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Am J Physiol Lung Cell Mol Physiol 281: L1512-L1522, 2001;
1040-0605/01 $5.00
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Vol. 281, Issue 6, L1512-L1522, December 2001

Albumin uptake and transcytosis in endothelial cells in vivo induced by albumin-binding protein

Stephen M. Vogel, Richard D. Minshall, Milena Pilipovic', Chinnaswamy Tiruppathi, and Asrar B. Malik

Department of Pharmacology, College of Medicine, University of Illinois at Chicago, Chicago, Illinois 60612

The 60-kDa endothelial cell surface albumin-binding glycoprotein (gp60) is postulated to be a docking site for albumin that mediates the uptake of albumin and its transport in cultured microvessel endothelial cells. In the present study, we used an isolated Krebs-perfused rat lung preparation to address the in vivo role of gp60 in mediating albumin uptake and transport. Addition of primary anti-gp60 antibody to the perfusate followed by the secondary antibody to cross-link gp60 increased the vessel wall 125I-albumin permeability-surface area (PS) product 2.5-fold without affecting the capillary filtration coefficient (Kf,c; a measure of liquid permeability). In contrast, EDTA (5 mM), which induces interendothelial gap formation, produced parallel increases in both Kf,c and 125I-albumin PS product. Increasing perfusate albumin concentration to >1 g/100 ml (EC50 1.2 g/100 ml) was sufficient to block 125I-albumin PS product, indicating that the perfusate albumin competed with tracer albumin for transendothelial albumin transport. Cross-linking of gp60 in lungs perfused with saturating concentration of albumin resulted in a greater increase in 125I-albumin PS product, indicating that gp60 function was capable of being modulated. These results show that activation of gp60 in pulmonary microvessels induces albumin uptake and its transport through a nonhydraulic pathway that fits with a model of albumin permeability via the transcellular pathway.

rat lung; filipin; gp60; antibody cross-linking


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