Proteomic analysis of human tooth pulp: proteomics of human tooth
Language English Country United States Media print-electronic
Document type Comparative Study, Journal Article, Research Support, Non-U.S. Gov't
PubMed
25305236
DOI
10.1016/j.joen.2014.07.001
PII: S0099-2399(14)00635-9
Knihovny.cz E-resources
- Keywords
- 2-dimensional gel electrophoresis, Dentin, human pulp, pulp-dentin complex, tandem mass spectrometry, tooth proteome,
- MeSH
- Electrophoresis, Gel, Two-Dimensional MeSH
- Chromatography, Liquid MeSH
- Dentin chemistry MeSH
- Adult MeSH
- Energy Metabolism physiology MeSH
- Mass Spectrometry MeSH
- Immunoproteins analysis MeSH
- Blood Proteins analysis MeSH
- Humans MeSH
- Cell Communication physiology MeSH
- Young Adult MeSH
- Nanotechnology MeSH
- Cell Proliferation MeSH
- Proteins metabolism MeSH
- Proteome analysis classification MeSH
- Signal Transduction physiology MeSH
- Tandem Mass Spectrometry MeSH
- Dental Pulp chemistry MeSH
- Check Tag
- Adult MeSH
- Humans MeSH
- Young Adult MeSH
- Male MeSH
- Female MeSH
- Publication type
- Journal Article MeSH
- Research Support, Non-U.S. Gov't MeSH
- Comparative Study MeSH
- Names of Substances
- Immunoproteins MeSH
- Blood Proteins MeSH
- Proteins MeSH
- Proteome MeSH
INTRODUCTION: The unique pulp-dentin complex demonstrates strong regenerative potential, which enables it to respond to disease and traumatic injury. Identifying the proteins of the pulp-dentin complex is crucial to understanding the mechanisms of regeneration, tissue calcification, defense processes, and the reparation of dentin by dental pulp. The lack of knowledge of these proteins limits the development of more efficient therapies. METHODS: The proteomic profile of human tooth pulp was investigated and compared with the proteome of human dentin and blood. The samples of tooth pulp were obtained from 5 sound permanent human third molars of 5 adults (n = 5). The extracted proteins were separated by 2-dimensional gel electrophoresis, analyzed by nano-liquid chromatography tandem mass spectrometry, and identified by correlating mass spectra to the proteomic databases. RESULTS: A total of 342 proteins were identified with high confidence, and 2 proteins were detected for the first time in an actual human sample. The identified tooth pulp proteins have a variety of functions: structural, catalytic, transporter, protease activity, immune response, and many others. In a comparison with dentin and blood plasma, 140 (pulp/dentin) shared proteins were identified, 37 of which were not observed in plasma. It can be suggested that they might participate in the unique pulp-dentin complex. CONCLUSIONS: This proteomic investigation of human tooth pulp, together with the previously published study of human dentin, is one of the most comprehensive proteome lists of human teeth to date.
References provided by Crossref.org
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