Bukatina A E, Fuchs F, Brandt P W
Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, PA 15261, USA.
J Mol Cell Cardiol. 1995 Jun;27(6):1311-5. doi: 10.1016/s0022-2828(05)82393-4.
Phalloidin binds very tightly and specifically to actin and brings about a marked stabilization of the F-actin filament. In this study the effects of phalloidin on force generation and Ca2+ sensitivity of skinned bovine ventricular muscle were investigated. At all free Ca2+ concentrations addition of phalloidin to activated fibers caused an enhancement of active force. At full Ca2+ activation the force increase was about 6% and the relative force enhancement became greater as the Ca2+ concentration was decreased. Force-pCa plots obtained with fibers pre-treated with phalloidin showed that phalloidin produced an approximately 0.2 pCa unit increase in Ca2+ sensitivity without significant changes in cooperativity of activation. These results suggest that interactions between G-actin subunits may play an important role in cardiac force development.
鬼笔环肽能非常紧密且特异性地结合肌动蛋白,并使F-肌动蛋白丝显著稳定。在本研究中,研究了鬼笔环肽对去表皮牛心室肌的力产生和Ca2+敏感性的影响。在所有游离Ca2+浓度下,向激活的纤维中添加鬼笔环肽都会导致主动力增强。在完全Ca2+激活时,力增加约6%,并且随着Ca2+浓度降低,相对力增强变得更大。用鬼笔环肽预处理的纤维得到的力-pCa图表明,鬼笔环肽使Ca2+敏感性增加约0.2个pCa单位,而激活的协同性没有显著变化。这些结果表明,G-肌动蛋白亚基之间的相互作用可能在心脏力的产生中起重要作用。