Wingler K, Brigelius-Flohé R
German Institute of Human Nutrition, Potsdam-Rehbrücke, Institute of Nutritional Science, University of Potsdam.
Biofactors. 1999;10(2-3):245-9. doi: 10.1002/biof.5520100223.
The gastrointestinal glutathione peroxidase (GI-GPx) is the fourth member of the GPx family. In rodents, it is exclusively expressed in the gastrointestinal tract, in humans also in liver. It has, therefore, been discussed to function as a primary barrier against the absorption of ingested hydroperoxides. A vital function of GI-GPx can be deduced from the unusual stability of its mRNA under selenium-limiting conditions, the presence of low amounts of GI-GPx protein in selenium deficiency where cGPx is absent, and the fast reappearance of the GI-GPx protein upon refeeding of cultured cells with selenium compared to the slower reappearance of cGPx protein. Furthermore, the Secis efficiency of GI-GPx is low when compared to cGPx and PHGPx. It is, however, almost independent of the selenium status of the cells tested. All these characteristics rank GI-GPx high in the hierarchy of selenoproteins and point to a role of GI-GPx which might be more crucial than that of cGPx, at least in the gastrointestinal system.
胃肠道谷胱甘肽过氧化物酶(GI-GPx)是谷胱甘肽过氧化物酶(GPx)家族的第四个成员。在啮齿动物中,它仅在胃肠道表达,在人类中还在肝脏表达。因此,有人认为它作为抵御摄入的氢过氧化物吸收的主要屏障发挥作用。GI-GPx的重要功能可以从其mRNA在硒限制条件下的异常稳定性、硒缺乏时(此时不存在细胞溶质谷胱甘肽过氧化物酶(cGPx))低量GI-GPx蛋白的存在,以及与cGPx蛋白较慢重新出现相比,用硒重新喂养培养细胞后GI-GPx蛋白快速重新出现推断出来。此外,与cGPx和磷脂氢谷胱甘肽过氧化物酶(PHGPx)相比,GI-GPx的硒代半胱氨酸插入序列(Secis)效率较低。然而,它几乎与所测试细胞的硒状态无关。所有这些特征使GI-GPx在硒蛋白等级体系中处于高位,并表明GI-GPx的作用可能比cGPx更关键,至少在胃肠道系统中如此。