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Am J Physiol Lung Cell Mol Physiol (July 8, 2005). doi:10.1152/ajplung.00250.2005
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Submitted on June 9, 2005
Accepted on July 4, 2005

Pathways for clearance of Surfactant Protein-A (SP-A) from the lung

Deepika Jain, Chandra Dodia, Aron B Fisher, and Sandra R Bates*

* To whom correspondence should be addressed. E-mail: batekenn{at}mail.med.upenn.edu.

Uptake and degradation of 125I-surfactant protein-A (SP-A) over a 1 hr period was studied in alveolar cells in culture and in isolated perfused (IP) lungs to elucidate the mechanism for the clearance of the protein from the alveolar space. Specific inhibitors of clathrin- and actin-dependent endocytosis were utilized. In type II cells, the uptake of SP-A, as compared to controls, was decreased by 60 % upon incubation with clathrin inhibitors (amantadine and PAO) or with the actin inhibitor, cytochalasin D. All agents reduced SP-A metabolism by alveolar macrophages. Untreated rat IP lungs internalized 36% of instilled SP-A, and 56 % of the incorporated SP-A was degraded. Inhibitors of clathrin and actin significantly reduced the uptake of SP-A by approximately 54 % while cytochalasin D inhibited SP-A degradation. Co-incubation of agents did not produce an additive effect on uptake of SP-A by cultured pneumocytes or IP lungs, indicating that all affected the same pathway. Thus, the clearance of SP-A from the lung occurs via a clathrin-mediated pathway that requires the polymerization of actin.




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