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Am J Physiol Lung Cell Mol Physiol 284: L458-L465, 2003. First published November 15, 2002; doi:10.1152/ajplung.00237.2002
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Vol. 284, Issue 3, L458-L465, March 2003

Absorption of intact albumin across rat alveolar epithelial cell monolayers

Kwang-Jin Kim1,2,3,4,9,*, Yasuhisa Matsukawa5,*, Hiroshi Yamahara5, Vijay K. Kalra6, Vincent H. L. Lee5,7, and Edward D. Crandall1,8,9

Departments of 1 Medicine, 2 Physiology and Biophysics, 3 Molecular Pharmacology and Toxicology, 4 Biomedical Engineering, 5 Pharmaceutical Sciences, 6 Biochemistry, 7 Ophthalmology, 8 Pathology, and 9 Will Rogers Institute Pulmonary Research Center, Schools of Pharmacy, Medicine, and Engineering, University of Southern California, Los Angeles, California 90033

Transport characteristics of intact albumin were investigated using primary cultured rat alveolar epithelial cell monolayers. The apical-to-basolateral (ab) flux of intact fluorescein isothiocyanate (FITC)-labeled albumin (F-Alb) is greater than basolateral-to-apical (ba) flux at the same upstream [F-Alb]. Net absorption of intact F-Alb occurs with half-maximal concentration of ~1.6 µM and maximal transport rate of ~0.15 fmol · cm-2 · s-1. At 15 and 4°C, both ab and ba F-Alb fluxes are not different from zero, collapsing net absorption. The presence of excess unlabeled albumin (but not other macromolecule species) in either the apical or basolateral fluid significantly reduces both ab and ba unidirectional F-Alb fluxes. Photoaffinity labeling of apical cell membranes revealed an ~60-kDa protein that exhibits specificity for albumin. These data indicate that net absorption of intact albumin takes place via saturable receptor-mediated transcellular endocytotic processes recognizing albumin, but not other macromolecules, that may play an important role in alveolar homeostasis in the mammalian lung.

protein transport; air-blood barrier; saturable transcytosis; albumin-binding sites; alveolar fluid balance

* K.-J. Kim and Y. Matsukawa contributed equally to this work.




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