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Essential functions of glycans in human epithelia dissected by a CRISPR/Cas9-engineered human organotypic skin model

ABSTRACT: We used RNA_Seq to quantify cellular transcripts in human immortalized N/TERT-1 keratinocytes upon knock out of genes delineating key subtypes of glycosylation pathways in humans.

ORGANISM(S): Homo sapiens

PROVIDER: GSE148284 | GEO | 2020/05/15

REPOSITORIES: GEO

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Essential Functions of Glycans in Human Epithelia Dissected by a CRISPR-Cas9-Engineered Human Organotypic Skin Model.

Project description: Not available

| S-EPMC7497784 | biostudies-literature

Essential functions of glycans in human epithelia dissected by a CRISPR/Cas9-engineered human organotypic skin model

Project description:The glycome undergoes characteristic changes during histogenesis and organogenesis, but our understanding of the importance of select glycan structures for tissue formation and homeostasis is incomplete. Here, we present a human organotypic platform that allows genetic dissection of cellular glycosylation capacities and systematic interrogation of the roles of distinct glycan types in tissue formation. We used CRISPR-Cas9 gene targeting to generate a library of 3D organotypic skin tissues that selectively differ in their capacity to produce glycan structures on the main types of Nand O-linked glycoproteins and glycolipids. This tissue library revealed distinct changes in skin formation associated with a loss of features for all tested glycoconjugates. The organotypic skin model provides phenotypic cues for the distinct functions of glycoconjugates, and serves as a unique resource for further genetic dissection and identification of the specific structural features involved. The strategy is also applicable to other organotypic tissue models.

2021-09-09 | PXD018418 | Pride

Essential functions of glycans in human epithelia dissected by a CRISPR/Cas9-engineered human organotypic skin model

Project description:Essential functions of glycans in human epithelia dissected by a CRISPR/Cas9-engineered human organotypic skin model

| PRJNA623735 | ENA

O-glycan initiation directs distinct biological pathways and controls epithelial differentiation

Project description:We used RNA_Seq to quantify cellular transcripts in human spontaneously immortalized HaCaT keratinocytes upon knock out of GALNT1, GALNT2, or GALNT3 - most abundantly expressed enzyme isoforms initiating mucin-type O-linked glycosylation.

2020-01-10 | GSE141387 | GEO

Invasive three-dimensional organotypic neoplasia from multiple normal human epithelia.

Project description: Not available

| S-EPMC3586217 | biostudies-literature

The role of glycans and glycosylation in cell-type specific effects on viral infectivity

Project description:Our lab has previously used the Glyco v3 gene-chip to analyze RNA from human macrophages and T-cells, as part of a project examining the effect of cellular origin on the viral infectivity of HIV/SIV. Our experiments have led us to hypothesize that the different glycosylation pathways present in macrophages and T-cells result in the production of virions with differently glycosylated viral proteins and different glycans present on the virion surface. Furthermore, studies with glycosidases using the Glyco v3 gene-chip have indicated that these differences in the glycosylation profiles of virions derived from different cell types may influence viral infectivity. Here we used glyco v3 chips for identifying the enzymes active in the glycosylation pathways of 174xCEM and 293 cells, which are cell types commonly used in HIV and SIV research. These analyses will allow us a better understanding of the role of glycans and glycosylation in cell-type specific effects on viral infectivity because there is a much larger amount of data on virus derived from these cell types and we will be able to relate our studies more directly to previous work in our lab and other labs. RNA from 174xCEM and HEK293 cells, cell types commonly used in HIV and SIV research, was isolated and sent to Microarray Core (E). RNA was prepared in duplicate, totaling 4 samples. Samples were labeled and hybridized to the GLYCOv3 array and gene expression patterns were used to identify enzymes active in glycosylation pathways.

2011-06-14 | E-GEOD-29924 | biostudies-arrayexpress

The role of glycans and glycosylation in cell-type specific effects on viral infectivity

2011-06-14 | GSE29924 | GEO

Sialylation of N-linked glycans influences the immunomodulatory effects of IgM on T cells

Project description:Human serum IgM antibodies are composed of heavily glycosylated polymers with five glycosylation sites on the μ (heavy) chain and one glycosylation site on the J chain. In contrast to IgG glycans, which are vital for a number of biological functions, virtually nothing is known about structure-function relationships of IgM glycans. Natural IgM is the earliest immunoglobulin produced and recognizes multiple antigens with low affinity, whilst immune IgM is induced by antigen exposure and is characterized by a higher antigen specificity. Natural anti-lymphocyte IgM is present in the serum of healthy individuals and increases in inflammatory conditions. It is able to inhibit T cell activation, but the underlying molecular mechanism is not understood. Here we show, for the first time, that sialylated N-linked glycans induce the internalization of IgM by T cells, which in turn causes severe inhibition of T cell responses. The absence of sialic acid residues abolishes these inhibitory activities, showing a key role of sialylated N-glycans in inducing the IgM-mediated immune suppression.

2014-11-11 | E-MTAB-3030 | biostudies-arrayexpress

O-glycan inhibitors generate aryl-glycans, induce apoptosis, and inhibit growth in colorectal cancer cell lines

Project description:Our studies provide direct evidence that O-glycosylation pathways play a role in the regulation of cell growth through apoptosis and proliferation pathways. Eight small molecular weight analogues of the GalNAc-alpha-1-O-serine/threonine structure based on 1-benzyl-2-acetamido-2- deoxy-alpha-O-D-galactopyranoside have been synthesised and tested in 5 human colorectal cancer cell lines. Three inhibitors, 1-benzyl-2-acetamido-2-deoxy-alpha-O-D-galactopyranoside and the corresponding 2-azido- and C-glycoside analogues, were screened in two colorectal cancer cell lines at 0.5mM and showed induction of apoptosis. Proliferation was down regulated in the same two cell lines with all three inhibitors, as detected by Ki67 staining and gene array. Treatment both cell lines with inhibitors led to changes in glycosylation detected with peanut lectin. The competitive action of the inhibitors resulted in the intracellular formation of 28 aryl-glycan products which were identified by MALDI and electrospray mass spectroscopy. The structures found map onto known O-glycosylation biosynthetic pathways and showed a differential pattern for each of the inhibitors in both cell lines. Gene array analysis of the glycogenes illustrated a pattern of glycosytransferases that matched the glycan structures found in glycoproteins and aryl-glycans formed in the PC/AA/C1/SB10C cells, however there was no action of the three inhibitors on glycogene transcript levels. The inhibitors act at both intermediary metabolic and genomic levels, resulting in altered protein glycosylation and arylglycan formation. These events may play a part in growth arrest. Keywords: Response to inhibitors, Apoptosis, Aryl-glycans, Benzyl-O-GalNAc, Growth Inhibition, O-Glycans

2008-08-18 | GSE12422 | GEO

Protocol for CRISPR-Cas9 modification of glycosylation in 3D organotypic skin models.

Project description: Not available

| S-EPMC8403582 | biostudies-literature