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Abstract #6212 Published in IGR 2-2

Effect of latrunculin-A on morphology and actin-associated adhesions of cultured human trabecular meshwork cells

Cai S; Liu X; Glasser A; Volberg T; Filla M; Geiger B; Polansky JR; Kaufman PL
Molecular Vision 2000; 6: 132-143


PURPOSE: Determine the effects of the actin cytoskeleton disrupting compound latrunculin-A (LAT-A) on morphology, cytoskeleton, and cellular adhesions of cultured human trabecular meshwork (HTM) cells. METHODS: HTM cells were cultured to high confluence with endothelial-like morphology and treated with LAT-A at different doses and duration. Topography of living cells was evaluated by videomicroscopy. Distribution and organization of the actin-based cytoskeleton, vinculin- and paxillin-containing focal contacts, and beta-catenin-rich intercellular adhesions were determined by immunofluorescence and digital microscopy. RESULTS: LAT-A induced pronounced but highly reversible rounding of HTM cells, intercellular separation, and disruption of actin filaments. beta-catenin-rich intercellular adherens junctions were particularly sensitive to LAT-A. Vinculin- and paxillin-containing focal contacts were only partially affected and appeared to be more resistant to the drug than the intercellular interactions. CONCLUSIONS: The increase in outflow facility in the living primate eye induced by LAT-A may be due to the disorganization and disruption of the actin cytoskeleton and its associated cellular adhesions in the trabecular meshwork.

Dr. S. Cai, Department of Ophthalmology & Visual Sciences, University of Wisconsin, Madison, WI 53792-3220, USA


Classification:

11.14 Investigational drugs; pharmacological experiments (Part of: 11 Medical treatment)



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