Proteomic analysis of dentin-enamel junction and adjacent protein-containing enamel matrix layer of healthy human molar teeth
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F67985823%3A_____%2F19%3A00504099" target="_blank" >RIV/67985823:_____/19:00504099 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11110/19:10395107 RIV/00216208:11310/19:10395107 RIV/00027006:_____/19:00004827
Result on the web
<a href="https://doi.org/10.1111/eos.12594" target="_blank" >https://doi.org/10.1111/eos.12594</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1111/eos.12594" target="_blank" >10.1111/eos.12594</a>
Alternative languages
Result language
angličtina
Original language name
Proteomic analysis of dentin-enamel junction and adjacent protein-containing enamel matrix layer of healthy human molar teeth
Original language description
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.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10406 - Analytical chemistry
Result continuities
Project
<a href="/en/project/GA17-10832S" target="_blank" >GA17-10832S: Advanced instrumentation and methodology for separation, analysis and characterization of (bio)moleclues by capillary electromigration methods.</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
European Journal of Oral Sciences
ISSN
0909-8836
e-ISSN
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Volume of the periodical
127
Issue of the periodical within the volume
2
Country of publishing house
DK - DENMARK
Number of pages
10
Pages from-to
112-121
UT code for WoS article
000461012500002
EID of the result in the Scopus database
2-s2.0-85056842697