Proteomic Analysis of Saliva Identifies Potential Biomarkers for Orthodontic Tooth Movement

Orthodontic treatment has been shown to induce inflammation, followed by bone remodelling in the periodontium. These processes trigger the secretion of various proteins and enzymes into the saliva. This study aims to identify salivary proteins that change in expression during orthodontic tooth movem...

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Bibliographic Details
Published in:TheScientificWorld 2012-01, Vol.2012 (2012), p.1-6
Main Authors: Ellias, Mohd Faiz, Zainal Ariffin, Shahrul Hisham, Karsani, Saiful Anuar, Abdul Rahman, Mariati, Senafi, Shahidan, Megat Abdul Wahab, Rohaya
Format: Article
Language:English
Subjects:
Adult
Binding sites
Biomarkers
Biomarkers - analysis
Bone remodeling
Bone resorption
Chains
Cytokines
Dehydrogenases
Dentistry
Electrophoresis
Electrophoresis, Polyacrylamide Gel
Female
Gel electrophoresis
Humans
Immunoglobulins
Inflammation
Isoelectric Focusing
Mass spectrometry
Mass spectroscopy
Orthodontics
Peptides
Periodontium
Phosphatase
Proteins
Proteomics
Saliva
Saliva - chemistry
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Tandem Mass Spectrometry
Teeth
Tooth Movement Techniques
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Summary:Orthodontic treatment has been shown to induce inflammation, followed by bone remodelling in the periodontium. These processes trigger the secretion of various proteins and enzymes into the saliva. This study aims to identify salivary proteins that change in expression during orthodontic tooth movement. These differentially expressed proteins can potentially serve as protein biomarkers for the monitoring of orthodontic treatment and tooth movement. Whole saliva from three healthy female subjects were collected before force application using fixed appliance and at 14 days after 0.014′′ Niti wire was applied. Salivary proteins were resolved using two-dimensional gel electrophoresis (2DE) over a pH range of 3–10, and the resulting proteome profiles were compared. Differentially expressed protein spots were then identified by MALDI-TOF/TOF tandem mass spectrometry. Nine proteins were found to be differentially expressed; however, only eight were identified by MALDI-TOF/TOF. Four of these proteins—Protein S100-A9, immunoglobulin J chain, Ig alpha-1 chain C region, and CRISP-3—have known roles in inflammation and bone resorption.
ISSN:2356-6140
1537-744X
1537-744X
DOI:10.1100/2012/647240