Department of Chemistry & Biochemistry, Kennesaw State University, Kennesaw, GA 30144-1203, USA.
FEBS Open Bio. 2012 Feb 28;2:51-5. doi: 10.1016/j.fob.2012.02.002. Print 2012.
Endothelial nitric oxide synthase (eNOS) contains a motif similar to recognition sequences in known MAPK binding partners. In optical biosensing experiments, eNOS bound p38 and ERK with ∼100 nM affinity and complex kinetics. Binding is diffusion-limited (k on ∼ .15 × 10(6) M(-1) s(-1)). Neuronal NOS also bound p38 but exhibited much slower and weaker binding. p38-eNOS binding was inhibited by calmodulin. Evidence for a ternary complex was found when eNOS bound p38 was exposed to CaM, increasing the apparent dissociation rate. These observations strongly suggest a direct role for MAPK in regulation of NOS with implications for signaling pathways including angiogenesis and control of vascular tone.
内皮型一氧化氮合酶 (eNOS) 含有与已知 MAPK 结合伙伴的识别序列相似的模体。在光学生物传感实验中，eNOS 以约 100 nM 的亲和力和复杂的动力学与 p38 和 ERK 结合。结合是扩散限制的 (k on 约为 1.5 × 10(6) M(-1) s(-1))。神经元型一氧化氮合酶也与 p38 结合，但结合速度较慢且较弱。p38-eNOS 结合受钙调蛋白抑制。当 eNOS 结合 p38 暴露于 CaM 时，发现了三元复合物的证据，从而增加了表观解离速率。这些观察结果强烈表明 MAPK 在调节 NOS 方面发挥直接作用，这对包括血管生成和血管张力控制在内的信号通路具有重要意义。
