Polar brain extracts (from SC and 2 and 200 μg/L fenitrothion exposures, each n = 6) resuspended in methanol/water were analyzed by DIMS and processed as for nontargeted analysis.
Brain extracts from PME-1 mice contained essentially no demethylated form of PP2A (Fig. 3A).
We performed, for the first time, a metabolomic study of brain extracts from Mecp2-null mice by using high-resolution magnetic resonance spectroscopy.
However, brain extracts from Epm2a-/ mice do not present any detectable alteration in the regulation of the UPR and proteasomal function.
GST-Parkin interacted with the Parkin substrate, α-tubulin, but not with PS129-α-synuclein when added to brain extracts from symptomatic hA30Pα-syn mice (Figure 7A).
In contrast, UMB-2 did not detect any immunoreactive band in embryonic brain extracts from CXCR4-deficient mice (Figure 2 A, left panel) and only a very weak band in brain extracts from adult CXCR4+/+ mice (Figure 2 A, right panel).
Spinal cord and brain extracts from normal and carrier mice display very efficient snRNP assembly, which is dramatically impaired in the corresponding extracts of severe SMA mice (Figure 3A and 3B).
However, Parkin did not bind to PS129-α-synuclein in brain extracts from hA30Pα-syn mice, and it was unable to promote the ubiquitylation of phosphorylated α-synuclein in vitro.
Signals were detected using the ImageQuant LAS4000 (GE Healthcare) and densitometric analysis was performed using the GeneTools software (Syngene, Frederick, MD) using the brain extracts from the vehicle cohort as reference for normalization.
Delocalization of PKA might also lead to compensatory changes in PKA-R subunit levels and western blots were performed on brain extracts from WT, KO, and D36 mice to examine this possibility.
