Abstract
The endometrial epithelial cell membrane is a key interface in female reproductive biology. Steroid hormones play a predominant role in cyclic changes which occur at this interface during the female menstrual cycle. Specific changes in the morphology of the endometrial epithelial cell surface become apparent with the epithelial transition that drives the switch from a non-receptive to receptive surface due to the action of progesterone on an oestrogen primed tissue. AFM (atomic force microscopy) allows the high-resolution characterization of the endometrial epithelial cell surface. Its contact probe mechanism enables a unique imaging method that requires little sample preparation, yielding topographical and morphological characterization. By stiffening the cell membrane, low concentrations of fixatives allow the surface detail of the cell to be resolved while preserving fine ultra-structural details for analysis. In the present study we use high resolution AFM analysis of endometrial epithelial cells to monitor the effect of progesterone on the nanoscale structure of the endometrial cell surface. High-resolution imaging reveals similar topographical nanoscale changes in both the Hec-1-A and Ishikawa model cell lines. Hec-1-B cells, used in the present study as a progesterone receptor negative control, however, exhibit a flattened cell surface morphology following progesterone treatment. Changes in average cell height and surface convolution correlate with increased surface roughness measurements, demonstrating alterations in molecular structure on the cell surface due to hormonal stimulation. Progesterone treatment induces changes to the cell surface as a result of nanoscale molecular modifications in response to external hormonal treatments. AFM provides the basis for the identification, visualization and quantification of these cell surface nanoscale changes. Together these findings demonstrate the utility of AFM for use in reproductive science and cancer biology where it could be applied in both in vitro analysis of protein structure-function relationships and clinical diagnosis.
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