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首页> 美国卫生研究院文献>other >THE IMMUNOPROTEASOME THE 20S PROTEASOME AND THE PA28αβ PROTEASOME REGULATOR ARE OXIDATIVE-STRESS-ADAPTIVE PROTEOLYTIC COMPLEXES
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THE IMMUNOPROTEASOME THE 20S PROTEASOME AND THE PA28αβ PROTEASOME REGULATOR ARE OXIDATIVE-STRESS-ADAPTIVE PROTEOLYTIC COMPLEXES

机译：免疫促进剂20S蛋白酶体和PA28αβ蛋白酶体调节剂是氧化应激 - 适应性蛋白水解络合物

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Oxidized cytoplasmic and nuclear proteins are normally degraded by proteasome, but accumulate with age and disease. We demonstrate the importance of various forms of the proteasome during transient (reversible) adaptation (hormesis), to oxidative stress in murine embryonic fibroblasts. Adaptation was achieved by ‘pre-treatment’ with very low concentrations of H2O2, and tested by measuring inducible resistance to a subsequent, much higher ‘challenge’ dose of H2O2. Following an initial direct physical activation of pre-existing proteasomes, 20S proteasome, immunoproteasome, and PA28αβ regulator, all exhibited substantially increased de novo synthesis during adaptation over 24 hours Cellular capacity to degrade oxidatively damaged proteins increased with 20S proteasome, immunoproteasome, and PA28αβ synthesis, and was mostly blocked by 20S proteasome, immunoproteasome, and PA28 siRNA knock-down treatments. Additionally, PA28αβ knockout mutants achieved only half the H2O2 induced adaptive increase in proteolytic capacity of wild-type controls. Direct comparison of purified 20S proteasome and immunoproteasome demonstrated that immunoproteasome can selectively degrade oxidized proteins. Cell proliferation and DNA replication both decreased, and oxidized proteins accumulated, during high H2O2 challenge, but prior H2O2 adaptation was protective. Importantly, siRNA knock-down of 20S proteasome, immunoproteasome, or PA28αβ regulator blocked 50–100% of these adaptive increases in cell division and DNA replication, and immunoproteasome knock-down largely abolished protection against protein oxidation.

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