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Expression data of E13.5 mouse Blood Brain Barrier and lung endothelial cells

ABSTRACT: Following the identification of a critical time window of Blood Brain Barrier formation in the mouse embryo, we aimed to identify genes important for barriergenesis. To this end, we isolated cortical and lung E13.5 endothelial cells and compared expression between the two populations. The working hypothesis was that endothelial cells which are actively building a barrier would have a uniqe pattern of gene expression that would be detectable in comparison to a non-barrier endothelial population that is also active in vasculogenesis.

ORGANISM(S): Mus musculus

PROVIDER: GSE56777 | GEO | 2014/05/14

SECONDARY ACCESSION(S): PRJNA244557

REPOSITORIES: GEO

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Expression data of E13.5 mouse Blood Brain Barrier and lung endothelial cells

Project description:Following the identification of a critical time window of Blood Brain Barrier formation in the mouse embryo, we aimed to identify genes important for barriergenesis. To this end, we isolated cortical and lung E13.5 endothelial cells and compared expression between the two populations. The working hypothesis was that endothelial cells which are actively building a barrier would have a uniqe pattern of gene expression that would be detectable in comparison to a non-barrier endothelial population that is also active in vasculogenesis. E13.5 Tie2-GFP embryos were micro-dissected for cortex and lungs. Cortex tissue was carefully cleared of the meninges and choroid plexus. FACS purification of GFP positive cells and GeneChip analysis was applied . All material from a single litter (10-13 embryos) was pooled and considered as a biological replicate. n=4 litters.

2014-05-14 | E-GEOD-56777 | biostudies-arrayexpress

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High glucose levels increase influenza-associated damage to the pulmonary epithelial-endothelial barrier

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2020-02-14 | GSE145232 | GEO

Interactome of Ca2+-bound secretagogin in mouse embryonic (E13.5) pancreas

Project description:By using His6-tagged recombinant human secretagogin in the presence of Ca2+ (100 µM), we isolated its putative interacting partners from mouse embryonic (E13.5) pancreata and identified their amino acid sequences by mass spectrometry. Next to previously described interacting partners (participating in vesicle-mediated transport, cytoskeletal organization and members of chaperonin-containing complex), we found a substantial group of proteins involved in proteasomal catabolic process including 15 different subunits of the 26S proteasome. Our data support that secretagogin protects Pdx1 from proteasomal degradation to control a transcriptional program required for β cell specification.

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