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Mapping of proteins in human saliva using two-dimensional gel electrophoresis and peptide mass fingerprinting
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.
Linköping University, Department of Molecular and Clinical Medicine, Occupational and Environmental Medicine. Linköping University, Faculty of Health Sciences.
2003 (English)In: Proteomics, ISSN 1615-9853, E-ISSN 1615-9861, Vol. 3, no 6, 1003-1015 p.Article in journal (Refereed) Published
Abstract [en]

Human saliva contains a large number of proteins that can be used for diagnosis and are of great potential in clinical and epidemiological research. The aim of this work was to map the proteins in saliva by two-dimensional gel electrophoresis (2-DE), and to identify abundant proteins by peptide mass fingerprinting using trypsin cleavage and matrix-assisted laser desorption/ionization-time of flight-mass spectrometry analysis. One hundred proteins were identified representing 20 different identities according to accession numbers. Abundant proteins expressed in different forms were: α-amylase, immunoglobulin A, prolactin-inducible protein, zinc-α2-glycoprotein and cystatins (S, SA, D and SN). Other proteins found were interleukin-1 receptor antagonist, von Ebner’s gland protein (lipocalin-1) and calgranulin A and B (S100A8 and A9). Furthermore, apolipoprotein A-I, β2-microglobulin, glutathione S-transferase P and fatty acid-binding protein were also identified. Our results show that human saliva contains a large number of proteins that are involved in inflammatory and immune responses. The 2-DE protein map constructed opens the possibility to investigate protein changes associated with disease processes.

Place, publisher, year, edition, pages
2003. Vol. 3, no 6, 1003-1015 p.
National Category
Medical and Health Sciences
Identifiers
URN: urn:nbn:se:liu:diva-26469DOI: 10.1002/pmic.200300426Local ID: 11020OAI: oai:DiVA.org:liu-26469DiVA: diva2:247018
Available from: 2009-10-08 Created: 2009-10-08 Last updated: 2017-12-13Bibliographically 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, BijarTagesson, ChristerLindahl, Mats

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