Phenobarbital enhances the aldehyde dehydrogenase activity of rat hepatocytes in vitro and in vivo.
Phenobarbital enhances the aldehyde dehydrogenase activity of rat hepatocytes in vitro and in vivo.
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苯巴比妥在体外和体内增强大鼠肝细胞的乙醛脱氢酶活性。
DOI：
10.1111/j.1600-0773.1986.tb00191.x
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发表时间：
1986
期刊：
影响因子：
--
通讯作者：
Michalopoulos,G
中科院分区：
文献类型：
--
作者：
Marselos,M;Michalopoulos,G
用胶原酶灌注Long - Evans大鼠肝脏获得的肝细胞进行原代培养，检测醛脱氢酶（ALDH）。培养7 d后，基础ALDH活性、蛋白质含量和DNA含量显著降低。将培养物暴露于苯巴比妥（PB，培养基中3 mM）并不能阻止DNA含量的降低，尽管它使蛋白质保持在相对较高的水平。以丙醛、苯乙醛、苯甲醛和D -葡萄糖醛酸内酯为底物，以NAD为辅酶时，ALDH的活性不仅保持不变，而且显著增强。当用苯甲醛和NADP测量ALDH时，也注意到活性的相对增加。用PB （1mg /ml，在饮用水中2周）处理Long - Evans动物，会导致ALDH活性类似的相对增加。然而，从绝对值来看，与体外暴露后相比，PB体内处理后发现的酶活性更高。这些结果表明，在原代肝细胞培养中，PB可以大大增强ALDH活性，而不受任何间接内源性影响。
Aldehyde dehydrogenase (ALDH) was measured in primary cultures of hepatocytes obtained with collagenase perfusion from livers of Long‐Evans rats. After seven days in culture, basal ALDH activity, protein content and DNA content are significantly decreased. Exposure of the cultures to phenobarbital (PB, 3 mM in the media) does not prevent the decrease of DNA content, although it keeps protein at relatively higher levels. The activity of ALDH is not only preserved, but also significantly enhanced, when propionaldehyde, phenylacetaldehyde, benzaldehyde and D‐glucuronolactone are used as substrates and NAD as the coenzyme. A relative increase of activity is also noted when ALDH is measured with benzaldehyde and NADP. Treatment of Long‐Evans animals with PB (1 mg/ml, in drinking water for 2 weeks) leads to similar relative increases of the ALDH activity. In absolute values, however, enzyme activities found afterin vivotreatment with PB are higher, compared to those obtained afterin vitroexposure. These results show that ALDH activity can be greatly enhanced by PB in primary hepatocyte cultures, free from any indirect endogenous influences.