Ca2+ can control vascular smooth-muscle thin filaments without caldesmon phosphorylation.
Ca2+ can control vascular smooth-muscle thin filaments without caldesmon phosphorylation.
复制标题
Ca2 可以控制血管平滑肌细丝，而无需钙结合蛋白磷酸化。
DOI：
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发表时间：
1986
影响因子：
4.1
通讯作者：
Steven B Marston
中科院分区：
文献类型：
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作者：
Steven B Marston
钙依赖性调节血管平滑肌细丝激活肌球蛋白MgATP酶涉及钙调蛋白。这种效应可能是由于钙调素与钙离子结合蛋白（如钙调蛋白）的直接相互作用或钙调素被钙依赖性激酶磷酸化。我已经发现，Ca 2+在不到10秒的时间内对主动脉细丝进行转换，而细丝中的钙调蛋白仅缓慢磷酸化（半衰期大于10分钟），最大磷酸化非常低（每7个钙调蛋白分子中有1个钙调蛋白分子）。因此，钙调素磷酸化假说是不成立的。
The Ca2+-dependent regulation of the activation of myosin MgATPase by vascular-smooth-muscle thin filaments involves caldesmon. This effect may be due to the direct interaction of caldesmon with a Ca2+-binding protein such as calmodulin or phosphorylation of caldesmon by a Ca2+-dependent kinase. I have found that Ca2+ switches on aorta thin filaments in less than 10 s, whereas the caldesmon in the thin filaments is phosphorylated only slowly (half-time greater than 10 min) and the maximum phosphorylation is very low (1 molecule per 7 molecules of caldesmon). I conclude that the phosphorylation of caldesmon hypothesis is untenable.