Browning M, Bennett W F, Kelly P, Lynch G
Brain Res. 1981 Aug 10;218(1-2):255-66. doi: 10.1016/0006-8993(81)91305-6.
We have previously shown that brief periods of high frequency synaptic stimulation of the rat hippocampus influence the endogenous phosphorylation of a 40,000 Mr brain protein (Browning et al.). The results of the present study demonstrate that this brain phosphoprotein is enriched in a purified mitochondrial fraction and co-migrates with the alpha-subunit of pyruvate dehydrogenase in sodium dodecyl sulfate polyacrylamide gels. Comparisons of total and partial proteolytic fingerprints indicate that the two proteins are essentially identical. In addition, the phosphorylation of the 40,000 Mr brain protein is sensitive to both dichloroacetate and magnesium as has been reported for pyruvate dehydrogenase. Taken together these data provide persuasive evidence that the brain protein is the alpha-subunit of pyruvate dehydrogenase and thereby raise the possibility that even very short periods of synaptic activity influence an enzyme of particular importance to mitochondrial metabolism in brain.
我们之前已经表明，对大鼠海马体进行短时间高频突触刺激会影响一种40000道尔顿脑蛋白的内源性磷酸化（布朗宁等人）。本研究结果表明，这种脑磷酸蛋白在纯化的线粒体组分中含量丰富，并且在十二烷基硫酸钠聚丙烯酰胺凝胶中与丙酮酸脱氢酶的α亚基迁移率相同。对完整和部分蛋白水解指纹图谱的比较表明，这两种蛋白基本相同。此外，正如丙酮酸脱氢酶的情况一样，40000道尔顿脑蛋白的磷酸化对二氯乙酸和镁都敏感。综合这些数据提供了有说服力的证据，表明该脑蛋白是丙酮酸脱氢酶的α亚基，从而增加了这样一种可能性，即即使是非常短时间的突触活动也会影响对脑线粒体代谢特别重要的一种酶。
