Proteomic analysis of saliva identifies potential biomarkers for orthodontic tooth movement

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21 Citations (Scopus)

Abstract

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 310, 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 proteinsProtein S100-A9, immunoglobulin J chain, Ig alpha-1 chain C region, and CRISP-3have known roles in inflammation and bone resorption.

Original languageEnglish
Article number647240
JournalThe Scientific World Journal
Volume2012
DOIs
Publication statusPublished - 2012

Fingerprint

Tooth Movement Techniques
saliva
proteomics
Biomarkers
Saliva
Proteomics
tooth
biomarker
protein
Salivary Proteins and Peptides
Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry
Proteins
Immunoglobulin J-Chains
Bone
Inflammation
Periodontium
bone
Bone Remodeling
Secretory Pathway
Electrophoresis, Gel, Two-Dimensional

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Environmental Science(all)
  • Medicine(all)

Cite this

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abstract = "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 310, 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 proteinsProtein S100-A9, immunoglobulin J chain, Ig alpha-1 chain C region, and CRISP-3have known roles in inflammation and bone resorption.",
author = "Ellias, {Mohd Faiz} and {Zainal Ariffin}, {Shahrul Hisham} and Karsani, {Saiful Anuar} and {Abdul Rahman}, Mariati and Sahidan Senafi and {Megat Abdul Wahab}, Rohaya",
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AU - Ellias, Mohd Faiz

AU - Zainal Ariffin, Shahrul Hisham

AU - Karsani, Saiful Anuar

AU - Abdul Rahman, Mariati

AU - Senafi, Sahidan

AU - Megat Abdul Wahab, Rohaya

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N2 - 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 310, 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 proteinsProtein S100-A9, immunoglobulin J chain, Ig alpha-1 chain C region, and CRISP-3have known roles in inflammation and bone resorption.

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