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Published ahead of print on March 27, 2003, doi:10.1165/rcmb.2002-0189OC

Am. J. Respir. Cell Mol. Biol., Volume 29, Number 3, September 2003, 273-282

A more recent version of this article appeared on September 1, 2003
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Submitted on September 27, 2002
Revised on March 20, 2003

CHARACTERIZATION OF ALPHA-SNAP IN ALVEOLAR TYPE II CELLS: IMPLICATIONS IN LUNG SURFACTANT SECRETION

Barack O Abonyo1, Pengcheng Wang2, Telugu A Narasaraju2, William H Rowan III3, David H McMillan3, Un-Jin Zimmerman4, and Lin Liu2*

1 Department of Physiological Sciences, Oklahoma State University, Stillwater, OK, USA; Department of Physiology, East Carolina University, Greenville, NC, USA, 2 Department of Physiological Sciences, Oklahoma State University, Stillwater, OK, USA, 3 Department of Physiology, East Carolina University, Greenville, NC, USA, 4 Institute for Environmental Medicine, University of Pennsylvania, Philadelphia, PA, USA

* To whom correspondence should be addressed. E-mail: liulin{at}okstate.edu.

NSF (N-ethylmaleimide sensitive fusion protein) and {alpha}-SNAP (soluble NSF attachment protein) are thought to be soluble factors that transiently bind and disassemble SNARE (SNAP receptor) complex during exocytosis in neuronal and endocrine cells. Lung surfactant is secreted via exocytosis of lamellar bodies from alveolar epithelial type II cells. However, the secretion of lung surfactant is a relatively slow process and involvement of SNAREs and its cofactors (NSF and {alpha}-SNAP) in this process has not been demonstrated. In this study, we investigated a possible role of {alpha}-SNAP in surfactant secretion. {alpha}-SNAP was predominantly associated with the membranes in alveolar type II cells as determined by Western blot and immunocytochemical analysis using confocal microscope. Membrane-associated {alpha}-SNAP was not released from the membrane fraction when the cells were lyzed in the presence of Ca2+ or Mg2+ATP. The alkaline condition (0.1 M Na2CO3, pH 12), known to extract peripheral membrane proteins also failed to release it from the membrane. Phase separation using Triton X-114 showed that {alpha}-SNAP partitioned into both aqueous and detergent phases. NSF had membrane-bound characteristics similar to {alpha}-SNAP in type II cells. Permeabilization of type II cells with {beta}-escin resulted in a partial loss of {alpha}-SNAP from the cells, but cellular NSF was relatively unchanged. Addition of exogenous {alpha}-SNAP to the permeabilized cells increased surfactant secretion in a dose dependent manner, whereas exogenous NSF has much less effects. An {alpha}-SNAP anti-sense oligonucleotide decreased its protein level and inhibited surfactant secretion. Our results suggest a role of {alpha}-SNAP in lung surfactant secretion.




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