Park Y S, Suzuki K, Mumby S, Taniguchi N, Gutteridge J M
Department of Biochemistry, Osaka University Medical School, Suita, Japan.
Free Radic Res. 2000 Sep;33(3):261-5. doi: 10.1080/10715760000301421.
The neutrophil enzyme myeloperoxidase (MPO) purposefully makes hypochlorous acid (HOCl) as part of the cells defence against microbial infections. During cell lysis, however, MPO will be released into the extracellular environment where production of HOCl, a powerful oxidant, will lead to molecular damage. Extracellular MPO binds to the copper-containing protein caeruloplasmin (Cp) and prevents MPO making HOCl. Cp has several important antioxidant functions in extracellular fluids associated with its ability to catalyse oxidation of ferrous ions and to remove peroxides. The binding of MPO to Cp did not inhibit these important extracellular antioxidant activities of Cp, but in so doing it provided additional antioxidant protection against formation of HOCl.
中性粒细胞酶髓过氧化物酶（MPO）特意生成次氯酸（HOCl），作为细胞抵御微生物感染防御机制的一部分。然而，在细胞裂解过程中，MPO会释放到细胞外环境中，在那里，强氧化剂HOCl的产生会导致分子损伤。细胞外的MPO与含铜蛋白铜蓝蛋白（Cp）结合，阻止MPO生成HOCl。Cp在细胞外液中具有多种重要的抗氧化功能，这与其催化亚铁离子氧化和清除过氧化物的能力有关。MPO与Cp的结合并未抑制Cp这些重要的细胞外抗氧化活性，但这样做提供了额外的抗氧化保护，防止HOCl的形成。
