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Expression of enzymes involved in gag synthesis and degradation in cartilage aging and arthritis

ABSTRACT: Glycoarrays are used to identify differences in the expression of enzymes involved in gag synthesis and degradation in cartilage aging and arthritis. This experiment includes 3 samples from donors with and without growth factor stimulation. Samples are from human biopsy/necropsy origin. Human knee chondrocytes were grown in monolayer culture from 3 donors unstimulated or stimulated with TGFß1 (10ng/ml) for 6 hours.

ORGANISM(S): Homo sapiens

SUBMITTER: Steven Head

PROVIDER: E-GEOD-27350 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Expression of enzymes involved in gag synthesis and degradation in cartilage aging and arthritis

Project description:Glycoarrays are used to identify differences in the expression of enzymes involved in gag synthesis and degradation in cartilage aging and arthritis. This experiment includes 3 samples from donors with and without growth factor stimulation. Samples are from human biopsy/necropsy origin.

2011-02-17 | GSE27350 | GEO

Collagen-GAG Biocompatibility Tests

Project description:All mRNA was isolated after 8 hours of culture time in each of three culture conditions. (1) TCPS Plate, (2) Collagen-GAG 2 dimensional coated plate and (3) collagen-GAG three dimensional mesh. Keywords: ordered

2004-11-09 | GSE1937 | GEO

CLIP-seq analysis of WT and Gag chimera HIV-1 virions 3

Project description:To investigate how the major HIV-1 structural protein Gag packages viral genomes efficiently, we replaced the NC domain of Gag with RNA binding domains from heterologous cellular RNA binding proteins to generate Gag chimeras. We hypothesize that the Gag chimeras that preferentially bind to purine-rich RNA sequences will package viral genomes efficiently. We performed CLIP-seq to identify the RNA sequences bound by WT Gag and Gag chimeras in cells, at the plasma membrane, and in virions.

2024-11-30 | GSE281424 | GEO

CLIP-seq analysis of WT and Gag chimera HIV-1 virions 2

2024-11-30 | GSE281423 | GEO

CLIP-seq analysis of WT and Gag chimera HIV-1 virions 1

2024-11-30 | GSE281422 | GEO

Anabolic Indices of Matrix Proteins Identify Regenerative Small RNA Intrinsic to Human Cartilage

Project description:human articular cartilage from ankle, knee, and hip joints of osteoarthritis and non-osteoarthritis donors.

2024-08-23 | MSV000095686 | MassIVE

Transcription profiling of human fibroblasts grown on TCPS plates, Collagen-GAG 2 D plate and Collagen-GAG 3D mesh

2008-06-11 | E-GEOD-1937 | biostudies-arrayexpress

Sex-linked differences in glyco-gene expression in thymocytes

Project description:This laboratory is focusing on to clarify the biologic relevance of a virulence factor known as trans-sialidase from Trypanosoma cruzi, the agent of the Chagas disease (American trypanosomiasis). We are working with an enzyme able to directly transfer sialyl residues among macromolecules known as the trans-sialidase. It constitutes a virulence factor from Trypanosoma cruzi, the agent of the Chagas' Disease the American trypanosomiasis. We described the ability of this virulence factor to induce thymocyte apoptosis in vivo that happens after silayl residue mobilization. The apoptosis is mediated by the thymic epithelial cells in the nurse cell complex. By employing the microarray approach we wish to analyze the gene expression induced in the thymus after TS treatment. Examination of differential expression in thymocytes between male and female mice of genes related to glycosylation. RNA samples (in triplicate) purified from thymocytes were analyzed by Glyco-gene Chip analysis.

2011-02-04 | E-GEOD-27054 | biostudies-arrayexpress

Human lung tissue

Project description:Dr. Clausen's laboratory is interested in the structure, biosynthesis and genetic regulation of glycoconjugates, with a major focus on mucins. This laboratory is studying the glycosylation and secretion process of mucins and biological functions involving mucins. This lab is also interested in receptor modulation mediated by glycosylation or through glycosphingolipids. We have a particular interest in understanding how mucin type O-glycosylation is regulated. Mucin type O-glycosylation is controlled by the ppGalNAc-transferase multigene family. An estimated 23 iso-forms belong to this family, so the specific involvement of each individual iso-form in any given organ seems complex to understand. An initial attempt to comprehend how this multigene family regulates mucin type O-glycosylation, is to get insight into which iso-forms are expressed in different organs and cell types. For this reason we have generated monoclonal antibodies towards 7 iso-forms, and the list of ppGalNAc-T iso-form specific monoclonals is currently growing. We have done some immuno histochemistry on lung using the available monoclonals, but are keen on assessing the number of ppGalNAc-T's expressed in lung as determined this Glyco-array. We have focused on lung because a number of ppGalNAc-T acceptor polypeptides, belonging to the mucin gene family, are expressed in this organ. An RNA sample pooled from two independent adult human healthy lung tissue samples was analyzed

2010-11-30 | E-GEOD-25712 | biostudies-arrayexpress

Gene expression in wild type and Mgat3 mouse embryos

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

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