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Updated: Sep 18, 2025
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Enrichment of Detergent-insoluble Protein Aggregates from Human Postmortem Brain
Published on: October 24, 2017
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Differences in the soluble and insoluble proteome between primary tauopathies.
Tomas Kavanagh1, Kaleah Balcomb1, Stephanie Trgovcevic1
1Brain and Mind Centre and School of Medical Sciences, University of Sydney, Camperdown, New South Wales, Australia.
Summary
Protein solubility differs across primary tauopathies like corticobasal degeneration (CBD), Pick's disease (PiD), and progressive supranuclear palsy (PSP). These solubility patterns reveal distinct disease processes and protein alterations in the brain.
Area of Science:
- Neuroscience
- Proteomics
- Biochemistry
Background:
- Primary tauopathies, including corticobasal degeneration (CBD), Pick's disease (PiD), and progressive supranuclear palsy (PSP), are characterized by aggregated tau pathology in the brain.
- Alterations in other proteins are implicated in these diseases but remain poorly understood.
Purpose of the Study:
- To characterize protein solubility differences across three primary tauopathies: CBD, PiD, and PSP.
- To investigate how protein solubility patterns diverge or converge between these tau-related neurodegenerative diseases.
Main Methods:
- Sarkosyl fractionation of post-mortem human brain tissue from CBD, PiD, and PSP cases (n=5/group).
- Assessment of protein differences in soluble and insoluble fractions.
- Analysis of protein solubility changes, enrichment, and correlation.
Main Results:
- Corticobasal degeneration (CBD) and Pick's disease (PiD) exhibited the highest proteomic similarity in both soluble and insoluble fractions.
- Progressive supranuclear palsy (PSP) demonstrated the most divergent proteomic profile compared to CBD and PiD.
- Significant changes in protein solubility were observed for lysosomal regulators, postsynaptic proteins, extracellular matrix (ECM) components, and mitochondrial proteins.
Conclusions:
- This study provides the first contrast of protein solubility patterns across three primary tauopathies.
- Distinct protein solubility profiles highlight divergent disease mechanisms in CBD, PiD, and PSP.
- Specific proteins like SORT1, ROCK1, and JAK2, along with unique lysosomal proteins, show differential solubility and aggregation patterns across tauopathies.
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