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PMID: 8531213 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Thin filament activation by phalloidin in skinned cardiac muscle.

Journal of molecular and cellular cardiology ·Vol. 27 ·No. 6 ·1995-06-00 ·Pages 1311-5

Bukatina AE, Fuchs F, Brandt PW

Abstract

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.

MeSH Terms
Actins/metabolism Animals Binding Sites Calcium/metabolism,pharmacology Cattle Heart/drug effects Heart Ventricles/drug effects In Vitro Techniques Kinetics Myocardial Contraction/drug effects Myocardium/metabolism Phalloidine/toxicity Ventricular Function
Chemicals
Actins Phalloidine Calcium
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Bukatina A E
Department of Cell Biology and Physiology, University of Pittsburgh School of Medicine, PA 15261, USA.
Fuchs F
Brandt P W
Article Info
Journal
Journal of molecular and cellular cardiology
Abbr.
J Mol Cell Cardiol
ISSN
0022-2828
Published
1995-06-00
Pages
1311-5
Language
English
Region
England
NLM ID
0262322
Subset
IM
Grants
NIAMS NIH HHS · AR10551 · United States
NIAMS NIH HHS · AR40300 · United States
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