REGULATION OF PYRUVATE-DEHYDROGENASE INTERCONVERSION IN ISOLATED HEPATOCYTES BY MITOCHONDRIAL ATP-ADP RATIO
REGULATION OF PYRUVATE-DEHYDROGENASE INTERCONVERSION IN ISOLATED HEPATOCYTES BY MITOCHONDRIAL ATP-ADP RATIO
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DOI：
10.1016/0014-5793(75)80811-8
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发表时间：
1975-01-01
期刊：
影响因子：
3.5
通讯作者：
WIELAND, OH
中科院分区：
文献类型：
--
作者：
SIESS, EA;WIELAND, OH
最近Wieland和Portenhauser证明离体大鼠肝线粒体中丙酮酸脱氢酶(PDH)(EC 1.2.4.1.)磷酸化程度与线粒体内腺嘌呤核苷酸(AN)的磷酸化状态有关[1]。为了了解这种机制在完整细胞中是否也有效，我们研究了 ATP 生成或易位抑制剂对分离肝细胞中 PDH 活性和线粒体 AN 水平的影响。通过利用 Zuurendonk 和 Tager [2] 开发的分离线粒体和线粒体外区室的方法，我们可以证明，就像在分离的线粒体中一样，完整肝细胞中 PDH 磷酸化和线粒体 ATP/ADP 比率之间存在明显的相关性。
Recently Wieland and Portenhauser have shown that the degree of pyruvate dehydrogenase (PDH)(EC 1.2. 4.1.) phosphorylation in isolated rat liver mitochondria is related to the phosphorylation state of intramitochondrial adenine nucleotides (AN)[l]. In order to see whether this mechanism is operative also in the intact cell we studied the effect of inhibitors of ATP generation or translocation on PDH-activities and mitochondrial AN levels in isolated hepatocytes. By taking advantage of the method developed by Zuurendonk and Tager [2] for the separation of mitochondrial and extramitochondrial compartments we could demonstrate that, like in isolated mitochondria, a clear correlation between PDH phosphorylation and the mitochondrial ATP/ADP ratio exists in intact liver cells.