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HIGHLIGHTED TOPICS
Lung Growth and Repair

Endothelial cells as early sensors of pulmonary interstitial edema

¹Department of Experimental, Environmental Medicine and Biotechnology, and ²Department of Neuroscience and Biomedical Technologies, University of Milano-Bicocca, Monza 20052, Italy

Submitted 3 March 2004 ; accepted in final form 31 May 2004

We studied responses of endothelial and epithelial cells in the thin portion of the air-blood barrier to a rise in interstitial pressure caused by an increase in extravascular water (interstitial edema) obtained in anesthetized rabbits receiving saline infusion (0.5 ml·kg^–1·min^–1 for 3 h). We obtained morphometric analyses of the cells and of their microenvironment (electron microscopy); furthermore, we also studied in lung tissue extracts the biochemical alterations of proteins responsible for signal transduction (PKC, caveolin-1) and cell-cell adhesion (CD31) and of proteins involved in membrane-to-cytoskeleton linkage (-tubulin and -tubulin). In endothelial cells, we observed a folding of the plasma membrane with an increase in cell surface area, a doubling of plasmalemma vesicular density, and an increase in cell volume. Minor morphological changes were observed in epithelial cells. Edema did not affect the total plasmalemma amount of PKC, -tubulin, and caveolin-1, but -tubulin and CD-31 increased. In edema, the distribution of these proteins changed between the detergent-resistant fraction of the plasma membrane (DRF, lipid microdomains) and the rest of the plasma membrane [high-density fractions (HDFs)]. PKC and tubulin isoforms shifted from the DRF to HDFs in edema, whereas caveolin-1 increased in DRF at the expense of a decrease in phosphorylated caveolin-1. The changes in cellular morphology and in plasma membrane composition suggest an early endothelial response to mechanical stimuli arising at the interstitial level subsequently to a modest (5%) increase in extravascular water.

pulmonary interstitial pressure; morphometry; air-blood barrier; mechanotransduction; plasma membrane proteins

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