Insolubilome profiling defines molecular features that influence protein insolubility with aging - PubMed
9 hours ago
- #aging
- #protein solubility
- #proteostasis
- Insolubilome profiling identifies molecular features affecting protein insolubility during aging.
- Mass spectrometry reveals tissue-specific insoluble/soluble protein ratios in young mice, varying widely (100-1,000×).
- Aging alters protein solubility: some proteins become more insoluble, others less, and some remain unaffected.
- Age-related solubility changes are not solely based on tissue similarity and differ in tissues with varying degeneration tendencies.
- Structural features correlate with tissue-specific changes in protein solubility with aging.
- Proteins becoming insoluble in multiple organs include aggregation-prone circulating factors and ectopically expressed proteins.
- Example: Hornerin, primarily expressed in epidermis, increases in insolubility in aging skeletal muscle; its upregulation causes muscle weakness.
- Age-insoluble proteins serve as biomarkers and may contribute to functional decline, indicating a complex remodeling of the insolubilome with aging.