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Am J Physiol Lung Cell Mol Physiol 284: L39-L49, 2003. First published August 23, 2002; doi:10.1152/ajplung.00164.2002
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Vol. 284, Issue 1, L39-L49, January 2003

Expression of the amino acid transporter ATB0+ in lung: possible role in luminal protein removal

Jennifer L. Sloan, Barbara R. Grubb, and Sela Mager

Department of Cell and Molecular Physiology and the Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina, Chapel Hill, North Carolina 27599

Normal lung function requires transepithelial clearance of luminal proteins; however, little is known about the molecular mechanisms of protein transport. Protein degradation followed by transport of peptides and amino acids may play an important role in this process. We previously cloned and functionally characterized the neutral and cationic amino acid transporter ATB0+ and showed expression in the lung by mRNA analysis. In this study, the tissue distribution, subcellular localization, and function of the transporter in native tissue were investigated. Western blots showed expression of the ATB0+ protein in mouse lung, stomach, colon, testis, blastocysts, and human lung. Immunohistochemistry revealed that ATB0+ is predominantly expressed on the apical membrane of ciliated epithelial cells throughout mouse airways from trachea to bronchioles and in alveolar type I cells. Electrical measurements from mouse trachea preparations showed Na+- and Cl--dependent, amino acid-induced short-circuit current consistent with the properties of ATB0+. We hypothesize that, by removing amino acids from the airway lumen, the transporter contributes to protein clearance and, by maintaining a low nutrient environment, plays a role in lung defense.

mucociliary clearance; airway surface liquid; acute respiratory distress syndrome; pulmonary alveolar phospholipoproteinosis; glucose transport


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