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Am J Physiol Cell Physiol 273: C1215-C1224, 1997;
0363-6143/97 $5.00
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Vol. 273, Issue 4, C1215-C1224, October 1997

F-actin modulates swelling-activated chloride current in cultured chick cardiac myocytes

Jianping Zhang, Terje H. Larsen, and Melvyn Lieberman

Division of Physiology, Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710

The integrity of F-actin and its association with the activation of a Cl- current (ICl) in cultured chick cardiac myocytes subjected to hyposmotic challenge were monitored by whole cell patch clamp and fluorescence confocal microscopy. Disruption of F-actin by 25 µM cytochalasin B augmented hyposmotic cell swelling by 51% (from a relative volume of 1.54 ± 0.10 in control to 2.33 ± 0.21), whereas stabilization of F-actin by 20 µM phalloidin attenuated swelling by 15% (relative volume of 1.31 ± 0.05). Trace fluorochrome-labeled (fluorescein isothiocyanate or tetramethylrhodamine isothiocyanate) phalloidin revealed an intact F-actin conformation in control cells under hyposmotic conditions despite the considerable changes in cell volume. Sarcoplasmic F-actin was very disorganized and occurred only randomly beneath the sarcolemma in cells treated with cytochalasin B, whereas no changes in F-actin distribution occurred under either isosmotic or hyposmotic conditions in cells treated with phalloidin. Swelling-activated ICl (68.0 ± 6.0 pA/pF at +60 mV) was suppressed by both cytochalasin B (22.7 ± 5.1 pA/pF) and phalloidin (22.5 ± 3.5 pA/pF). On the basis of these results, we suggest that swelling of cardiac myocytes initiates dynamic changes in the cytoarchitecture of F-actin, which may be involved in the volume transduction processes associated with activation of ICl.

cell volume; cytoskeleton; cytochalasin B; phalloidin; whole cell patch clamp; confocal microscopy


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