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PLUNC in human nasal lavage fluid: multiple isoforms that bind to lipopolysaccharide

Bijar Ghafouri1, Erik Kihlström, Christer Tagesson

  • 1Division of Occupational and Environmental Medicine, Department of Molecular and Clinical Medicine, Faculty of Health Sciences, Linköping University, S-581 85 Linköping, Sweden.

Biochimica Et Biophysica Acta
|May 26, 2004
PubMed

Insights

Multiple palate lung nasal epithelial clone (PLUNC) isoforms were found in human nasal lavage fluid. These PLUNC isoforms bind to lipopolysaccharide (LPS), suggesting a role in upper airway innate immunity.

Area of Science:

  • Biochemistry
  • Immunology
  • Proteomics

Background:

  • Palate lung nasal epithelial clone (PLUNC) is a protein found in the airways.
  • Its specific functions and forms in human nasal lavage fluid (NLF) are not fully understood.

Purpose of the Study:

  • To identify and characterize different isoforms of PLUNC in human NLF.
  • To investigate the binding properties of PLUNC isoforms, particularly their interaction with lipopolysaccharide (LPS).

Main Methods:

  • Two-dimensional gel electrophoresis (2-DE) to separate PLUNC isoforms.
  • Matrix assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF MS) and nanoelectrospray MS/MS for peptide mapping and amino acid sequencing.
  • In vitro binding assays using LPS-coated surfaces.

Main Results:

  • Eight distinct PLUNC isoforms were identified in human NLF.
  • At least one PLUNC isoform was found to be glycosylated.
  • PLUNC isoforms demonstrated specific binding to LPS in vitro, with other NLF proteins showing no such adsorption.

Conclusions:

  • PLUNC is expressed as multiple, distinct isoforms in human NLF.
  • These PLUNC isoforms exhibit lipopolysaccharide-binding activity.
  • PLUNC may function as a component of the innate immune response in the upper airways.

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