Proteomic analysis of human tooth pulp proteomes – Comparison of caries-resistant and caries-susceptible persons

Jágr, Michal; Eckhardt, Adam; Pataridis, Statis; Foltán, René; Myšák, Jaroslav; Mikšı́k, Ivan

doi:10.1016/j.jprot.2016.04.022

Cited by 24 publications

(25 citation statements)

References 52 publications

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“…Sample purification was improved by extracting tryptic peptides using Stage Tips . Nano‐liquid chromatography procedure, mass spectrometry (MS), and tandem MS (MS/MS) analyses were performed as described in our previous studies, with upgraded software. Our MS device (Maxis quadrupole time‐of‐flight mass spectrometer (Bruker Daltonics, Bremen, Germany)) allowed us to compare up to 100 most abundant proteins in two data sets using label‐free quantification.…”

Section: Methodsmentioning

confidence: 99%

Novel contribution to clubfoot pathogenesis: The possible role of extracellular matrix proteins

Eckhardt

Novotný

Doubková

et al. 2019

Journal Orthopaedic Research

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Idiopathic pes equinovarus (clubfoot) is a congenital deformity of the feet and lower legs. Clubfoot belongs to a group of fibro‐proliferative disorders but its origin remains unknown. Our study aimed to achieve the first complex proteomic comparison of clubfoot contracted tissue of the foot (medial side; n = 16), with non‐contracted tissue (lateral side; n = 13). We used label‐free mass spectrometry quantification and immunohistochemistry. Seven proteins were observed to be significantly upregulated in the medial side (asporin, collagen type III, V, and VI, versican, tenascin‐C, and transforming growth factor beta induced protein) and four in the lateral side (collagen types XII and XIV, fibromodulin, and cartilage intermediate layer protein 2) of the clubfoot. Comparison of control samples from cadavers brought only two different protein concentrations (collagen types I and VI). We also revealed pathological calcification and intracellular positivity of transforming growth factor beta only in the contracted tissue of clubfoot. Most of the 11 differently expressed proteins are strongly related to the extracellular matrix architecture and we assume that they may play specific roles in the pathogenesis of this deformity. These proteins seem to be promising targets for future investigations and treatment of this disease. © 2019 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res

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Section: Methodsmentioning

confidence: 99%

Novel contribution to clubfoot pathogenesis: The possible role of extracellular matrix proteins

Eckhardt

Novotný

Doubková

et al. 2019

Journal Orthopaedic Research

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“…2.3.0, http://www.matrixscience.com). Database searches were performed, as described in our previous study, with the taxonomy restricted to Homo sapiens to remove protein identification redundancy . Briefly, trypsin (or semitrypsin) was chosen as an enzyme parameter.…”

Section: Methodsmentioning

confidence: 99%

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

Jágr

Ergang

Pataridis

et al. 2018

European J Oral Sciences

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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.

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“…The mixture was centrifuged PLOS ONE at 9000 × g for 10 min at 4˚C and the remaining pellet was solubilized with 600 μl lysis buffer containing 30 mM Tris, 7 M urea, 2 M thiourea, 4% (w/v) 3-[(3-cholamidopropyl) dimethylammonio]-1-propanesulfonate (CHAPS), pH was adjusted to 8.5 with 50 mM NaOH. Each 50 μg of protein sample (−M10, +M10 and −M10/−M20, +M10/−M20) was labeled with 600 pmol of cyanine CyDye DIGE Fluor minimal dyes Cy3, Cy5 or Cy2 according to Jágr et al [20].…”

Section: D-digementioning

confidence: 99%

“…The two-dimensional fluorescence difference gel electrophoresis (2D-DIGE) and MALDI--TOF MS/MS was used for comparison of protein profiling in hippocampal samples prepared from (+M10), (−M10), (+M10/−M20) and (−M10/−M20) groups of rats, [19,20]. Results obtained by 2D-DIGE were verified by immunoblot analysis of 2D gels and a gel-free, label free proteomic analysis, MaxLFQ [21].…”

Section: Introductionmentioning

confidence: 99%

Proteomic analysis of protein composition of rat hippocampus exposed to morphine for 10 days; comparison with animals after 20 days of morphine withdrawal

et al. 2020

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Opioid addiction is recognized as a chronic relapsing brain disease resulting from repeated exposure to opioid drugs. Cellular and molecular mechanisms underlying the ability of organism to return back to the physiological norm after cessation of drug supply are not fully understood. The aim of this work was to extend our previous studies of morphine-induced alteration of rat forebrain cortex protein composition to the hippocampus. Rats were exposed to morphine for 10 days and sacrificed 24 h (groups +M10 and −M10) or 20 days after the last dose of morphine (groups +M10/−M20 and −M10/−M20). The six altered proteins (�2-fold) were identified in group (+M10) when compared with group (−M10) by twodimensional fluorescence difference gel electrophoresis (2D-DIGE). The number of differentially expressed proteins was increased to thirteen after 20 days of the drug withdrawal. Noticeably, the altered level of α-synuclein, β-synuclein, α-enolase and glyceraldehyde-3phosphate dehydrogenase (GAPDH) was also determined in both (±M10) and (±M10/ −M20) samples of hippocampus. Immunoblot analysis of 2D gels by specific antibodies oriented against α/β-synucleins and GAPDH confirmed the data obtained by 2D-DIGE analysis. Label-free quantification identified nineteen differentially expressed proteins in group (+M10) when compared with group (−M10). After 20 days of morphine withdrawal (±M10/−-M20), the number of altered proteins was increased to twenty. We conclude that the morphine-induced alteration of protein composition in rat hippocampus after cessation of drug supply proceeds in a different manner when compared with the forebrain cortex. In forebrain cortex, the total number of altered proteins was decreased after 20 days without morphine, whilst in hippocampus, it was increased.

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Proteomic analysis of human tooth pulp proteomes – Comparison of caries-resistant and caries-susceptible persons

Cited by 24 publications

References 52 publications

Novel contribution to clubfoot pathogenesis: The possible role of extracellular matrix proteins

Novel contribution to clubfoot pathogenesis: The possible role of extracellular matrix proteins

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

Proteomic analysis of protein composition of rat hippocampus exposed to morphine for 10 days; comparison with animals after 20 days of morphine withdrawal

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