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Cao_detergent insoluble pellets_Cortex_proteomics

ABSTRACT: This dataset consists of 3 raw MS files, acquired on an Orbitrap Fusion mass spectrometer operated in Data Dependent Acquisition mode. The files are associated with a manuscript submitted for publication by Luyan Cao et al. titled: SPIN90 associates with mDia1 and the Arp2/3 complex to regulate cortical actin organisation. The manuscript defines the role of SPIN90 and its association with mDia1 and the Arp2/3 complex in the regulation of the actin cortex. The experiment is LC-MS/MS analysis of detergent-insoluble fractions of M2 whole cell lysates, performed in biological triplicates.

INSTRUMENT(S): LTQ Orbitrap XL

ORGANISM(S): Homo Sapiens (ncbitaxon:9606)

SUBMITTER: Philippe Roux

PROVIDER: MSV000085211 | MassIVE | Wed Apr 01 07:37:00 BST 2020

SECONDARY ACCESSION(S): PXD018318

REPOSITORIES: MassIVE

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Project description:A hallmark pathology of Alzheimer’s disease (AD) is the formation of amyloid ß (Aß) deposits that exhibit diverse localization and morphologies, ranging from diffuse to cored-neuritic deposits in brain parenchyma, with cerebral vascular deposition in leptomeningeal and parenchymal compartments. Most AD brains exhibit the full spectrum of pathologic Aß morphologies. In the course of studies to model AD amyloidosis, we have generated multiple transgenic mouse models that vary in the nature of the transgene constructs that are expressed; including the species origin of Aß peptides, the levels and length of Aß that is deposited, and whether mutant presenilin 1 (PS1) is co-expressed. These models recapitulate features of human AD amyloidosis, but interestingly some models can produce pathology in which one type of Aß morphology dominates. In prior studies of mice that primarily develop cored-neuritic deposits, we determined that Aß deposition is associated with changes in cytosolic protein solubility in which a subset of proteins become detergent-insoluble, indicative of secondary proteome instability. Here, we survey changes in cytosolic protein solubility across seven different transgenic mouse models that exhibit a range of Aß deposit morphologies. We find a surprisingly diverse range of changes in proteome solubility across these models. Mice that deposit human Aß40 and Aß42 in cored-neuritic plaques had the most robust changes in proteome solubility. Insoluble cytosolic proteins were also detected in the brains of mice that develop diffuse Aß42 deposits but to a lesser extent. Notably, mice with cored deposits containing only Aß42 had relatively few proteins that became detergent-insoluble. Our data provide new insight into the diversity of biological effects that can be attributed to different types of Aß pathology and support the view that fibrillar cored-neuritic plaque pathology is the more disruptive Aß pathology in the Alzheimer’s cascade.

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Cao_detergent insoluble pellets_Cortex_proteomics

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