3,3 ',4,4 ' -四氯联苯在鱼类,鸟类和爬行动物中的氧化:与细胞色素P450 1A失活和活性氧产生的关系

Jennifer J Schlezinger, Jennifer Keller, Lori A Verbrugge, John J Stegeman
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引用次数: 109

摘要

先前我们发现,多氯联苯3,3 ',4,4 ' -四氯联苯(TCB)可引起鱼的细胞色素P450 1A (CYP1A)以及大鼠和人的CYP1A1释放活性氧(ROS)。这与TCB和nadph依赖的酶氧化失活有关,在猪和大鼠中,这与TCB氧化率呈负相关。我们研究了其他脊椎动物(包括鳐(Raja erinacea)、鳗鱼(Anguilla rostrata)、鳉鱼(Fundulus heteroclitus)、美洲鲽鱼(Pleuronectes americanus)、鸡(Gallus domesticus)、鸬鹚(Phalacrocorax auritus)、海鸥(Larus argentatus)和龟(Chrysemys picta picta))肝微体中TCB氧化率、CYP1A失活率和ROS产生率之间的关系。用芳烃受体激动剂处理后,所有鱼和鸟的TCB氧化率均被诱导。诱导的TCB氧化率在所有鱼类中为1 pmol/min/mg,在鸟类中为6-14 pmol/min/mg。在所有物种中,TCB氧化率与EROD率呈正相关,表明CYP1A可能参与了TCB氧化。用TCB+NADPH孵育大多数物种的肝微粒体导致EROD立即(TCB依赖性)抑制,并逐渐丧失EROD能力,表明CYP1A的氧化失活与scup类似。NADPH刺激肝微粒体产生ROS (H2O2和/或O2−),在某些物种(鳗鱼)中轻微,而在其他物种(鸡、龟)中则显著。在鸟类和鱼类中,nadph刺激的ROS产生与EROD活性呈正相关。TCB能显著刺激比目鱼、鳉鱼、鸬鹚、海鸥和水嘴鱼的肝微粒体产生活性氧。CYP1A失活和ROS生成的刺激表明,在许多物种中,TCB使CYP1A解偶联,当在物种之间进行比较时,CYP1A失活率与TCB氧化率呈负相关。结合/活性位点拓扑结构的某些特征可能会阻碍TCB氧化,从而增加活性位点氧化物质攻击的可能性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
3,3′,4,4′-Tetrachlorobiphenyl oxidation in fish, bird and reptile species: relationship to cytochrome P450 1A inactivation and reactive oxygen production

Previously we showed that the polychlorinated biphenyl 3,3′,4,4′-tetrachlorobiphenyl (TCB) caused a release of reactive oxygen species (ROS) from cytochrome P450 1A (CYP1A) of the fish scup (Stenotomus chrysops), and from rat and human CYP1A1. This was linked to a TCB- and NADPH-dependent oxidative inactivation of the enzyme, which in scup and rat was inversely related to the rates of TCB oxidation. We examined the relationship between rates of TCB oxidation, CYP1A inactivation and ROS production in liver microsomes from additional vertebrate species, including skate (Raja erinacea), eel (Anguilla rostrata), killifish (Fundulus heteroclitus), winter flounder (Pleuronectes americanus), chicken (Gallus domesticus), cormorant (Phalacrocorax auritus), gull (Larus argentatus), and turtle (Chrysemys picta picta). TCB oxidation rates were induced in all fish and birds treated with aryl hydrocarbon receptor agonists. Induced rates of TCB oxidation were <1 pmol/min/mg microsomal protein in all fish, and 6–14 pmol/min/mg in the birds. In all species but one, TCB oxidation rates correlated positively with EROD rates, indicating likely involvement of CYP1A in TCB oxidation. Incubation of liver microsomes of most species with TCB+NADPH resulted in an immediate (TCB-dependent) inhibition of EROD, and a progressive loss of EROD capacity, indicating an oxidative inactivation of CYP1A like that in scup. NADPH stimulated production of ROS (H2O2 and/or O2) by liver microsomes, slightly in some species (eel) and greatly in others (chicken, turtle). Among the birds and the fish, NADPH-stimulated ROS production correlated positively with EROD activity. TCB caused a significant stimulation of ROS production by liver microsomes of flounder, killifish, cormorant and gull, as well as scup. The stimulation of CYP1A inactivation and ROS generation indicates an uncoupling of CYP1A by TCB in many species, and when compared between species, the rates of CYP1A inactivation correlated inversely with rates of TCB oxidation. Some feature(s) of binding/active site topology may hinder TCB oxidation, enhancing the likelihood for attack of an oxidizing species in the active site.

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