Proteomic analysis of dentin–enamel junction and adjacent protein‐containing enamel matrix layer of healthy human molar teeth

• Published in: European journal of oral sciences Vol. 127; no. 2; pp. 112 - 121
• Main Authors: Jágr, Michal, Ergang, Peter, Pataridis, Statis, Kolrosová, Marta, Bartoš, Martin, Mikšík, Ivan
• Format: Journal Article
• Language: English
• Published: England Wiley Subscription Services, Inc 01-04-2019
• Subjects: AMBN protein; Amelogenin; Binding; Calcium; Calcium ions; Cell adhesion; Cell adhesion & migration; Chromatography, Liquid; Collagen; Crack propagation; Cytoskeleton; Dental Enamel; Dentin; Dentistry; Enamel; Extracellular matrix; Fracture toughness; Humans; laser capture microdissection; Liquid chromatography; Mass spectrometry; Mass spectroscopy; Microdissection; Mineralization; Molar; Molars; Proteins; Proteins - metabolism; proteome; Proteome - analysis; Proteomics; Proteomics - methods; Tandem Mass Spectrometry; Teeth; Tissues; Trypsin; mass spectrometry; dentin; laser capture microdissection; proteome
• ISSN: 0909-8836; 1600-0722
• DOI: 10.1111/eos.12594

The dentin–enamel junction (DEJ) is the border where two different mineralized structures – enamel and dentin – meet. The protein‐rich DEJ, together with the inner enamel region of mature teeth, is known to exhibit higher fracture toughness and crack growth resistance than bulk phase enamel. However, an explanation for this behavior has been hampered by the lack of compositional information for the DEJ and the adjacent enamel organic matrix (EOM). We studied proteomes of the DEJ and EOM of healthy human molars and compared them with dentin and enamel proteomes from the same teeth. These tissues were cut out of tooth sections by laser capture microdissection, proteins were extracted and cleaved by trypsin, then processed by liquid chromatography coupled to tandem mass spectrometry to analyze the proteome profiles of these tissues. This study identified 46 proteins in DEJ and EOM. The proteins identified have a variety of functions, including calcium ion‐binding, formation of extracellular matrix, formation of cytoskeleton, cytoskeletal protein binding, cell adhesion, and transport. Collagens were identified as the most dominant proteins. Tissue‐specific proteins, such as ameloblastin and amelogenin, were also detected. Our findings reveal new insight into proteomics of DEJ and EOM, highly mineralized tissues that are obviously difficult to analyze.