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Vol. 14, Issue 8, 3156-3168, August 2003
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* Department of Cell Biology, The Lerner Research Institute, Cleveland Clinic
Foundation, Cleveland, Ohio 44195;
Cole Eye Institute, Cleveland Clinic Foundation, Cleveland, Ohio 44195
Submitted November 22, 2002;
Revised March 27, 2003;
Accepted April 17, 2003
Monitoring Editor: Anthony Bretscher
Endothelial cell (EC) migration is a critical event during multiple physiological and pathological processes. ECs move in the plane of the endothelium to heal superficially injured blood vessels but migrate in three dimensions during angiogenesis. We herein investigate differences in these modes of movement focusing on caveolae and their defining protein caveolin-1. Using a novel approach for morphological analysis of transmigrating cells, we show that ECs exhibit a polarized distribution of caveolin-1 when traversing a filter pore. Strikingly, in these cells caveolin-1 seems to be released from caveolar structures in the cell rear and to relocalize at the cell front in a cytoplasmic form. In contrast, during planar movement caveolin-1 is concentrated at the rear of ECs, colocalizing with caveolae. The phosphorylatable Tyr14 residue of caveolin-1 is required for polarization of the protein during transmigration but does not alter polarization during planar movement. Palmitoylation of caveolin-1 is not essential for redistribution of the protein during either mode of movement. Thus, ECs migrating in three dimensions uniquely exhibit dissociation of caveolin-1 from caveolae and phosphorylation-dependent relocalization to the cell front.
Abbreviations used: BSA, bovine serum albumin; EC, endothelial cell; FGF, fibroblast growth factor; GFP, green fluorescent protein; PBS, phosphate-buffered saline.
Corresponding author. E-mail address:
foxp{at}ccf.org.
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