Protein oxidation and degradation caused by particulate matter
Ching-Huang Lai1, Chun-Nin Lee2,3, Kuan-Jen Bai2,4
1School of Public Health, National Defense Medical Center, Taipei, Taiwan.
Scientific Reports
|September 21, 2016
Summary
Particulate matter exposure causes protein oxidation and affects cell health. Different particle types trigger distinct cellular responses, impacting protein degradation pathways and proteotoxicity.
Area of Science:
- Environmental Health
- Cell Biology
- Toxicology
Background:
- Particulate matter (PM) influences cellular autophagy, but its role in selective autophagy is not fully understood.
- Understanding how PM induces protein oxidation and degradation is crucial for assessing its health impacts.
Purpose of the Study:
- To investigate the mechanisms of protein oxidation and degradation induced by different types of particulate matter.
- To elucidate the role of selective autophagy in PM-induced cellular damage.
Main Methods:
- Human epithelial A549 cells were exposed to diesel exhaust particles (DEPs), urban dust (UD), and carbon black (CB).
- Assessed cell survival, proliferation, protein adduct formation, methionine oxidation (MetO), and the activity of protein repair and degradation pathways (proteasome, autophagy, ubiquitin).
Main Results:
- DEPs and UD reduced cell survival and proliferation. DEPs formed benzo(a)pyrene diolepoxide (BPDE) protein adducts.
- Methionine oxidation was induced by all PM types. DEP exposure activated methionine repair, while UD inhibited it, leading to oxidized protein accumulation.
- CB induced proteasome and autophagy with ubiquitin accumulation, suggesting ubiquitin-dependent degradation.
- DEPs induced proteasome and autophagy without ubiquitin accumulation, suggesting ubiquitin-independent degradation.
Conclusions:
- Distinct particulate matter physicochemical properties lead to unique proteotoxic effects.
- Diesel exhaust particles may induce protein degradation via an ubiquitin-independent autophagy pathway.
- Urban dust and carbon black exhibit different mechanisms of protein oxidation and degradation compared to DEPs.
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