モルモット結腸紐平滑筋の種々筋長における張力発生と2万ダルトンのミオシン軽鎖のリソ酸化について
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Tension development and phosphorylation of 20,000 dalton myosin light chain (LC20) induced by 100mM K+ at various lengths of guinea pig taenia coli were examined. The results obtained were as follows: 1) At the in situ length (Lb), isometric tension reached its peak after 20 sec of stimulation by 100mM K+. After the peaking, isometric tension spontaneously declined to a plateau (about 75% of maximum isometric tension) and this tension was maintained during the remainder of the period of observation (10 min). 2) At Lb, the maximum phosphorylation of LC20 (about 40%) was attained after 10 sec of stimulation by 100mM K+, and this value was maintained during the remainder of the period of observation (10 min). 3) No appreciable resting tension was observed below 0.5 Lb. The resting tension slightly increased in the range from 0.5 Lb to Lb and markedly increased in the range from Lb to 1.5 Lb. 4) Active tension in 100mM K+-depolarized muscle reached its maximum at Lb. The active tension at 0.5Lb and 1.5Lb were about 40% and 30%, respectively. 5) The amounts of the phosphorylated LC20 in 100mM K+-depolarized muscle at 0.5Lb and 1.5Lb were almost equal to that at Lb (about 40%). 6) The amounts of the phosphorylated LC20 at 30 sec after application of norepinephrine remained at the same level (about 20%) regardless of muscle length. From the above results, the sliding filament mechanism in smooth muscle contraction was examined for its validity on the basis of the relationship between length-tension and phosphorylation of LC20.
- 札幌医科大学の論文
- 1986-04-01
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