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Am J Physiol Lung Cell Mol Physiol (July 25, 2003). doi:10.1152/ajplung.00271.2002
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Submitted on August 12, 2002
Accepted on July 13, 2003

Effect of Surfactant Protein-A on Granular Pneumocyte Surfactant Secretion in Vitro

Sandra R. Bates1*, Jian-Qin Tao1, Kathleen Notarfrancesco1, Kristine DeBolt1, Henry Shuman1, and Aron B. Fisher1

1 The Institute for Environmental Medicine, University of Pennsylvania School of Medicine, Philadelphia, PA, USA

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

Surfactant secretion by lung type II cells occurs when lamellar bodies (LBs) fuse with the plasma membrane and surfactant is released into the alveolar lumen. Surfactant protein A (SP-A) blocks secretagogue-stimulated phospholipid (PL) release, even in the presence of surfactant-like lipid. The mechanism of action is not clear. We have shown previously that an antibody to LB membranes (mAb 3C9) can be used to measure LB membrane trafficking. Although the ATP-stimulated secretion of PL was blocked by SP-A, the cell-association of iodinated mAb 3C9 was not altered, indicating no effect on LB movement. FM 1-45 is a hydrophobic dye used to monitor the formation of fusion pores. After secretagogue exposure, the 3-fold enhancement of the number of FM 1-43 fluorescent LBs (per 100 cells) was not altered by the presence of SP-A. Finally, there was no evidence of a large phospholipid pool retained on the cell surface through interaction with SP-A. Thus, SP-A exposure does not affect these stages in the surfactant secretory pathway of type II cells.




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