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Truncated O-glycan connection to Cancer: Depletion of O-glycosyltransferase C1GALT1 leads to early PDAC onset and metastasis

ABSTRACT: Truncated O-glycan connection to Cancer: Depletion of O-glycosyltransferase C1GALT1 leads to early PDAC onset and metastasis

PROVIDER: PRJNA413293 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR6132160_1.fastq.gz	Fastqsanger.gz
	SRR6132160_2.fastq.gz	Fastqsanger.gz
	SRR6132170_1.fastq.gz	Fastqsanger.gz
	SRR6132170_2.fastq.gz	Fastqsanger.gz
	SRR6132180_1.fastq.gz	Fastqsanger.gz

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Truncated O-glycan connection to Cancer: Depletion of O-glycosyltransferase C1GALT1 leads to early PDAC onset and metastasis

Project description:Aberrant expression of truncated O-glycan structures, such as Tn and STn, is frequently observed in pancreatic ductal adenocarcinoma (PDAC). The focus of our study is to investigate the functional role of truncated O-glycans in PDAC progression and metastasis. Our study revealed that kmockout of C1GALT1 leads to increased expression of truncated glycans and accelerates PDAC progression and metastasis.

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Identify changes in gene expression during overexpression of the glycosyltransferase LARGE

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Screen glycosyltransferase ST6GalNAc2 KO mice and B4GalNT1/B4GalNT2 double KO mice relative to C75 Wild Type controls

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.

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Identify changes in gene expression during overexpression of the glycosyltransferase LARGE

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

Glycan and gene chip analysis of purified osteoclast cell populations

Project description:Osteoclast derived from macrophage lineage cells are responsible for bone resorption and important in bone remodeling. Emerging of a new discipline-osteoimmunology highlights the important connection between immunology and bone biology. We had mouse osteoclast's RNA samples analyzed by the consortium’s gene microarray and identified a number of significant changes in expression of genes involved in glycan biosynthesis. Osteoclasts were treated with: control, Rankl (Receptor activator of nuclear factor kappa-B ligand (RANKL), tunicamycin, and both rankl and tunicamycin. RNA preparations from osteoclasts purified from mice: control (1,2,3), Rankl (1,2,3), tunicamycin (1,2,3), and both rankl and tunicamycin (1,2,3) were sent to the Microarray Core (E). The RNA was amplified, labeled, and hybridized to the GLYCOv3 microarrays.

2011-04-29 | E-GEOD-28947 | biostudies-arrayexpress

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Project description:Deficiencies in the protein O-mannose β1,2-N-acetylglucosaminyltransferase 1 (POMGNT1), a glycosyltransferase involved in the elongation of classic O-mannosyl glycans, are mainly associated with muscle-eye-brain disease (MEB), a genetically heterogeneous congenital muscular dystrophy with brain and eye anomalies. Although occasional aberrant cell-cell adhesion has been observed in response to changes in POMGNT1 levels, direct molecular mechanisms are largely unknown. POMGNT1 knock-out HEK293T cells and fibroblasts derived from MEB patients were used to get deeper insight in POMGNT1 deficiency by the combination of biochemical, cell and molecular biological techniques with proteomics and glycan-profile.

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2017-04-27 | MSV000081020 | MassIVE

Glycosyltransferase Extl1 promotes CCR7-mediated dendritic cell migration to restrain infection and autoimmunity

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