Thin filament activation by phalloidin in skinned cardiac muscle
Anna E. Bukatina, Franklin Fuchs, Philip W. Brandt
Abstract
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Anna E. Bukatina, Franklin Fuchs, Philip W. Brandt
Abstract
Open-access reader
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.
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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.
Key concepts: Phalloidin, Actin, Cooperativity, Protein filament, Biophysics, Chemistry, Biochemistry, Cytoskeleton