Phosphatase inhibition with okadaic acid does not alter the relationship between force and myosin light chain phosphorylation in permeabilized smooth muscle.
Phosphatase inhibition with okadaic acid does not alter the relationship between force and myosin light chain phosphorylation in permeabilized smooth muscle.
复制标题
用冈田酸抑制磷酸酶不会改变通透平滑肌中力和肌球蛋白轻链磷酸化之间的关系。
DOI:
10.1016/0006-291x(89)92676-4
复制
发表时间:
1989
影响因子:
3.1
通讯作者:
Mooers,SU
中科院分区:
文献类型:
--
作者:
Siegman,MJ;Butler,TM;Mooers,SU
The phosphatase inhibitor, okadaic acid, has been used to test the hypothesis that myosin light chain phosphatase activity plays a central role in latchbridge formation in smooth muscle. In the permeabilized rabbit portal vein there is a non-linear relationship between myosin light chain phosphorylation and force production such that maximum force output occurs with about 50% phosphorylation. Treatment of the muscle with okadaic acid does not change this relationship even though there is a profound inhibition of phosphatase activity. The data suggest that dephosphorylation of the myosin light chain while the myosin is in the force producing state does not account for the high force output with low levels of light chain phosphorylation in smooth muscle.