人类leukotriene-C4合成酶的分子克隆和表达。
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豪泽Welsch DJ,克里族DP, SD,马西斯KJ, Krivi GG,•艾萨克森电脑
人类leukotriene-C4合成酶的分子克隆和表达。
《美国国家科学院刊S a . 1994年10月11日;91 (21):9745 - 9。
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7937884 (在PubMed]
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Leukotriene-C4合成酶(LTC4S;EC 2.5.1.37)催化peptidoleukotrienes生物合成的关键步骤,在哮喘的发病机制是重要的。抗体生成基于部分合成肽氨基酸序列之前报道人类LTC4S (D.W.尼科尔森阿里,。瓦兰蔻,摩根大通、Calaycay jr,芒福德,Zamboni R.J. & Ford-Hutchinson, a . w . (1993) Proc。国家的。学会科学。美国90年、2015 - 2019年)和专门detergent-solubilized LTC4S从THP-1细胞,获得确认公布的序列与酶活性有关。Inosine-containing基于部分蛋白质寡核苷酸序列被用来隔离679 - bp cDNA LTC4S THP-1细胞。互补脱氧核糖核酸含有一个开放阅读框,编码150个氨基酸的蛋白质(M (r) = 16568),计算π值为11.1。推导出的蛋白质序列是主要由疏水性氨基酸组成; hydropathy analysis predicts three transmembrane domains connected by two hydrophilic loops. Analysis of the deduced sequence identified two potential protein kinase C phosphorylation sites and a potential N-linked glycosylation site. The amino acid sequence for human LTC4S is unique and shows no homology to other glutathione S-transferases. LTC4S was found to be most similar to 5-lipoxygenase activating protein (31% identity, 53% similarity), another protein involved in leukotriene biosynthesis. Active enzyme was expressed in bacterial, insect, and mammalian cells as shown by the biosynthesis of LTC4 in incubation mixtures containing LTA4 and reduced glutathione. The cloning and expression of human LTC4S provide the basis for a better understanding of this key enzyme in peptidoleukotriene biosynthesis.