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Vol. 10, Issue 5, 1537-1551, May 1999
*Division of Infectious Diseases, Department of Medicine,
Department of Veterans Affairs Medical Center, University of Maryland
School of Medicine, Baltimore, Maryland 21201; and
§Department of Pathology, Division of Molecular and
Cellular Pathology, University of Alabama at Birmingham, Birmingham,
Alabama 35294
Thrombospondin-1 (TSP) induces endothelial cell (EC) actin
reorganization and focal adhesion disassembly and influences multiple EC functions. To determine whether TSP might regulate EC-EC
interactions, we studied the effect of exogenous TSP on the movement of
albumin across postconfluent EC monolayers. TSP increased
transendothelial albumin flux in a dose-dependent manner at
concentrations 
1 µg/ml (2.2 nM). Increases in albumin flux were
observed as early as 1 h after exposure to 30 µg/ml (71 nM) TSP.
Inhibition of tyrosine kinases with herbimycin A or genistein protected
against the TSP-induced barrier dysfunction by >80% and >50%,
respectively. TSP-exposed monolayers exhibited actin reorganization and
intercellular gap formation, whereas pretreatment with herbimycin A
protected against this effect. Increased staining of
phosphotyrosine-containing proteins was observed in plaque-like
structures and at the intercellular boundaries of TSP-treated cells. In
the presence of protein tyrosine phosphatase inhibition, TSP induced
dose- and time-dependent increments in levels of
phosphotyrosine-containing proteins; these TSP dose and time
requirements were compatible with those defined for EC barrier
dysfunction. Phosphoproteins that were identified include the adherens
junction proteins focal adhesion kinase, paxillin, 
-catenin, and
p120Cas. These combined data indicate that TSP can modulate
endothelial barrier function, in part, through tyrosine phosphorylation
of EC proteins.
Corresponding author.
These authors contributed equally to this manuscript.
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