GEO DataSets

Analysis of MEFs deficient in ER thiol oxidases (ERO1a, ERO1b) and PRDX4, enzymes that initiate the disulfide relay. Combined loss-of-function mutations compromise the extracellular matrix and interfere with procollagen maturation. Results provide insight into the molecular basis of these defects.

Organism:

Mus musculus

Type:

Expression profiling by array, transformed count, 3 genotype/variation sets

Platform:

GPL6246

Series:

GSE39492

9 Samples

Download data: CEL, CHP

(Submitter supplied) Endoplasmic reticulum (ER) thiol oxidases initiate a disulfide relay to oxidatively-fold secreted proteins. We found that combined loss-of-function mutations in genes encoding the ER thiol oxidases ERO1alpha, ERO1beta and PRDX4, compromised the extracellular matrix in mice and interfered with the intracellular maturation of procollagen. These severe abnormalities were associated with an unexpectedly-modest delay in disulfide bond formation in secreted proteins but a profound, five-fold lower procollagen 4 hydroxyproline content and enhanced cysteinyl sulfenic acid modification of ER proteins. more...

Organism:

Mus musculus

Type:

Expression profiling by array

Dataset:

GDS4507

Platform:

GPL6246

9 Samples

Download data: CEL, CHP

(Submitter supplied) The overall cellular response to oxidative stress generated by Ero1α in the lumen of the mammalian endoplasmic reticulum (ER) is poorly characterized. Here, we investigate the effects of overexpressing a hyperactive mutant (C104A/C131A) of Ero1α. Using microarray analysis, we demonstrate that the cell reacts to the oxidative challenge caused by Ero1α hyperactivity by turning on the unfolded protein response. more...

Organism:

Homo sapiens

Type:

Expression profiling by array

Platform:

GPL6244

12 Samples

Download data: CEL