Abstract
Eukaryotic cells have an internal cytoskeletal scaffolding, giving them their distinctive shapes. The cytoskeleton enables cells to transport vesicles, undergo changes in shape, migrate and contract. This dynamic structure is formed by three classes of filamentous assembly: actin microfilaments, intermediate filaments and microtubules. In this investigation the cytoskeleton of cultured human myometrial cells was studied by immunohistochemistry using specific antibodies against vinculin, cytokeratin, vimentin, tubulin and RhoA, covalently labelled with a fluorescent tag. Polymerized actin was visualized with fluorescein-conjugated phalloidin. Myometrial cells were very rich in actin fibres, which generally appeared as parallel bundles along the longest axis of the cells. There was a strong expression of vinculin which concentrated at actin--vinculin focal adhesion sites. By contrast, intermediate filaments (vimentin and cytokeratin) were organized in a dense cytoplasmic meshwork which excluded the nuclear space. A similar pattern was observed for tubulin. RhoA had a diffuse distribution and was associated with actin fibres. Exposure of the cells to oxytocin provoked a 10% shortening of actin stress fibres. These results demonstrate that myometrial smooth muscle cells have a rich cytoskeletal structure and that agonists that stimulate myometrial activation provoke measurable changes in actin fibres which may be important for efficient contractility.
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