Cellular glutathione peroxidase as a predominant scavenger of hydroperoxyeicosatetraenoic acids in rabbit alveolar macrophages.
Cellular glutathione peroxidase as a predominant scavenger of hydroperoxyeicosatetraenoic acids in rabbit alveolar macrophages.
复制标题
细胞谷胱甘肽过氧化物酶作为兔肺泡巨噬细胞中氢过氧二十碳四烯酸的主要清除剂。
DOI：
10.1248/bpb.22.1047
复制
发表时间：
1999
影响因子：
2
通讯作者：
Y. Nakagawa
中科院分区：
文献类型：
--
作者：
N. Chiba;H. Imai;K. Narashima;M. Arai;G. Oshima;M. Kunimoto;Y. Nakagawa
兔肺泡巨噬细胞胞浆中含有大量过氧化物酶，可在谷胱甘肽存在下将5-氢过氧二十碳四烯酸（5-HPETE）还原为5-羟基二十碳四烯酸（5-HETE）。该过氧化物酶纯度为69倍，整体活性回收率为18.5%。经凝胶过滤，酶的分子量约为80 kDa，经十二烷基硫酸钠聚丙烯酰胺凝胶电泳（SDS-PAGE）还原，酶的分子量为23.1 kDa。纯化的过氧化物酶的氨基末端序列与兔肝细胞谷胱甘肽过氧化物酶（cGPx）基因的序列完全一致。在纯化过程中未观察到将5-HPETE还原为5-HETE的其他活性。提示cGPx在肺泡巨噬细胞脂质氢过氧化物尤其是HPETE的代谢中起重要作用。
The cytosol of rabbit lung alveolar macrophages contains a high amount of peroxidase, which reduces 5-hydroperoxyeicosatetraenoic acid (5-HPETE) to 5-hydroxyeicosatetraenoic acid (5-HETE) in the presence of glutathione. This peroxidase was purified 69-fold to homogeneity with overall recovery of activity of 18.5%. The molecular mass of the enzyme was approximately 80 kDa by gel filtration, and emerged as a single band at 23.1 kDa under reducing condition by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The amino-terminal sequence of the purified peroxidase was completely identical to the sequence deduced from cellular glutathione peroxidase (cGPx) gene of rabbit liver. No other activity that reduces 5-HPETE to 5-HETE was observed during purification. These results suggest that cGPx plays an important role in metabolism of lipid hydroperoxides, especially HPETE, in lung alveolar macrophages.