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PLUNC (palate, lung and nasal epithelial clone) proteins in human nasal lavage fluid
Linköping University, Department of Molecular and Clinical Medicine, Occupational and Environmental Medicine. Linköping University, Faculty of Health Sciences.
Östergötlands Läns Landsting, Centre for Laboratory Medicine, Department of Clinical Microbiology. Linköping University, Faculty of Health Sciences.
Linköping University, Department of Molecular and Clinical Medicine, Occupational and Environmental Medicine. Linköping University, Faculty of Health Sciences.
Linköping University, Department of Molecular and Clinical Medicine, Occupational and Environmental Medicine. Linköping University, Faculty of Health Sciences.
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2003 (English)In: Biochemical Society Transactions, ISSN 0300-5127, E-ISSN 1470-8752, Vol. 31, no 4, 810-814 p.Article in journal (Refereed) Published
Abstract [en]

PLUNC (palate, lung and nasal epithelial clone) is a newly discovered gene that is expressed in the upper respiratory tract and is suggested to be of importance in host defence against bacteria. We have identified two forms of the PLUNC protein in human nasal lavage fluid (NLF) using two-dimensional gel electrophoresis (2-DE) and MS. The apparent molecular masses and isoelectric points of these forms are 24.8 kDa/pI 5.4 and 25.1 kDa/pI 5.5. Notably, the 24.8 kDa/pI 5.4 form of PLUNC is an abundant protein in the 2-DE protein patterns of NLF from healthy subjects. Decreased levels of PLUNC were found in NLF from smokers and workers exposed to reactive epoxy chemicals, indicating that long-term exposure to airway irritants impairs the production of PLUNC in the upper respiratory tract. We have also investigated the presence of lipopolysaccharide (LPS)-binding proteins in NLF. Five proteins were found to adsorb to a LPS-coated surface; two of these proteins correspond to the two PLUNC forms, as judged by 2-DE pattern matching. For comparison, human saliva was found to contain a set of LPS-binding proteins with similar 2-DE spot positions (the same pIs but somewhat lower apparent molecular masses of 20 kDa). These results indicate that PLUNC may be a new marker of airway inflammation and may play a part in the innate immune response, and that human saliva contains yet other members of the family of LPS-binding proteins.

Place, publisher, year, edition, pages
2003. Vol. 31, no 4, 810-814 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-26470DOI: 10.1042/BST0310810Local ID: 11021OAI: oai:DiVA.org:liu-26470DiVA: diva2:247019
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2012-10-02Bibliographically approved
In thesis
1. Proteomics of the upper airways: studies on a new lipopolysaccharide-binding protein, PLUNC
Open this publication in new window or tab >>Proteomics of the upper airways: studies on a new lipopolysaccharide-binding protein, PLUNC
2005 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

There is now significant interest in identifying, quantifying and characterizing the human proteome, and new powerful techniques (proteomics) have evolved to deal with this giant task. In the present study, proteomics have been applied for the first time to map the proteins of the upper airways. The protein contents of human nasal fluid (NLF) and saliva were analysed using two-dimensional polyacrylamide gel electrophoresis (2-D PAGE) and the proteins were identified by peptide mass fingerprinting using matrix assisted laser desorptioniionization time of night mass spectrometry (MALDI-TOF MS) or by amino acid sequencing using electrospray ionization tandem mass spectrometry (ESI- MS/MS). More than 100 proteins were identified and protein maps of nasal fluid and saliva were thus established. Of particular interest was the identification of a new lipopolysaccharide (LPS)-binding protein, PLUNC (palate lung and nasal epithelial clone), which was shown to be the only protein in NLF that binds to LPS. PLUNC was characterized as multiple isoforms (Mr/p1: 27/5.1, 26/5.2, 25/5.3, 27.5/5.1, 27/5.2, 26/5.3, 25.1/5.5 and 24.8/5.4), and several of these isoforms were demonstrated to be sialylated. Notably, decreased levels of PLUNC were found in NLF of (i) smokers, (ii) epoxy workers with airway irritation, and (iii) patients with seasonal allergic rhinitis (SAR) during allergy season. In addition, the levels of von Ebner's gland protein, α1-antitrypsin, cystatin S, Clara cell protein 16 and lipocortin-1 were altered, either in smokers or SAR patients or both. One previously unidentified NLF protein was found in SAR patients during allergy season but not before season: this protein was identified as eosinophil lysophospholipase. Many of these proteins were post-translationally modified by glycosylation (PLUNC, α1-antitrypsin, von Ebner's gland protein), phosphorylation (cystatin S), acetylation (eosinophil lysophospholipase), or truncation (lipocortin-1). Altogether, these findings illustrate the potential use of proteomics for identifying new markers of upper airway inflammation and for revealing structural details of such markers. The findings also indicate that allergic inflammation in the nasal mucosa is associated with decreased nasal fluid levels of the endogenous proteinase inhibitors, cystatin S and von Ebner's gland protein, and of the new irritation marker, PLUNC. Further studies are required to explore the possibility that PLUNC plays an important part in microbial  recognition and that this function is impaired after exposure to airway irritants and during upper airway inflammation.

Place, publisher, year, edition, pages
Linköping: Linköping University Electronic Press, 2005. 63 p.
Series
Linköping University Medical Dissertations, ISSN 0345-0082 ; 927
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-31423 (URN)17204 (Local ID)91-85497-64-9 (ISBN)17204 (Archive number)17204 (OAI)
Public defence
2005-12-16, Berzeliussalen, Hälsouniversitetet, Campus US, Linköpings universitet, Linköping, 09:00 (Swedish)
Opponent
Available from: 2009-10-09 Created: 2009-10-09 Last updated: 2012-10-02Bibliographically approved

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Ghafouri, BijarKihlström, ErikStåhlbom, BengtTagesson, ChristerLindahl, Mats

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