Proteomic Analysis of Human Tooth Pulp: Proteomics of Human Tooth

Eckhardt, Adam; Jágr, Michal; Pataridis, Statis; Mikšı́k, Ivan

doi:10.1016/j.joen.2014.07.001

Cited by 39 publications

(75 citation statements)

References 29 publications

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“…Collagens type I are among the most abundant proteins in humans . They have also been detected in various human teeth tissues, such as dentin, tooth pulp, or dental cementum . Other types of collagen (type III and V) are scarce but present .…”

Section: Discussionmentioning

confidence: 99%

“…We detected 140 (pulp/dentin) shared proteins, 37 of which were not observed in plasma. We suggested that these proteins might participate in the unique pulp–dentin complex . On a weight basis, mature dentin consists of approximately 70% mineral, 20% organic matrix, and 10% water .…”

mentioning

confidence: 96%

“…It is a highly mineralized tissue that forms the bulk of the tooth, serving as a protective covering for the pulp as well as a support for overlying enamel. In our previous studies, we analyzed proteomics of human tooth dentin and pulp . We detected 140 (pulp/dentin) shared proteins, 37 of which were not observed in plasma.…”

mentioning

confidence: 99%

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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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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 96%

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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 transcriptome or RNA expression levels in these organisms are also being explored with the goal of understanding the timing of transcription, translation, and protein secretion as it pertains to the events occurring in the biomineralizing matrix . What has emerged from these studies…”

Section: Biomineral‐associated Secretomesmentioning

confidence: 99%

“…Within these genomes lurk mineralization‐associated genes. Since many biomineral‐associated proteins are extracellular and thus subjected to post‐translational modifications, these genomic studies have been augmented by proteomic studies that identify gene products that are phosphorylated, sulfated, glycosylated, enzymatically cleaved, or otherwise chemically modified at side‐chain groups . The challenge that we are now facing is to identify these mineralization‐associated proteins, their structure, synthesis, secretion, and temporal/regional localization, and most importantly, their purpose or function.…”

Section: Introductionmentioning

confidence: 99%

The Biomineralization Proteome: Protein Complexity for a Complex Bioceramic Assembly Process

Evans

2019

Proteomics

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There are over 62 different biominerals on Earth and a diverse array of organisms that generate these biominerals for survival. This review will introduce the process of biomineralization and the current understanding of the molecular mechanisms of mineral formation, and then comparatively explore the representative secretomes of two well-documented skeletal systems: vertebrate bone (calcium phosphate) and invertebrate mollusk shell (calcium carbonate). It is found that both skeletal secretomes have gross similarities and possess proteins that fall into four functional categories: matrix formers, nucleation assisters, communicators, and remodelers. In many cases the mineral-associated matrix former and nucleation assister sequences in both skeletal systems are unique and possess interactive conserved globular domains, intrinsic disorder, post-translational modifications, sequence redundancy, and amyloid-like aggregation-prone sequences. Together, these molecular features create a protein-based environment that facilitates mineral formation and organization and argue in favor of conserved features that evolve from the mollusk shell to bone. Interestingly, the mollusk shell secretome appears to be more complex compared to that of bone tissue, in that there are numerous protein subcategories that are required for the nucleation and organization of inner (nacre) and outer (prismatic) calcium carbonate regions of the shell. This may reflect the organizational and material requirements of an exoskeletal protective system.

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In‐bone protein digestion followed by LC‐MS/MS peptide analysis as a new way towards the routine proteomic characterization of human maxillary and mandibular bone tissue in oral surgery

et al. 2021

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In-bone protein digestion followed by LC-MS/MS peptide analysis as a new way towards the routine proteomic characterization of human maxillary and mandibular bone tissue in oral surgeryProteomic characterization of alveolar bones in oral surgery represents an analytical challenge due to their insoluble character. The implementation of a straightforward technique could lead to the routine use of proteomics in this field. This work thus developed a simple technique for the characterization of bone tissue for human maxillary and mandibular bones. It is based on the direct in-bone tryptic digestion of proteins in both healthy and pathological human maxillary and mandibular bone samples. The released peptides were then identified by the LC-MS/MS. Using this approach, a total of 1120 proteins were identified in the maxillary bone and 1151 proteins in the mandibular bone. The subsequent partial least squares-discrimination analysis (PLS-DA) of protein data made it possible to reach 100% discrimination between the samples of healthy alveolar bones and those of the bone tissue surrounding the inflammatory focus. These results indicate that the in-bone protein digestion followed by the LC-MS/MS and subsequent statistical analysis can provide a deeper insight into the field of oral surgery at the molecular level. Furthermore, it could also have a diagnostic potential in the differentiation between the proteomic patterns of healthy and pathological alveolar bone tissue. Data are available via ProteomeXchange with the identifier PXD026775.

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Proteomic Analysis of Human Tooth Pulp: Proteomics of Human Tooth

Cited by 39 publications

References 29 publications

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

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

The Biomineralization Proteome: Protein Complexity for a Complex Bioceramic Assembly Process

In‐bone protein digestion followed by LC‐MS/MS peptide analysis as a new way towards the routine proteomic characterization of human maxillary and mandibular bone tissue in oral surgery

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