培养的大鼠心肌细胞中丙酮酸脱氢酶激酶的长期调节
Longer-term regulation of pyruvate dehydrogenase kinase in cultured rat cardiac myocytes.
作者信息
Marchington D R, Kerbey A L, Randle P J
机构信息
Nuffield Department of Clinical Biochemistry, John Radcliffe Hospital, Oxford, U.K.
出版信息
Biochem J. 1990 Apr 1;267(1):245-7. doi: 10.1042/bj2670245.
Abstract
The increased activity of pyruvate dehydrogenase (PDH) kinase induced in hearts of rats by starvation for 48 h was maintained following preparation of cardiac myocytes, and it was also maintained, though at a decreased level, after 25 h of culture in medium 199. This loss of PDH kinase activity was not prevented by n-octanoate, dibutyryl cyclic AMP or glucagon. The PDH kinase activity of myocytes from fed rats was increased to that of starved rats after 25 h of culture with n-octanoate, dibutyryl cyclic AMP or both agents together.
摘要
饥饿48小时诱导的大鼠心脏丙酮酸脱氢酶（PDH）激酶活性增加，在制备心肌细胞后仍得以维持，并且在199培养基中培养25小时后，尽管水平有所下降，但仍保持不变。正辛酸、二丁酰环磷酸腺苷或胰高血糖素均不能阻止PDH激酶活性的这种丧失。用正辛酸、二丁酰环磷酸腺苷或两种试剂共同培养25小时后，喂食大鼠的心肌细胞的PDH激酶活性增加到饥饿大鼠的水平。
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