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Departments of 1 Pharmacology and 2 Anesthesiology, College of Medicine, University of Illinois, Chicago, Illinois 60612
We determined the concentration
dependence of albumin binding, uptake, and transport in confluent
monolayers of cultured rat lung microvascular endothelial cells
(RLMVEC). Transport of 125I-albumin in RLMVEC
monolayers occurred at a rate of 7.2 fmol · min
1 · 106
cells1. Albumin transport was inhibited by cell surface
depletion of the 60-kDa albumin-binding glycoprotein gp60 and by
disruption of caveolae using methyl-
-cyclodextrin. By contrast, gp60
activation (by means of gp60 cross-linking using primary and secondary
antibodies) increased 125I-albumin uptake 2.3-fold. At
37°C, 125I-albumin uptake had a half time of 10 min and
was competitively inhibited by unlabeled albumin (IC50 = 1 µM). Using a two-site model, we estimated by Scatchard analysis
the affinity (KD) and maximal capacity
(Bmax) of albumin uptake to be 0.87 µM
(KD1) and 0.47 pmol/106 cells
(Bmax1) and 93.3 µM (KD2) and 20.2 pmol/106 cells (Bmax2). At 4°C, we also
observed two populations of specific binding sites, with high
(KD1 = 13.5 nM, 1% of the total) and low
(KD2 = 1.6 µM) affinity. On the basis of
these data, we propose a model in which the two binding affinities
represent the clustered and unclustered gp60 forms. The model predicts
that fluid phase albumin in caveolae accounts for the bulk of albumin
internalized and transported in the endothelial monolayer.
capillary permeability; vesicular transport; caveolae; albumin-binding glycoprotein gp60
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