Global proteome profiling of dental cementum under experimentally-induced apposition

Salmon, Cristiane R.; Giorgetti, Ana Paula Oliveira; Leme, Adriana Franco Paes; Domingues, Romênia R.; Sallum, Enílson Antônio; Alves, Marcelo Corrêa; Kolli, Tamara N.; Foster, Brian L.; Nociti, Francisco Humberto

doi:10.1016/j.jprot.2016.03.036

Cited by 22 publications

(29 citation statements)

References 59 publications

(69 reference statements)

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“…It is used for isolation of small pieces of cells and tissues, often mineralized, and for further proteomic study of these samples. In this way, LCM – together with the LC‐MS/MS technique – was successfully used to study proteins associated with dental cementum formation in mouse teeth . Laser capture microdissection was also utilized in comprehensive analyses of gene expression in mouse junctional epithelium and oral gingival epithelium to search for specific genetic markers of junctional epithelium, which attaches to tooth enamel at the dentogingival junction .…”

Section: Discussionmentioning

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%

“…Combining the results obtained from these two methods enabled us to identify a total of 46 proteins in DEJ + EOM samples (Table ). We also tried another protein‐extraction method –extraction of proteins to 8 M urea solution . However, this method afforded a significantly lower yield in protein numbers (data not shown).…”

Section: Discussionmentioning

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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“…DCN has been suggested not only to regulate the organization of collagen fibrils but also to be involved in PDL homeostasis by regulating cell proliferation (Häkkinen et al, 2000 ; Wang et al, 2014 ). In the adult, all these antigens are still present in the PDL (Salmon et al, 2016 ). Asporin is considered a negative regulator of mineralization, specific for the PDL (Leong et al, 2012 ).…”

Section: Discussionmentioning

confidence: 99%

Regulators of Collagen Fibrillogenesis during Molar Development in the Mouse

2017

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Development of mammalian teeth and surrounding tissues includes time–space changes in the extracellular matrix composition and organization. This requires complex control mechanisms to regulate its synthesis and remodeling. Fibril-associated collagens with interrupted triple helices (FACITs) and a group of small leucine-rich proteoglycans (SLRPs) are involved in the regulation of collagen fibrillogenesis. Recently, collagen type XII and collagen type XIV, members of the FACITs family, were found in the peridental mesenchyme contributing to alveolar bone formation. This study was designed to follow temporospatial expression of collagen types XIIa and XIVa in mouse first molar and adjacent tissues from embryonic day 13, when the alveolar bone becomes morphologically apparent around the molar tooth bud, until postnatal day 22, as the posteruption stage. The patterns of decorin, biglycan, and fibromodulin, all members of the SLRPs family and interacting with collagens XIIa and XIVa, were investigated simultaneously. The situation in the tooth was related to what happens in the alveolar bone, and both were compared to the periodontal ligament. The investigation provided a complex localization of the five antigens in soft tissues, the dental pulp, and periodontal ligaments; in the mineralized tissues, predentin/dentin and alveolar bone; and junction between soft and hard tissues. The results illustrated developmentally regulated and tissue-specific changes in the balance of the two FACITs and three SLRPs.

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“…Samples were sonicated and centrifuged briefly. Whole protein extracts were reduced, alkylated, and trypsin digested as described previously [28–30]. The resulting tryptic peptide samples were dried in a vacuum concentrator and reconstituted in 0.1% formic acid for analysis.…”

Section: Methodsmentioning

confidence: 99%

Osteopontin regulates dentin and alveolar bone development and mineralization

Foster

Salmon

et al. 2018

Bone

108

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The periodontal complex is essential for tooth attachment and function and includes the mineralized tissues, cementum and alveolar bone, separated by the unmineralized periodontal ligament (PDL). To gain insights into factors regulating cementum-PDL and bone-PDL borders and protecting against ectopic calcification within the PDL, we employed a proteomic approach to analyze PDL tissue from progressive ankylosis knock-out (Ank) mice, featuring reduced PP, rapid cementogenesis, and excessive acellular cementum. Using this approach, we identified the matrix protein osteopontin (Spp1/OPN) as an elevated factor of interest in Ank mouse molar PDL. We studied the role of OPN in dental and periodontal development and function. During tooth development in wild-type (WT) mice, Spp1 mRNA was transiently expressed by cementoblasts and strongly by alveolar bone osteoblasts. Developmental analysis from 14 to 240days postnatal (dpn) indicated normal histological structures in Spp1 comparable to WT control mice. Microcomputed tomography (micro-CT) analysis at 30 and 90dpn revealed significantly increased volumes and tissue mineral densities of Spp1 mouse dentin and alveolar bone, while pulp and PDL volumes were decreased and tissue densities were increased. However, acellular cementum growth was unaltered in Spp1 mice. Quantitative PCR of periodontal-derived mRNA failed to identify potential local compensators influencing cementum in Spp1 vs. WT mice at 26dpn. We genetically deleted Spp1 on the Ank mouse background to determine whether increased Spp1/OPN was regulating periodontal tissues when the PDL space is challenged by hypercementosis in Ank mice. Ank; Spp1 double deficient mice did not exhibit greater hypercementosis than that in Ank mice. Based on these data, we conclude that OPN has a non-redundant role regulating formation and mineralization of dentin and bone, influences tissue properties of PDL and pulp, but does not control acellular cementum apposition. These findings may inform therapies targeted at controlling soft tissue calcification.

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Global proteome profiling of dental cementum under experimentally-induced apposition

Cited by 22 publications

References 59 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

Regulators of Collagen Fibrillogenesis during Molar Development in the Mouse

Osteopontin regulates dentin and alveolar bone development and mineralization

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