STIMULATION OF TYROSINE-SPECIFIC PROTEIN-PHOSPHORYLATION IN THE RAT-LIVER PLASMA-MEMBRANE BY OXYGEN RADICALS
STIMULATION OF TYROSINE-SPECIFIC PROTEIN-PHOSPHORYLATION IN THE RAT-LIVER PLASMA-MEMBRANE BY OXYGEN RADICALS
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DOI：
10.1016/s0006-291x(86)80010-9
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发表时间：
1986-09-01
影响因子：
3.1
通讯作者：
HOCHSTEIN, P
中科院分区：
文献类型：
--
作者：
CHAN, TM;CHEN, E;HOCHSTEIN, P
加入组蛋白和共聚物Glu80Tyr20后，大鼠肝细胞质膜的~(32)P掺入内源性蛋白质的能力被包括甲萘二酮在内的几种萘醌类化合物显著增加。这种刺激最明显的是Glu80 Tyr20，对二硫苏糖醇或还原型谷胱甘肽有绝对需求，并被超氧化物歧化酶、过氧化氢酶和去铁胺抑制，程度取决于所用的苯二酚。它们在刺激明显的酪氨酸特异性蛋白磷酸化方面的有效性与依赖DIT的氧化还原循环的速率有关，通过耗氧量来衡量。从与苯二酚孵育的肝细胞中分离出的颗粒组分也增加了蛋白质的磷酸化。提出了苯二酚促进蛋白质磷酸化的自由基机制。
Incorporation of 32P from [.gamma.-32P]ATP into endogenous proteins, added histone and the copolymers Glu80Tyr20 by rat liver plasma membranes was markedly increased by several naphthoquinones, including menadione. This stimulation was most marked with Glu80 Tyr20, has an absolute requirement for either dithiothreitol or reduced glutathione, and was inhibited by superoxide dismutase, catalase, and desferrioxamine to varying degrees depending on the quinones used. Their effectiveness in stimulating the apparent tryosine-specific protein phoshorylation correlated with the rates of DIT-dependent redox cycling measured by oxygen consumption. Increased protein phosphorylation was also seen with particulate fractions isolated from hepatocytes incubated with quinones. A free radical-mediated mechanism is suggested for the quinone stimulation of protein phosphorylation.