Abstract
Human dentin is not only a composite material of a collagenous matrix and mineral to provide strength and elasticity to teeth, but also a precious reservoir full of bioactive proteins. They are released after demineralization caused by bacterial acids in carious lesions, by decalcifying irrigants or dental materials and they modulate tissue responses in the underlying dental pulp. This work describes a first-time analysis of the proteome of human dentin using a shotgun proteomic approach that combines three different protein fractionation methods. Dentin matrix proteins were extracted by EDTA and separated by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), OFFGEL isoelectric focusing (IEF) or strong cation exchange chromatography (SCX). Liquid chromatography tandem mass spectrometry (LC-MS/MS) identified 813 human proteins with high confidence, however, isoelectric focusing turned out to be the most beneficial prefractionation method. All Proteins were categorized based on the PANTHER system and representation analysis revealed 31 classes and subclasses to be overrepresented. The acquired knowledge provides a comprehensive insight into the number of proteins in human dentin as well as their physiological and pathological functions. Thus, the data presented paves the way to the analysis of specific functions of dentin matrix proteins in vivo and their potential in tissue engineering approaches to regenerate dental pulp.
Highlights
It is known that these signaling molecules are released and allowed to diffuse into the pulpal tissue via the dentinal tubules by decalcification of dentin in carious lesions or by application of alkaline pulp-capping agents or acidic etchants in dentin bonding agents[2,3]
813 human proteins were detected in dentin extracts with high confidence (Mascot score ≥30; false discovery rate (FDR) ≤ 1%). 327 proteins were exclusively discovered after fractionation by isoelectric focusing (40.2%), 68 after gel electrophoresis (8.4%) and 28 after cation exchange chromatography (3.4%)
A comparison of the Mascot scores of all repeatedly detected proteins revealed that prefractionation by isoelectric focusing (IEF) led to the best score in 295 cases followed by SDS-PAGE (89) and strong cation exchange chromatography (SCX) (9) (Fig. 2a)
Summary
It is known that these signaling molecules are released and allowed to diffuse into the pulpal tissue via the dentinal tubules by decalcification of dentin in carious lesions or by application of alkaline pulp-capping agents or acidic etchants in dentin bonding agents[2,3]. The proteins released from dentin are believed to modulate immunoresponse, to exert chemotactic effects, to stimulate angiogenesis, cell proliferation and differentiation and to promote regenerative or reparative processes[4,5,6,7]
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