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

التفاصيل البيبلوغرافية
العنوان: Effect of latrunculin-A on morphology and actin-associated adhesions of cultured human trabecular meshwork cells
المؤلفون: S, Cai, X, Liu, A, Glasser, T, Volberg, M, Filla, B, Geiger, J R, Polansky, P L, Kaufman
المصدر: Molecular vision. 6
سنة النشر: 2000
مصطلحات موضوعية: Microscopy, Video, Bridged Bicyclo Compounds, Heterocyclic, Actins, Vinculin, Cytoskeletal Proteins, Thiazoles, Microscopy, Fluorescence, Trabecular Meshwork, Cell Adhesion, Trans-Activators, Humans, Thiazolidines, Macrolides, Cells, Cultured, Cytoskeleton, beta Catenin
الوصف: 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.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.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.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.
تدمد: 1090-0535
الوصول الحر: https://explore.openaire.eu/search/publication?articleId=pmid________::a5fee6589d5be640b1bcaddab4a2c7ccTest
https://pubmed.ncbi.nlm.nih.gov/10930474Test
حقوق: OPEN
رقم الانضمام: edsair.pmid..........a5fee6589d5be640b1bcaddab4a2c7cc
قاعدة البيانات: OpenAIRE