Abstract
The response of human MG-63 osteosarcoma cells to physiological levels of hydrostatic pressure was studied. Cell cultures were subjected to a 20-min, 4-MPa hydrostatic pressure pulse. Adhesion was measured at 20 min and 2 h post-hydrostatic pressure. Morphometric measurements of cell shape and immunofluorescent assays of cytoskeletal and adhesion proteins were done pre- and post-hydrostatic pressure. Pressure-treated cells showed increased adhesion (resistance to deadhesion by trypsinization) with increased recovery time. Indirect immunofluorescence demonstrated increased heterotypic adhesion receptor at cell–cell interfaces and increased α3,β1-integrin at cell–substrate interfaces. Indirect immunofluorescence demonstrated depolymerization of α-tubulin, vimentin, and actin during the pressure pulse. Actin reorganization was slower than that of α-tubulin and vimentin, with stress filaments not well organized even after 1 h postpressure. The depolymerization of α-tubulin, vimentin, and actin observed at relatively low levels of hydrostatic pressure suggests disintegration of the integrin–cytoskeletal attachment complex. The increased resistance of the cells to trypsinization and the increase in both heterotypic adhesion receptor and the α3,β1-integrin at cell interfaces suggest that cells compensate for loss of cytoskeletal integrity by increasing attachment to both adjacent cells and the extracellular matrix.Key words: hydrostatic pressure, integrins, tubulin, vimentin.

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