Phosphorylation-dephosphorylation of the 18,000-dalton light chain of myosin during the contraction-relaxation cycle of frog muscle.
Phosphorylation-dephosphorylation of the 18,000-dalton light chain of myosin during the contraction-relaxation cycle of frog muscle.
复制标题
青蛙肌肉收缩-舒张周期期间肌球蛋白 18,000 道尔顿轻链的磷酸化-去磷酸化。
DOI:
10.1016/s0021-9258(18)50806-1
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发表时间:
1979
期刊:
影响因子:
--
通讯作者:
M. Kushmerick
中科院分区:
文献类型:
--
作者:
K. Bárány;M. Bárány;J. Gillis;M. Kushmerick
The l&000-dalton light chain of myosin was phosphorylated and dephosphorylated during the contraction and relaxation cycle of frog muscle. The extent of light chain phosphorylation was a function of stimulus duration in the early phase of contraction. At O” C, 0.14 and 0.22 mol of [S2P] phosphate was transferred/m01 of light chain in muscles which were stimulated for 200 and 500 ms, respectively, and produced 40 and 80% of the maximal tetanic tension, respectively. During a few seconds of tetanization at various temperatures, 0.2 to 0.3 mol of [3eP] phosphate was transferred, whereas electrical stimulation for 20 to 30 s or caffeine treatment for 20 min resulted in esterification of 0.35 to 0.4 mol of [3” P] phosphate. This increase of phosphorylation seems to be related to the continued presence of sarcoplasmic Ca2+ at activating levels, that is,> lO-8 M.Light chain phosphorylation in stimulated semitendinosus muscles stretched beyond the point of overlap of the thick and thin filaments was identical to that in muscles stimulated at standard rest length when the time of stimulation was at least 3 s. The data indicate that the stimulation of the muscle per se and not the mechanical event initiates the phosphorylation. Light chain dephosphorylation took place in the relaxing phase of muscle activity. After short tetani, dephosphorylation approximately followed relaxation. After longer tetani, relaxation occurred before dephosphorylation. In vitro experiments demonstrated that the absence of CaZ+ was required for light chain dephosphorylation and that phosphoryl groups did not turn over during active myofibrillar ATPase. Light chain phosphorylation may be involved in activation of muscle contraction by providing a driving force to place the cross-bridges in the vicinity of actin filaments.