TRANSIENT MYOSIN PHOSPHORYLATION AT CONSTANT CA2+ DURING AGONIST ACTIVATION OF PERMEABILIZED ARTERIES

被引:61
作者
MORELAND, S
NISHIMURA, J
VANBREEMEN, C
AHN, HY
MORELAND, RS
机构
[1] BOCKUS RES INST,GRAD HOSP,PHILADELPHIA,PA 19146
[2] UNIV MIAMI,SCH MED,DEPT MOLEC & CELLULAR PHARMACOL,MIAMI,FL 33152
来源
AMERICAN JOURNAL OF PHYSIOLOGY | 1992年 / 263卷 / 02期
关键词
MYOSIN LIGHT CHAIN PHOSPHORYLATION; MUSCLE MECHANICS; SHORTENING VELOCITY; STIFFNESS; ALPHA-TOXIN; MESENTERIC ARTERY; SENSITIZATION; G-PROTEINS;
D O I
10.1152/ajpcell.1992.263.2.C540
中图分类号
Q4 [生理学];
学科分类号
071003 ;
摘要
Norepinephrine (NE) plus guanosine triphosphate (GTP) increases myofilament Ca2+ sensitivity in alpha-toxin-permeabilized smooth muscle. We used alpha-toxin-permeabilized rabbit mesenteric arteries to determine the temporal relationships among force, myosin light chain (MLC) phosphorylation, stiffness, and shortening velocity during contractions in response to Ca2+ alone and to the same [Ca2+] in the presence of NE plus GTP. The addition of NE plus GTP caused a marked increase in the tonic contraction but only transiently elevated the level of MLC phosphorylation over that observed in the presence of Ca2+ alone. NE plus GTP induced similar increases in force and stiffness, but shortening velocity depended solely on the [Ca2+]. A regulated MLC phosphatase could explain the initial increase in force and MLC phosphorylation, but not the maintenance of enhanced force while MLC phosphorylation levels fell to values similar to those in response to Ca2+ alone. Therefore, additional elements must be involved in the maintenance of the receptor and G protein-dependent increase in myofilament Ca2+ sensitivity.
引用
收藏
页码:C540 / C544
页数:5
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