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Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)
by
Feridouni Khamaneh, Yaghoup
, Schlüter, Hartmut
, Kiani, Parnian
, Friedrich, Reinhard E.
, Miller, R. J. Dwayne
in
Dental disorders
/ Dental Pulp
/ Dentistry
/ Humans
/ Lasers
/ Localization
/ Mass Spectrometry
/ Mass spectroscopy
/ Medicine
/ Original
/ Original Article
/ Proteins
/ Proteome
/ Proteomes
/ Proteomics
/ Sampling
/ Specimen Handling
/ Teeth
/ Trypsin
2021
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Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)
by
Feridouni Khamaneh, Yaghoup
, Schlüter, Hartmut
, Kiani, Parnian
, Friedrich, Reinhard E.
, Miller, R. J. Dwayne
in
Dental disorders
/ Dental Pulp
/ Dentistry
/ Humans
/ Lasers
/ Localization
/ Mass Spectrometry
/ Mass spectroscopy
/ Medicine
/ Original
/ Original Article
/ Proteins
/ Proteome
/ Proteomes
/ Proteomics
/ Sampling
/ Specimen Handling
/ Teeth
/ Trypsin
2021
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Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)
by
Feridouni Khamaneh, Yaghoup
, Schlüter, Hartmut
, Kiani, Parnian
, Friedrich, Reinhard E.
, Miller, R. J. Dwayne
in
Dental disorders
/ Dental Pulp
/ Dentistry
/ Humans
/ Lasers
/ Localization
/ Mass Spectrometry
/ Mass spectroscopy
/ Medicine
/ Original
/ Original Article
/ Proteins
/ Proteome
/ Proteomes
/ Proteomics
/ Sampling
/ Specimen Handling
/ Teeth
/ Trypsin
2021
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Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)
Journal Article
Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)
2021
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Overview
Objectives
The aim of this investigation was the detailed analysis of the human pulp proteome using the new picosecond infrared laser (PIRL)-based sampling technique, which is based on a completely different mechanism compared to mechanical sampling. Proteome analysis of healthy pulp can provide data to define changes in the proteome associated with dental disease.
Material and methods
Immediately after extraction of the entire, undamaged tooth, 15 wisdom teeth were deep frozen in liquid nitrogen and preserved at −80°C. Teeth were crushed, and the excised frozen pulps were conditioned for further analysis. The pulps were sampled using PIRL, and the aspirates digested with trypsin and analyzed with mass spectrometry. Pulp proteins were categorized according to their gene ontology terminus. Proteins identified exclusively in this study were searched in the Human Protein Atlas (HPA) for gaining information about the main known localization and function.
Results
A total of 1348 proteins were identified in this study. The comparison with prior studies showed a match of 72%. Twenty-eight percent of the proteins were identified exclusively in this study. Considering HPA, almost half of these proteins were assigned to tissues that could be pulp specific.
Conclusion
PIRL is releasing proteins from the dental pulp which are not dissolved by conventional sampling techniques.
Clinical Relevance
The presented data extend current knowledge on dental pulp proteomics in healthy teeth and can serve as a reference for studies on pulp proteomics in dental disease.
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