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Published ahead of print on August 14, 2003, doi:10.1165/rcmb.2003-0142OC

Am. J. Respir. Cell Mol. Biol., Volume 30, Number 2, February 2004, 184-192

A more recent version of this article appeared on February 1, 2004
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Submitted on April 24, 2003
Revised on August 12, 2003

PURIFICATION AND CHARACTERIZATION OF PLUNC FROM HUMAN TRACHEOBRONCHIAL SECRETIONS

Michael A Campos1, Alexandre R Abreu1, Marie C Nlend1, Miguel A Cobas2, Gregory E Conner3, and Philip L Whitney1*

1 Pulmonary and Critical Care Medicine, University of Miami School of Medicine, Miami, Fl, USA, 2 Department of Anesthesiology, University of Miami School of Medicine, Miami, Fl, USA, 3 Pulmonary and Critical Care Medicine, University of Miami School of Medicine, Miami, Fl, USA; Department of Cell Biology and Anatomy, University of Miami School of Medicine, Miami, Fl, USA

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

To study proteins secreted into the airway, we used secretions from primary human airway epithelial cells, re-differentiated at the air-liquid interface (ALI), and from patients intubated during surgery. A major protein of the cultured cell secretions was ethanol soluble. This protein was purified, analyzed by Edman degradation, MALDI-TOF MS of tryptic digests, and Western blots of 2-dimensional electrophoresis gels using antisera against the purified preparation. The protein was identified as palate lung nasal epithelial clone (PLUNC). The protein had multiple truncated molecules, a pattern also seen in tracheal aspirates. PLUNC was poorly soluble in water (50µmg/ml) or in 50 mM NaCl but was more soluble in 75% ethanol (>380µg/ml). PLUNC secretion dramatically increased during the second week in ALI culture and continued to increase over time. Immunohistochemistry showed that PLUNC was expressed in human airway epithelium and submucosal glands. Although PLUNC is in the LPS-binding protein (LBP) and BPI bactericidal/permeability-increasing protein (BPI) family of antibacterial host defense proteins, purified PLUNC failed to compete with LBP for the binding of LPS, while polymyxin B, a known inhibitor of LPS-LBP binding, did interfere with binding. This study showed that plunc gene product is expressed both in vivo and in vitro, detailed a method for its purification and provided basic information on its biochemical properties in secretions.




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