PHOSPHORYLATION BY CALCIUM CALMODULIN-DEPENDENT PROTEIN KINASE-II AND PROTEIN-KINASE-C MODULATES THE ACTIVITY OF NITRIC-OXIDE SYNTHASE
PHOSPHORYLATION BY CALCIUM CALMODULIN-DEPENDENT PROTEIN KINASE-II AND PROTEIN-KINASE-C MODULATES THE ACTIVITY OF NITRIC-OXIDE SYNTHASE
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DOI：
10.1016/s0006-291x(05)81351-8
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发表时间：
1991-11-14
影响因子：
3.1
通讯作者：
MURAD, F
中科院分区：
文献类型：
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作者：
NAKANE, M;MITCHELL, J;MURAD, F
从大鼠脑中纯化的一氧化氮合酶是钙离子和钙调素依赖性的，它可被钙调素依赖性蛋白激酶II和蛋白激酶C磷酸化。钙钙调蛋白依赖性蛋白激酶II的磷酸化导致酶活性显著降低（对照的33%），而不改变辅因子的要求，而蛋白激酶C磷酸化后观察到酶活性适度增加（对照的140%）。这些发现表明，脑一氧化氮合酶活性可能不仅由Ca ~（2+）/钙调素和几个辅助因子，但也通过磷酸化调节。
Nitric oxide synthase purified from rat brain, which is Ca2+and calmodulin dependent, was phosphorylated by calcium calmodulin-dependent protein kinase II as well as protein kinase C. Phosphorylation by calcium calmodulin-dependent protein kinase II resulted in a marked decrease in enzyme activity (33% of control) without changing the co-factor requirements, whereas a moderate increase in enzyme activity (140% of control) was observed after phosphorylation by protein kinase C. These findings indicate that brain nitric oxide synthase activity may be regulated not only by Ca2+/calmodulin and several co-factors, but also by phosphorylation.