Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine.
Expression of human arginine decarboxylase, the biosynthetic enzyme for agmatine.
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DOI：
10.1016/j.bbagen.2003.11.006
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发表时间：
2004-01
期刊：
影响因子：
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通讯作者：
Meng-Yang Zhu;A. Iyo;J. Piletz;S. Regunathan
中科院分区：
文献类型：
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作者：
Meng-Yang Zhu;A. Iyo;J. Piletz;S. Regunathan
胍丁胺是由精氨酸脱羧酶（ADC）使L-精氨酸脱羧形成的一种胺，最近在哺乳动物脑和其他组织中发现。虽然来自植物和细菌的ADC的克隆和测序已被广泛报道，但哺乳动物酶的结构尚不清楚。利用同源性筛选方法，我们已经确定了一个人的cDNA克隆，表现出ADC活性时，在COS-7细胞中表达。该人ADC克隆的cDNA和推导的氨基酸序列不同于其它形式的ADC。人ADC是一种460个氨基酸的蛋白质，与哺乳动物鸟氨酸脱羧酶（ODC）具有约48%的同一性，但没有ODC活性。虽然幼稚COS-7细胞不产生胍丁胺，但当用ADC cDNA转染时，这些细胞能够产生胍丁胺，如通过HPLC所测量的。使用cDNA探针的北方印迹分析表明ADC信息在选择的人脑区域和其他人体组织中表达。
Agmatine, an amine formed by decarboxylation of l-arginine by arginine decarboxylase (ADC), has been recently discovered in mammalian brain and other tissues. While the cloning and sequencing of ADC from plant and bacteria have been reported extensively, the structure of mammalian enzyme is not known. Using homology screening approach, we have identified a human cDNA clone that exhibits ADC activity when expressed in COS-7 cells. The cDNA and deduced amino acid sequence of this human ADC clone is distinct from ADC of other forms. Human ADC is a 460-amino acid protein that shows about 48% identity to mammalian ornithine decarboxylase (ODC) but has no ODC activity. While naive COS-7 cells do not make agmatine, these cells are able to produce agmatine, as measured by HPLC, when transfected with ADC cDNA. Northern blot analysis using the cDNA probe indicated the expression of ADC message in selective human brain regions and other human tissues.