Developmental studies of phospholipid-sensitive Ca2+-dependent protein kinase and its substrates and of phosphoprotein phosphatases in rat brain.

Developmental studies of phospholipid-sensitive Ca2+-dependent protein kinase and its substrates and of phosphoprotein phosphatases in rat brain.
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大鼠脑中磷脂敏感性 Ca2+ 依赖性蛋白激酶及其底物以及磷蛋白磷酸酶的发育研究。

DOI:
10.1073/pnas.81.10.3143
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发表时间:
1984
影响因子:
11.1
通讯作者:
Kuo,JF
Kuo,JF
中科院分区:
综合性期刊1区
文献类型:
--
作者:
Turner,RS;Raynor,RL;Mazzei,GJ;Girard,PR;Kuo,JF

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研究了大鼠脑蛋白磷酸化/去磷酸化系统的个体发生变化。结果发现,出生后灰质和白质颗粒部分和灰质可溶性部分中磷脂敏感Ca2+依赖性蛋白激酶(PL-Ca-PK)活性水平迅速显著升高,在第30天达到最高水平,此后略有下降或保持不变。相比之下,白质可溶性部分的酶水平在整个大脑发育和成熟过程中保持不变。还注意到PL-Ca-PK底物蛋白的各种个体发生变化。髓鞘碱性蛋白和其他底物(特别是灰质中的Mr 87,000, 58,000, 54,000和50,000蛋白)的水平在发育过程中逐渐增加,在成年期达到最高水平。另一方面,来自白质和灰质颗粒部分的Mr 66000蛋白水平在出生后迅速增加,在第18天达到峰值,然后在成年期下降到初始新生儿水平。PL-Ca-PK及其许多底物水平增加的时间尺度与大脑发育和成熟(突触发生和髓鞘形成)的时间尺度相似。磷酸化蛋白磷酸酶的活性水平(使用32p标记的髓磷脂碱性蛋白、组蛋白和硫酸鱼精蛋白进行测定)在发育过程中,来自不同大脑区域的某些部分仅轻微(高达60%)增加或减少,这表明与去磷酸化相比,磷酸化在决定细胞蛋白的磷酸化状态方面可能更重要。
Ontogenetic changes in the protein phosphorylation/dephosphorylation systems in rat brain were investigated. It was found that the activity level of phospholipid-sensitive Ca2+-dependent protein kinase (PL-Ca-PK) in the particulate fraction of grey and white matter and the soluble fraction of grey matter increased rapidly and markedly after birth, reached the highest level at day 30, and declined slightly or remained unchanged thereafter. The enzyme level in the soluble fraction of white matter, in contrast, remained constant throughout the development and maturation of brain. Various ontogenetic changes in the substrate proteins for PL-Ca-PK were also noted. The levels of myelin basic protein and other substrates (notably the Mr 87,000, 58,000, 54,000, and 50,000 protein in grey matter) progressively increased during development, reaching the highest level at adulthood. The level of the Mr 66,000 protein from the particulate fraction of white and grey matter, on the other hand, increased rapidly after birth, reached a peak at day 18, and then declined to the initial neonatal level at the adult stage. The time scale for the increases in the levels of PL-Ca-PK and its many substrates paralleled that of brain development and maturation (synaptogenesis and myelinogenesis). The activity levels of phosphoprotein phosphatases (assayed using 32P-labeled myelin basic protein, histone, and protamine sulfate) were found to only slightly (up to 60%) increase or decrease in certain fractions from different brain regions during development, suggesting that phosphorylation, compared to dephosphorylation, may be more important in determining the phosphorylation state of cellular proteins.
DOI: 10.1016/s0006-291x(83)80157-0
发表时间: 1983
影响因子: 3.1
作者:
Ashendel,CL;Staller,JM;Boutwell,RK
通讯作者: Boutwell,RK