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1 Renal Unit, Massachusetts General Hospital East, Charlestown 02129; 3 Division of Experimental Medicine, Brigham and Women's Hospital, and 2 Department of Medicine, Harvard Medical School, Boston, Massachusetts 02115
The actin cytoskeleton is an important contributor to the
modulation of the cell function. However, little is known about the
regulatory role of this supermolecular structure in the membrane events
that take place in the heart. In this report, the regulation of cardiac
myocyte function by actin filament organization was investigated in
neonatal mouse cardiac myocytes (NMCM) from both wild-type mice and
mice genetically devoid of the actin filament severing protein gelsolin
(Gsn
/). Cardiac L-type calcium channel currents
(ICa) were
assessed using the whole cell voltage-clamp technique. Addition of the
actin filament stabilizer phalloidin to wild-type NMCM increased
ICa by 227% over
control conditions. The basal
ICa of
Gsn/ NMCM was 300% higher than wild-type controls. This
increase was completely reversed by intracellular perfusion of the
Gsn/ NMCM with exogenous gelsolin. Further, cytoskeletal disruption of either Gsn/ or phalloidin-dialyzed
wild-type NMCM with cytochalasin D (CD) decreased the enhanced
ICa by 84% and 87%, respectively. The data indicate that actin filament stabilization by either a lack of gelsolin or intracellular dialysis with phalloidin increase ICa,
whereas actin filament disruption with CD or dialysis of
Gsn/ NMCM with gelsolin decrease
ICa. We conclude
that cardiac L-type calcium channel regulation is tightly controlled by
actin filament organization. Actin filament rearrangement mediated by gelsolin may contribute to calcium channel inactivation.
neonatal mouse cardiac myocytes; cytochalasin D; inactivation
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