Protein kinase C increases force and slows relaxation in smooth muscle: evidence for regulation of the myosin light chain phosphatase.
Protein kinase C increases force and slows relaxation in smooth muscle: evidence for regulation of the myosin light chain phosphatase.
复制标题
蛋白激酶 C 增加平滑肌的力量并减缓松弛：肌球蛋白轻链磷酸酶调节的证据。
DOI：
10.1006/bbrc.1996.1182
复制
发表时间：
1996
影响因子：
3.1
通讯作者：
Brozovich,FV
中科院分区：
文献类型：
--
作者：
Ikebe,M;Brozovich,FV
To determine if activation of protein kinase C (PKC) participates in the molecular mechanism for agonist induced force enhancement, force was measured in single β-escin skinned smooth muscle cells stimulated to contract with Ca2+, myosin light chain (MLC) kinase, PKC and microcystin-LR. The constituently active fragment of protein kinase C (PKM) increased both force and MLC phosphorylation in cells previously stimulated to contract at submaximal Ca2+. For cells contracted with saturating Ca2+, PKM stimulation did not increase either force or MLC phosphorylation. For contractions stimulated with both PKM and microcystin-LR, force rose significantly slower than contractions produced by Ca2+or MLC kinase, suggesting that PKM increases force by a decrease in the rate of myosin dephosphorylation. Consistent with this hypothesis is the finding that the rate of force relaxation was slowed by PKM. This is the first direct demonstration that activation of PKC increases force in smooth muscle, and these results suggest that in smooth muscle, agonist induced activation of PKC plays a role in force regulation via an inhibition of myosin light chain phosphatase activity.
