Proteomics of Human Teeth and Saliva

Jágr, Michal; Eckhardt, Adam; Pataridis, Statis; Broukal, Z; Dušková, Jana; Mikšı́k, Ivan

doi:10.33549/physiolres.932702

Cited by 38 publications

(25 citation statements)

References 100 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…However, so far, there are only a few studies dealing with the proteome analysis of dental pulp. The studies differ from each other in the total number and characteristics of the proteins [3][4][5][6][7]. The differences in the number and composition of the identified dental pulp proteins from previous studies are in part due to different methods of determination as well as the presence of blood proteins, which can reduce the number of identifiable proteins because of the suppression effect in mass spectrometry (MS), which is in general a successful technique for protein analysis [8][9][10][11][12].…”

Section: Introductionmentioning

confidence: 99%

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

et al. 2021

View full text Add to dashboard Cite

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.

show abstract

Section: Introductionmentioning

confidence: 99%

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

et al. 2021

View full text Add to dashboard Cite

show abstract

“…All the proteins common to the five proteomes, with the exception of COL10A1 and COL23 A1, have already been identified in human dentine extracts [44,46,52], although AMBN may also be derived from the enamel [45,53]. COL22A1 and F2 have been detected…”

Section: Discussionmentioning

confidence: 98%

“…The other 30% proteins include the amelogenin protein specific to the enamel tissue, diverse collagens, in addition to constituents of the extracellular matrix and immune system proteins (Fig S5B). The later components may reflect the dynamic and heterogeneous part of dentine, a tissue rich in diverse bioactive peptides involved in host defense, regenerative process, angiogenesis, growth and differentiation [44][45][46][47]. These are expected to vary between species or individuals depending on health status and/or traumatic injury [42,47,48].…”

Section: Discussionmentioning

confidence: 99%

Protein sequence comparison of human and non-human primate tooth proteomes

Froment

Zanolli

Hourset

et al. 2021

Journal of Proteomics

View full text Add to dashboard Cite

In the context of human evolution, the study of proteins may overcome the limitation of the high degradation of ancient DNA over time to provide biomolecular information useful for the phylogenetic reconstruction of hominid taxa. In this study, we used a shotgun proteomics approach to compare the tooth proteomes of extant human and non-human primates (gorilla, chimpanzee, orangutan and baboon) in order to search for a panel of peptides able to discriminate between taxa and further help reconstructing the evolutionary relationships of fossil primates. Among the 25 proteins shared by the five genera datasets, we found a combination of peptides with sequence variations allowing to differentiate the hominid taxa in the proteins AHSG, AMBN, APOA1, BGN, C9, COL11A2, COL22A1, COL3A1, DSPP, F2, LUM, OMD, PCOLCE and SERPINA1. The phylogenetic tree confirms the placement of the samples in the appropriate genus branches. Altogether, the results provide experimental evidence that a shotgun proteomics approach on dental tissue has the potential to detect taxonomic variation, which is promising for future investigations of uncharacterized and/or fossil hominid/hominin specimens.

show abstract

“…Recent advances in protein fragmentation methods and mass spectrometry technologies have made possible the analysis of proteomic profiles from the acquired enamel pellicle and have detected up to 363 various peptides and proteins 150 . Abundant proteinic pellicle constituents, such as sialylated mucins, statherins, histatins, cystatins, or proline‐rich proteins reveal binding motifs for surface receptors of bacteria, thereby enabling the adhesion of early colonizing species 36‐38 . Predominant early colonizers such as Streptococcus salivarius, Streptococcus mitis, Streptococcus oralis , and Streptococcus sanguinis allow the subsequent co‐adhesion of Gram‐negative anaerobes, including Fusobacterium nucleatum, Prevotella melaninogenica , and Veillonella spp 17 .…”

Section: The Metaproteome Of Caries‐associated Biofilmsmentioning

confidence: 99%

Metaproteome and metabolome of oral microbial communities

Bostancı

Grant

Bao

et al. 2020

Periodontology 2000

View full text Add to dashboard Cite

Protein function is representative of active biologic processes, and the proteome describes the entire protein makeup of a cell, tissue, or bodily fluid at a given point in time. The composition and modular organization of the proteome governs the phenotype. The term proteomics was coined in 1994 1 and over the last 25 years the field has advanced with the rapid changes in mass spectrometry instrumentation and innovations in quantitative chemistries and bioinformatic tools. Although two-dimensional gel electrophoresis, accompanied by mass spectrometry detection, was extensively used as the proteomics method of choice in earlier days, 2,3 it is time-consuming, labor-intensive, and limited by the number of resolved proteins. 4 Currently, liquid chromatography coupled to tandem mass spectrometry is the most valuable tool for the systematic identification and quantification of proteins on a large scale. 5 Most of the proteomics workflows seek to identify a set of proteins (discovery proteomics) or to quantify a relative or absolute amount of identified proteins (quantitative proteomics) between conditions or to study the protein interactions within larger protein complexes (interactomes) or in the context of broader biologic networks (systems biology). 6 The spectrum fragmentation method includes two approaches, namely, "untargeted shotgun proteomics", which help achieve a deep coverage of the proteome, and "targeted proteomics" for quantitatively comparing large numbers of samples (hundreds to thousands) based on a defined set of proteins (eg, selected reaction monitoring) (Figure 1). Most high-throughput proteomic strategies utilize "bottom-up" workflows that rely on mass spectrometry analysis of digested peptides from proteins with the help of specific enzymes (eg, trypsin), but a "top-down" approach for analysis of intact proteins is also possible. This allows not only identification of a protein by name, but also of its intact molecular form, the presence of isoforms, and potential modifications. 7 The large-scale characterization of any given proteome is accomplished by comparing measured protein or peptide data with predicted protein or peptide data derived from genomic information.

show abstract

Proteomics of Human Teeth and Saliva

Cited by 38 publications

References 100 publications

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

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

Protein sequence comparison of human and non-human primate tooth proteomes

Metaproteome and metabolome of oral microbial communities

Contact Info

Product

Resources

About