Ca2+, cAMP, and changes in myosin phosphorylation during contraction of smooth muscle.
Ca2+, cAMP, and changes in myosin phosphorylation during contraction of smooth muscle.
复制标题
平滑肌收缩过程中 Ca2、cAMP 和肌球蛋白磷酸化的变化。
DOI:
10.1152/ajpcell.1983.245.3.c255
复制
发表时间:
1983
期刊:
影响因子:
--
通讯作者:
Murphy,RA
中科院分区:
文献类型:
--
作者:
Aksoy,MO;Mras,S;Kamm,KE;Murphy,RA
Phosphorylation of myosin increases rapidly upon stimulation of an arterial smooth muscle. However, peak values are not maintained and phosphorylation declines, while active stress increases monotonically to a sustained steady state. The aim of this study was to determine the reason(s) for the transient change in myosin phosphorylation. Four hypotheses were considered: 1) reduced substrate, i.e., ATP depletion, 2) altered access of either the myosin kinase or phosphatase to the cross bridge, 3) reduced myosin kinase activity secondary to its phosphorylation by adenosine 3',5'-cyclic monophosphate-dependent protein kinase, and 4) reduced myoplasmic [Ca2+] during the contraction. Our results suggest that the most likely explanation is that there are two Ca2+-dependent regulatory processes: 1) myosin phosphorylation and 2) a second, unidentified site allowing stress maintenance with reduced cross-bridge cycling rates. A higher cell Ca2+ concentration appears to be necessary to activate myosin kinase and produce myosin phosphorylation than is needed for force maintenance. We suggest that agonist-induced Ca2+ transients, coupled with the differential Ca2+ sensitivity of the two regulatory systems, may explain the observed transient in myosin phosphorylation during a maintained contraction in smooth muscle.
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DOI:
10.1016/0006-291x(80)91209-7
发表时间:
1980
影响因子:
3.1
作者:
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通讯作者:
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影响因子:
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作者:
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DOI:
10.1016/0006-291x(82)91160-3
发表时间:
1982
影响因子:
3.1
作者:
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通讯作者:
G. D. Ford
影响因子:
20.1
作者:
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通讯作者:
MURPHY, RA