Proteotoxicity
Proteotoxicity is toxicity caused by proteins, usually of misfolded proteins.[1] Examples of proteotoxic proteins are the prion protein, and several proteins that when mutated result in neurodegenerative disease and produce aggregates in brain tissues, such as amyloid-beta in Alzheimer's disease and huntingtin in Huntington's disease. It is hypothesized that chaperones and co-chaperones, collectively referred to as the chaperome, proteins that assist protein folding, antagonize proteotoxicity during aging and in protein misfolding-diseases to maintain proteostasis.[2][3][4]
See also
References
- ^ Douglas, P. M.; Dillin, A. (2010). "Protein homeostasis and aging in neurodegeneration". The Journal of Cell Biology. 190 (5): 719–729. doi:10.1083/jcb.201005144. PMC 2935559. PMID 20819932.
- ^ Douglas, P. M.; Summers, D. W.; Cyr, D. M. (2009). "Molecular chaperones antagonize proteotoxicity by differentially modulating protein aggregation pathways". Prion. 3 (2): 51–58. doi:10.4161/pri.3.2.8587. PMC 2712599. PMID 19421006.
- ^ Brehme M, et al. (2014). "A conserved chaperome sub-network safeguards protein homeostasis in aging and neurodegenerative disease". Cell Rep. 9: 1135–1150. doi:10.1016/j.celrep.2014.09.042. PMID 25437566.
- ^ Brehme M, Voisine C (2016). "Model systems of protein-misfolding diseases reveal chaperone modifiers of proteotoxicity". Dis Model Mech. 9. doi:10.1242/dmm.024703. PMID 27491084.
{{cite journal}}: Cite has empty unknown parameter:|1=(help)