Enzymes involved in the metabolism of γ-hydroxybutyrate in SH-SY5Y cells: Identification of an iron-dependent alcohol dehydrogenase ADHFe1
Enzymes involved in the metabolism of γ-hydroxybutyrate in SH-SY5Y cells: Identification of an iron-dependent alcohol dehydrogenase ADHFe1
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DOI：
10.1016/j.cbi.2008.10.025
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发表时间：
2009-03-16
影响因子：
5.1
通讯作者：
Ellis, Elizabeth M.
中科院分区：
文献类型：
--
作者：
Lyon, Robert C.;Johnston, Stuart M.;Ellis, Elizabeth M.
在人神经母细胞瘤细胞系SH-SY 5 Y中研究了内源性代谢物γ-羟基丁酸（GHB）的代谢，作为检查神经元代谢的模型。我们表明，GHB可以合成和释放这些细胞，表明GHB合成和分泌的途径存在。报道了参与GHB代谢的主要酶的活性，并且可以通过RT-PCR检测AKR 1A 1、AKR 7A 2、ALDH 5A 1和GABA-T的转录物。我们还证明了ADHFe 1转录本的存在，据报道该基因编码羟酸-含氧酸反式氢化酶（HOT）。我们发现ADHFe 1基因与细菌GHB脱氢酶相关，并具有保守的NAD结合位点。讨论了利用SH-SY 5 Y细胞系研究GHB催化剂的潜力。(C)2008爱思唯尔爱尔兰有限公司保留所有权利。
The metabolism of the endogenous metabolite gamma-hydroxybutyrate (GHB) has been studied in a human neuroblastoma cell line SH-SY5Y as a model for examining neuronal metabolism. We show that GHB can be synthesized and released from these cells, indicating that pathways for GHB synthesis and secretion are present. Activities for the major enzymes that are involved in GHB metabolism are reported, and transcripts for AKR1A1, AKR7A2, ALDH5A1 and GABA-T can be detected by RT-PCR. We also demonstrate the presence of the ADHFe1 transcript, a gene that has been reported to encode a hydroxyacid-oxoacid trans hydrogenase (HOT). We show that the ADHFe1 gene is related to bacterial GHB dehydrogenases and has a conserved NAD-binding site. The potential for using the SH-SY5Y cell line for investigating GHB catabolism is discussed. (C) 2008 Elsevier Ireland Ltd. All rights reserved.