD25 and CD25- CD4 T cells selected from mouse spleens was conducted using these four strains. Three replicate samples of each condition were hybridized to the GLYCOv2 array, for a total of 48 samples.
2011-03-02 | E-GEOD-27591 | biostudies-arrayexpress
Project description:alpha-dystroglycan is a component of the dystrophin associated glycoprotein complex that binds components of the extracellular matrix (including laminin, perlecan and neurexin) via its carbohydrate groups. Recently, a group of muscular dystrophies have been identified due to the aberrant glycosylation of this molecule (dystroglycanopathies). The overexpression of the glycosyltransferase LARGE in several cell lines results in alpha-dystroglycan hyperglycosylation and enhanced ligand binding. The glycan structures induced by LARGE overexpression are unknown. We have injected into mouse legs two LARGE constructs, one wild type and the second in which a DxD motif has been mutated to NNN as a control. We aim to identify genes unregulated during LARGE induced hyperglycosylation in order to gain insight into the enzymes involved in this process and ultimatley the nature of the glycans responsible for ligand binding. RNA preparations from two LARGE constructs, were sent to Microarray Core (E). One wild type and the second in which a DxD motif has been mutated to NNN as a control. The aim is to identify genes unregulated during LARGE induced hyperglycosylation in order to gain insight into the enzymes involved in this process and ultimatley the nature of the glycans responsible for ligand binding. The RNA was amplified, labeled, and hybridized to teh GLYCOv3 microarrays.
2011-04-29 | E-GEOD-28932 | biostudies-arrayexpress
Project description:Uterine leiomyomas are the most common benign tumor in humans causing significant morbidity with vaginal bleeding, pelvic pressure and pain. Histologically, leiomyomas show a large degree of extracellular matrix disorganization. I am working with a colleague who recently found Notch pathway gene expression were clearly altered in fibroids (“Differential expression of the Notch signal transduction pathway: ligands, receptors and Numb in uterine leiomyomas vs. myometrium,” G. Christman, H. Tang, I. Ahmad, J. Stribley, Fertility and Sterility, Volume 88, Supp 1, S72, September 2007). Glycosaminoglycan expression was found to be over-expressed in uterine leiomyomas compared to myometrial samples (Fertility and Sterility, Vol 88 Supp 1, S106, September, 2007), but glycosyltransferase and glycosidase expression has not been reported. We have purified RNA samples from paired uterine leiomyoma and normal myometrium from a previous clinical study. Dr. Domino's laboratory hypothesis is that Notch pathway activation inhibits apoptosis in uterine leiomyomas leading to fibroid growth. Notch ligands are fucosylated glycans. The bulk of a fibroid is the extracellular matrix yet little has been studied on leiomyocyte expression of enzymes that model glycans in the extracellular matrix. RNA preparations of paired samples of excess human tissues from hysterectomies, with two different groups normal myometrium, and leiomyoma tumors were sent to Microarray Core (E). The RNA was amplified, labeled, and hybridized to GLYCO_v3 microarrays.
2011-04-29 | E-GEOD-28945 | biostudies-arrayexpress
Project description:Bronchial inflammation is common in patients suffering from Cystic Fibrosis (CF) and is commonly responsible for mortality from CF. It is known that this inflammation has an influence over glycosylation events in bronchial mucins and abnormal glycosylation has been described in CF. These abnormalities can not be directly linked to CF, as the cells that secrete bronchial mucins do not express CFTR. This study is to determine if bronchial inflammation could be responsible for abnormal glycoslylation in CF. Pro-inflammatory cytokines TNF, IL6, and IL8, as well as anti-inflammatory cytokine IL10 are present and seem to have active roles in the respiratory tree of CF patients. In this study, the effects of these cytokines on the expression of glycosyl- and sulfotransferases involved in the biosynthesis of O-glycans in the bronchial cell line Calu-3 were analyzed. Three replicates for each cytokine treated group and controls were hybridized to GLYCOv2 array.
