Ketone-body metabolism in glioma and neuroblastoma cells.

Ketone-body metabolism in glioma and neuroblastoma cells.
复制标题

神经胶质瘤和神经母细胞瘤细胞中的酮体代谢。

DOI:
--
复制
发表时间:
1981
影响因子:
11.1
通讯作者:
H. Gershman
H. Gershman
中科院分区:
综合性期刊1区
文献类型:
--
作者:
M. Patel;J. Russell;H. Gershman

文献摘要

被引文献

相似文献

我们已经研究了酮体在神经母细胞瘤C1300和神经胶质瘤C6细胞,两个已建立的线的神经起源的代谢。这三种酮体代谢酶在两种细胞系中的相对比例与脑中正常情况下的比例相同(D-3-羟基丁酸脱氢酶低于乙酰乙酰辅酶A硫解酶低于3-酮酸辅酶A转移酶),前两种酶在神经胶质瘤细胞中的活性高于神经母细胞瘤,第三种酶在神经母细胞瘤细胞中的活性是神经胶质瘤细胞的2倍。随着培养物达到汇合,两种细胞系中3-酮酸CoA-转移酶(EC 2.8.3.5)的比活性增加,然后降低。酮体,特别是乙酰乙酸是两种细胞系中神经脂质合成的优选底物。在酮体存在下,两种细胞系的细胞中葡萄糖碳掺入脂质显著减少。添加乙酰乙酸,但不是DL-3-羟基丁酸的培养基中导致显着增加的3-酮酸CoA-转移酶的活性,也在神经母细胞瘤细胞,但不是神经胶质瘤细胞的乙酰乙酸氧化率。这些结果表明,这两种细胞系代谢酮体的能力存在特定差异,并且酮体代谢途径存在底物水平调节。因此,这两条线提供了一个潜在的有用的系统,这些酶的调节机制可以检查。
We have examined the metabolism of ketone bodies in neuroblastoma C1300 and glioma C6 cells, two established lines of neural origin. The three ketone body-metabolizing enzymes are present in cells of both lines in the relative proportions normally found in brain (D-3-hydroxybutyrate dehydrogenase less than acetoacetyl-CoA thiolase less than 3-ketoacid CoA-transferase), the activities of the first two are higher in glioma cells than in neuroblastoma, and that of the third is 2-fold higher in neuroblastoma cells than in glioma cells. The specific activity of 3-ketoacid CoA-transferase (EC 2.8.3.5) in both cell lines increased as the cultures achieved confluence, then decreased. Ketone bodies and especially acetoacetate are preferred substrates for synthesis of neural lipids in cells of both lines. The incorporation of glucose carbon into lipids is significantly reduced in cells of both lines in the presence of ketone bodies. Addition of acetoacetate but not DL-3-hydroxybutyrate to the culture medium resulted in a significant increase in the activity of 3-ketoacid CoA-transferase and also in the rate of acetoacetate oxidation in neuroblastoma cells but not glioma cells. These findings indicate that specific differences exist in the capacity of these two cell lines to metabolize ketone bodies and also that substrate-level regulation of the ketone body-metabolizing pathway exists. These two lines therefore provide a potentially useful system in which the mechanisms of regulation of these enzymes may be examined.