Krieg P, Kinzig A, Heidt M, Marks F, Fürstenberger G
Research Program on Tumor Cell Regulation, Deutsches Krebsforschungszentrum, Im Neuenheimer Feld 280, 69120 Heidelberg, Germany.
Biochim Biophys Acta. 1998 Mar 6;1391(1):7-12. doi: 10.1016/s0005-2760(97)00214-2.
Using a combination of PCR cloning and conventional screening procedures, we isolated from phorbol ester-treated mouse epidermis two full length cDNA clones encoding novel lipoxygenases. One of the cDNAs turned out to be identical to the recently cloned 8-lipoxygenase [Jisaka et al., J. Biol. Chem. 272 (1997) 24 410-24 416], the open reading frame of the second one corresponded to a protein of 701 amino acids with a calculated molecular mass of 80.6 kDa. The amino acid sequence showed 50.8% identity to human 15-lipoxygenase 2, approximately 40% to 5-lipoxygenase and 35% to 12- and 15-lipoxygenases. A unique structural feature is the insertion of 31 amino acid residues in the amino-terminal part of the molecule. Based on these data, we conclude that this epidermis-derived cDNA encodes a novel lipoxygenase isoform termed provisionally epidermis-type lipoxygenase 2 (e-LOX 2).
利用聚合酶链反应（PCR）克隆和传统筛选程序相结合的方法，我们从佛波酯处理的小鼠表皮中分离出两个编码新型脂氧合酶的全长cDNA克隆。其中一个cDNA与最近克隆的8-脂氧合酶相同[Jisaka等人，《生物化学杂志》272 (1997) 24410 - 24416]，另一个的开放阅读框对应于一个由701个氨基酸组成的蛋白质，计算分子量为80.6 kDa。该氨基酸序列与人类15-脂氧合酶2的同一性为50.8%，与5-脂氧合酶约为40%，与12-和15-脂氧合酶为35%。一个独特的结构特征是在分子的氨基末端部分插入了31个氨基酸残基。基于这些数据，我们得出结论，这个源自表皮的cDNA编码一种新型脂氧合酶同工型，暂称为表皮型脂氧合酶2（e-LOX 2）。