2011-03-02 | E-GEOD-27594 | biostudies-arrayexpress
Project description:Dr. Schwarting's research is focused on the analysis of developmentally regulated cell surface molecules and their role in axon guidance and neuronal migration, using the olfactory system as a model. The interaction of cell surface glycans with endogenous lectins in the extracellular matrix provides one mechanism by which axons can utilize specific pathways as they grow towards their targets. Beta3GnT1 mutant mice lose lactosamine expression and have an olfactory axon guidance phenotype (Henion et al, 2005). Olfactory neurons are capable of regeneration and we know that when these neurons regenerate in beta3GnT1 mutant they synthesize lactosamine by a secondary mechanism. By comparing RNA from the olfactory epithelium from wild type and mutant mice, we would expect to see the upregulation of glycosyltransferases that could produce lactosamine in the absence of beta3GnT1. In a preliminary experiment carried out by the CFG staff, we saw that radical fringe, a beta 3GnT, was upregulated in the olfactory epithelium, although it is probably not responsible for the new lactosamine expression. beta3GnT1 Knock out. Strain info: The b3GnT1 mice were generated on a mixed 129Ola-C57BL/6 background and backcrossed to C57BL/6 for four generations. They were then crossed to I7-Internal ribosomal entry site (IRES)-tau greeen fluorescent protein (GFP) mice generated by Dr. Peter Mombaerts. RNA preparations from wild type and beta3GnT1 mutant mouse olfactory epithelium were sent to Microarray Core (E). Three replicate samples from each condition were used in the study. The RNA was amplified, labeled, and hybridized to the GLYCOv3 microarrays. Data was analyzed to determine glycosyltransferase expression changes in beta3GnT1 mutant mice, with specific interest on glycosyltransferases that could produce lactosamine in the in the absence of beta3GnT1.
2011-04-29 | E-GEOD-28926 | biostudies-arrayexpress
Project description:Dr. Esko's laboratory focuses on the structure, function, and biosynthesis of glycoproteins and proteoglycans. This laboratory also works on the design and synthesis of small molecule inhibitors of glycosylation. We analyzed the expression patterns of glycosyltransferase, growth factors, and receptors in endothelial cells derived from NDST1 deficient and wild-type mice using cancer cell line types U937 and LS180 .
2011-02-17 | E-GEOD-27351 | biostudies-arrayexpress
Project description:Gene expression patterns were surveyed using RNA from 4 different murine sources. Four classes of RNA were analyzed: undifferentiated embryonic stem cells, differentiated ES cells, kidney and liver tissues. Classes were prepared in triplicate for a total of 12 samples. All samples were hybridized to the custom designed CFG GLYCOv2 glycogene array. Analysis results were used for comparison with parallel experiments using qRT-PCR.
2011-03-02 | E-GEOD-27595 | biostudies-arrayexpress
Project description:In collaboration with Professor Anne Dell at the South Kensington Campus of Imperial College London, we have conducted preliminary glycomic surveys of C57BL/6 CD25+ and CD25- CD4+ T cells. Cells selected in serum-containing culture medium demonstrated unusual N-glycan profiles compared to those prepared in phosphate buffered saline (PBS). These profiles were subsequently shown to result from cellular sequestration of glycoproteins present in fetal calf serum (FCS) used to supplement the medium (1). Analysis of the N-glycan profile of murine CD4+CD25+ Tregs prepared in PBS revealed distinct differences from CD4+CD25- T cells – namely, a reduction in sialic acid capping and loss of core fucose. Preliminary studies are underway to ascertain the minimum medium required to sustain general T cell survival, whilst maintaining ‘clean’ glycomic profiles. The effect of glycoprotein withdrawal on CD25+ and CD25- CD4+ T cells in culture was investigated by selecting the cells in FCS-free medium and incubating them for six hours with either FCS-containing medium, or PBS supplemented with FCS, fetuin or fetuin-derived glycans. Early apoptosis was measured using Annexin-V (BD Biosciences, Heidelberg, Germany) and late apoptosis using 7-aminoactinomycin D (7-AAD) (BD Biosciences), in parallel with a complementary apoptosis detection method – measurement of the mitochondrial membrane potential using the BD™ Mitoscreen Kit (BD Biosciences). This apoptosis staining study demonstrated that there was a remarkably higher percentage of death in both CD25+ and CD25- CD4+ T cells cultured in PBS versus cells cultured in RPMI-1640 or medium containing FCS. Both CD25+ and CD25- CD4+ T cells were highly susceptible to apoptosis in glycoprotein-free medium, demonstrating their exquisite sensitivity to the lack of glycoprotein survival factors. Continuing studies are addressing the minimum medium required to sustain cells undergoing polyclonal activation in vitro and the impact of activation on the N-glycan profiles of Tregs versus conventional T cells. To complement this work, we used Core E resources to investigate glycosyltransferase gene expression in freshly isolated versus activated C57BL/6 CD25+ and CD25- CD4+ T cells.
2011-06-14 | E-GEOD-29925 | biostudies-arrayexpress