Effects of 2,3-butanedione monoxime on activation of contraction and crossbridge kinetics in intact and chemically skinned smooth muscle fibres from guinea pig taenia coli
Effects of 2,3-butanedione monoxime on activation of contraction and crossbridge kinetics in intact and chemically skinned smooth muscle fibres from guinea pig taenia coli
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2,3-丁二酮单肟对豚鼠大肠杆菌带状完整平滑肌纤维和化学剥皮平滑肌纤维收缩激活和横桥动力学的影响
DOI：
10.1007/bf00115453
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发表时间：
1993
影响因子：
2.7
通讯作者：
U. Malmqvist
中科院分区：
文献类型：
--
作者：
Å. Österman;A. Arner;U. Malmqvist
研究了2，3-丁二酮单肟（BDM）对豚鼠结肠带平滑肌纤维的作用。在完整的肌肉中，高K+诱导的收缩过程中的主动力在1 mM BDM中被抑制约10%，在10 mM BDM中被抑制约70%。在收缩过程中，用Fura-2技术测量的细胞内[Ca 2 +]在BDM存在下减少。在1和10 mM BDM存在下，力和[Ca 2 +]的减少可以通过细胞外Ca 2+的减少来再现，这表明BDM影响Ca 2+的进入或释放。在皮肤肌肉制剂中，BDM降低主动力的Ca 2+敏感性。这种变化可以通过肌球蛋白轻链磷酸化水平降低来解释。在纤维最大限度地激活thiophosphorylation，BDM的影响力发生在较高的浓度; 10 mM没有减少的力量和60 mM 15%的减少。最大缩短速度（Vmax）和力不受30 mM BDM在硫代磷酸化的肌肉和减少几乎平行的钙激活收缩。目前的结果表明，BDM抑制肌球蛋白轻链磷酸化，直接降低力的产生在横桥水平和抑制平滑肌中的Ca 2+易位。在比抑制横纹肌中的力所需的浓度更高的BDM浓度下观察到对带皮纤维中的力的影响。在完整的平滑肌中的力的抑制可以解释的影响Ca 2+易位。
SummaryThe effects of 2,3-butanedione monoxime (BDM) were studied in smooth muscle fibres from guinea pig taenia coli. In intact muscle, active force during contractions induced by high-K+ was inhibited by about 10% in 1 mM BDM and by approximately 70% in 10 mM BDM. Intracellular [Ca2+] during contraction, measured with the fura-2 technique, was reduced in the presence of BDM. The reduction in force and [Ca2+] in the presence of 1 and 10 mM BDM could be reproduced by reduction in extracellular Ca2+, suggesting that BDM influences the Ca2+ entry or release. In skinned muscle preparations, BDM decreased the Ca2+ sensitivity of active force. This change could be explained by a decreased level of myosin light chain phosphorylation. In fibres maximally activated by thiophosphorylation, the effect of BDM on force occurred at higher concentrations; 10 mM gave no reduction of force and 60 mM 15% reduction. The maximal shortening velocity (Vmax) and force were unaffected by 30 mM BDM in thiophosphorylated muscle and decreased almost in parallel in Ca2+-activated contractions. The present results suggest that BDM inhibits myosin light chain phosphorylation, directly decreases force generation at the crossbridge level and inhibits the Ca2+ translocation in smooth muscle. The effect on force in skinned fibres is observed at higher BDM concentrations than those reported to be required for inhibition of force in striated muscle. The inhibition of force in intact smooth muscle could be explained by an influence on Ca2+ translocation.
二乙酰单肟对心脏兴奋-收缩耦合的影响。
DOI：
--
发表时间：
1985
期刊：
The Journal of pharmacology and experimental therapeutics
影响因子：
--
作者：
Li,T;Sperelakis,N;Teneick,RE;Solaro,RJ
通讯作者：
Solaro,RJ
影响因子：
--
作者：
DRISKA, SP;AKSOY, MO;MURPHY, RA
通讯作者：
MURPHY, RA