Complementing the pulp proteome via sampling with a picosecond infrared laser (PIRL)

Abstract

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.

Comparative proteomic analysis of dental pulp from supernumerary and normal permanent teeth

“…Despite differences in total detected proteins, GO enrichment analysis based on biological process terms in the present study highlighted similar functions as compared to previous studies of normal permanent dental pulp tissue (Fig. S1 ) [ 19 – 21 , 23 ]. For supernumerary permanent teeth, a total of 1,093 proteins were detected (Supplementary Table 3).…”

“…For supernumerary permanent teeth, a total of 1,093 proteins were detected (Supplementary Table 3). Interestingly, according to previous reports and this study, there have only been roughly 66 − 4,332 identified proteins in dental pulp tissue thus far (Supplementary Table 5) [19][20][21][22][23]. This is a relatively low number when compared to the number of proteins found in other tissue or in a single cell that have been previously reported [33,34].…”

“…However, the majority of current research, (Fig. S1) [19][20][21]23]. For supernumerary permanent teeth, a total of 1,093 proteins were detected (Supplementary Table 3).…”

“…including proteomic profiling, has focused mainly on the dental pulp of normal permanent teeth [19][20][21][22][23]. Investigation into the structure and function of supernumerary tooth dental pulp is needed, as the proteomic profile cannot be assumed identical to that of a normal permanent tooth.…”

“…As such, obtaining proteomics data for a particular tissue enhances our comprehension of its function and structure. To date, current literature on dental pulp tissue has focused mainly on the proteomic profile of normal permanent teeth [19][20][21][22][23]. The proteome of supernumerary dental pulp tissue has never been investigated, despite such teeth being far from fully understood.…”