McCormack J G
FEBS Lett. 1985 Jan 28;180(2):259-64. doi: 10.1016/0014-5793(85)81082-6.
The effects of intramitochondrial Ca2+ on the activities of the Ca2+-sensitive intramitochondrial enzymes, (i) pyruvate dehydrogenase (PDH) phosphate phosphatase, and (ii) oxoglutarate dehydrogenase (OGDH), were investigated in intact rat liver mitochondria by measuring (i) the amount of active PDH (PDHa) and (ii) the rate of decarboxylation of alpha-[l-14C]oxoglutarate (at non-saturating [oxoglutarate]), at different concentrations of extramitochondrial Ca2+. In the presence of Na+ and Mg2+, both PDH and OGDH could be activated by increases in extramitochondrial [Ca2+] within the expected physiological range (0.05-5 microM). When liver mitochondria were prepared from rats treated with adrenaline, and then incubated in Na-free media containing EGTA, both PDH and OGDH activities were found to be enhanced. Evidence is presented that the activation of these enzymes by adrenaline is brought about by a mechanism involving increases in intramitochondrial [Ca2+].
通过测量(i)活性丙酮酸脱氢酶(PDHa)的量以及(ii)在不同线粒体外Ca2+浓度下α-[l-14C]酮戊二酸的脱羧速率(在非饱和[酮戊二酸]浓度下),研究了线粒体内Ca2+对Ca2+敏感的线粒体内酶(i)丙酮酸脱氢酶磷酸酶和(ii)酮戊二酸脱氢酶(OGDH)活性的影响。在Na+和Mg2+存在的情况下,线粒体外[Ca2+]在预期的生理范围内(0.05 - 5 microM)升高时,PDH和OGDH均可被激活。当从用肾上腺素处理的大鼠制备肝线粒体,然后在含有EGTA的无钠培养基中孵育时,发现PDH和OGDH活性均增强。有证据表明,肾上腺素对这些酶的激活是通过一种涉及线粒体内[Ca2+]增加的机制实现的。