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

Mol Vis. 2000 Jul 28:6:132-43.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Actins / metabolism*
  • Bridged Bicyclo Compounds, Heterocyclic / pharmacology*
  • Cell Adhesion
  • Cells, Cultured
  • Cytoskeletal Proteins / metabolism
  • Cytoskeleton / drug effects
  • Cytoskeleton / metabolism
  • Cytoskeleton / ultrastructure
  • Humans
  • Macrolides / pharmacology*
  • Microscopy, Fluorescence
  • Microscopy, Video
  • Thiazoles / pharmacology*
  • Thiazolidines
  • Trabecular Meshwork / cytology
  • Trabecular Meshwork / drug effects*
  • Trabecular Meshwork / ultrastructure
  • Trans-Activators*
  • Vinculin / metabolism
  • beta Catenin

Substances

  • Actins
  • Bridged Bicyclo Compounds, Heterocyclic
  • CTNNB1 protein, human
  • Cytoskeletal Proteins
  • Macrolides
  • Thiazoles
  • Thiazolidines
  • Trans-Activators
  • beta Catenin
  • Vinculin
  • latrunculin A