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Articles in PresS, published online ahead of print August 23, 2002
Am J Physiol Lung Cell Mol Physiol, 10.1152/ajplung.00164.2002
Submitted on May 24, 2002
Accepted on August 20, 2002
1 Department of Cell and Molecular Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
2 Cystic Fibrosis/Pulmonary Research and Treatment Center, University of North Carolina at Chapel Hill, Chapel Hill, NC, USA
* To whom correspondence should be addressed. E-mail: sela_mager{at}med.unc.edu.
Normal lung function requires transepithelial clearance of lumenal 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.
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