[Change in fibroblast polarization during change in contractility of the actin cytoskeleton].
The aim of this work was to study role of the contractility in the process of fibroblast spreading. We investigated the morphology and cytoskeleton of cells seeded in the medium containing 2,3 butanedione monoxime (BDM), an inhibitor of myosin II and myosin-ATPase. Time-lapse video observation and immunofluorescence microscopy were used. BDM caused delay in spreading and blocked cell polarization, that led eventually to the conservation of disk-like cell morphology. The actin-myosin cytoskeleton was also BDM-changed. The number and thickness of stress-fibers decreased. Myosin II orientation was dramatically disturbed to obtain a difuse pattern in the cytoplasm. Paxillin-containing focal adhesions decreased in length and their distribution was changed. The movement of concanavalin A receptors and concanavalin A-coated beads on the lamellar cell surface was also BDM inhibited. It indicates an obvious depression of the lamellar cytoplasm activity and points to the damage of the actin-myosin cytoskeleton. Thus, the change in contractility of the latter alters significantly the morphogenesis of fibroblast spreading.
Domnina
L V
LV
A. N. Belozersky Institute of Physical and Chemical Biology, Moscow State University. Domnina@mbio.genebee.msu.su
Ivanova
O Iu
OIu
Vasil'ev
Iu M
IuM
D000199:Actins / Q000378:metabolism*; D003598:Cytoskeletal Proteins / Q000378:metabolism; D003599:Cytoskeleton / Q000378:metabolism*; D005347:Fibroblasts / Q000166:cytology; D005455:Fluorescent Antibody Technique; D051419:Paxillin; D010750:Phosphoproteins / Q000378:metabolism
D000199:Actins; D003598:Cytoskeletal Proteins; D051419:Paxillin; D010750:Phosphoproteins