Phosphorylation-contraction coupling in smooth muscle: role of caldesmon.
Phosphorylation-contraction coupling in smooth muscle: role of caldesmon.
复制标题
平滑肌中的磷酸化-收缩耦合：卡尔德斯蒙的作用。
DOI：
10.1007/978-1-4615-2872-2_18
复制
发表时间：
1993
影响因子：
--
通讯作者：
Chalovich,JM
中科院分区：
文献类型：
--
作者：
Pfitzer,G;Fischer,W;Chalovich,JM
In intact smooth muscle strips from chicken gizzard, carbachol elicited brief, phasic contractions which were associated with a very rapid, transient phosphorylation of the 20 kDa myosin light chains. Phosphorylation was not significantly different from basal levels after 30 s while force still amounted to 50% of the peak value. The rate of tension decline could be increased by addition of atropine, even at apparently basal phosphorylation levels suggesting a phosphorylation independent regulation. The force, at a given level of phosphorylation, could also be modulated by addition of the actin binding, putative regulatory protein, caldesmon. Caldesmon, inhibits phosphorylation dependent force in skinned fiber bundles of chicken gizzard without affecting myosin light chain phosphorylation. This suggests that caldesmon might modulate contraction in smooth muscle. Moreover our results suggest that caldesmon does not function to maintain passive tension.
