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Current Biology : CB May 2020Mammals and reptiles have evolved divergent adaptations for processing abrasive foods. Mammals have occluding, diphyodont dentitions with taller teeth (hypsodonty), more...
Mammals and reptiles have evolved divergent adaptations for processing abrasive foods. Mammals have occluding, diphyodont dentitions with taller teeth (hypsodonty), more complex occlusal surfaces, continuous tooth eruption, and forms of prismatic enamel that prolong the functional life of each tooth [1, 2]. The evolution of prismatic enamel in particular was a key innovation that made individual teeth more resilient to abrasion in early mammals [2-4]. In contrast, reptiles typically have thin, non-prismatic enamel, and shearing, polyphyodont dentitions with multi-cusped or serrated tooth crowns, multiple tooth rows, rapid tooth replacement rates, or batteries made of hundreds of teeth [5-9]. However, there are rare cases where reptiles have evolved alternative solutions to cope with abrasive diets. Here, we show that the combined effects of herbivory and an ancestral loss of tooth replacement in a lineage of extinct herbivorous sphenodontians, distant relatives of the modern tuatara (Sphenodon punctatus) [10], are associated with the evolution of wear-resistant and highly complex teeth. Priosphenodon avelasi, an extinct sphenodontian from the Cretaceous of Argentina, possesses a unique cone-in-cone dentition with overlapping generations of teeth forming a densely packed tooth file. Each tooth is anchored to its predecessor via a rearrangement of dental tissues that results in a novel enamel-to-bone tooth attachment. Furthermore, the compound occlusal surfaces, thickened enamel, and the first report of prismatic enamel in a sphenodontian are convergent strategies with those in some mammals, challenging the perceived simplicity of acrodont dentitions [11-15] and showcasing the reptilian capacity to produce complex and unusual dentitions.
Topics: Animals; Argentina; Dental Enamel; Fossils; Reptiles; Tooth
PubMed: 32220319
DOI: 10.1016/j.cub.2020.02.071 -
Scientific Reports Feb 2022As the hardest tissue in the human body, tooth enamel formation is a highly regulated process involving several stages of differentiation and key regulatory genes. One...
As the hardest tissue in the human body, tooth enamel formation is a highly regulated process involving several stages of differentiation and key regulatory genes. One such gene, tryptophan-aspartate repeat domain 72 (WDR72), has been found to cause a tooth enamel defect when deleted or mutated, resulting in a condition called amelogenesis imperfecta. Unlike the canonical genes regulating tooth development, WDR72 remains intracellularly and is not secreted to the enamel matrix space to regulate mineralization, and is found in other major organs of the body, namely the kidney, brain, liver, and heart. To date, a link between intracellular vesicle transport and enamel mineralization has been suggested, however identification of the mechanistic regulators has yet to be elucidated, in part due to the limitations associated with studying highly differentiated ameloblast cells. Here we show compelling evidence that WDR72 regulates endocytosis of proteins, both in vivo and in a novel in vitro ameloblast cell line. We elucidate WDR72's function to be independent of intracellular vesicle acidification while still leading to defective enamel matrix pH extracellularly. We identify a vesicle function associated with microtubule assembly and propose that WDR72 directs microtubule assembly necessary for membrane mobilization and subsequent vesicle transport. Understanding WDR72 function provides a mechanistic basis for determining physiologic and pathologic tissue mineralization.
Topics: Ameloblasts; Amelogenesis Imperfecta; Brain; Calcification, Physiologic; Cell Differentiation; Dental Enamel; Endocytosis; Humans; Kidney; Liver; Microtubules; Myocardium; Tooth
PubMed: 35181734
DOI: 10.1038/s41598-022-06751-1 -
Proceedings of the National Academy of... Dec 2022The outstanding mechanical and chemical properties of dental enamel emerge from its complex hierarchical architecture. An accurate, detailed multiscale model of the...
The outstanding mechanical and chemical properties of dental enamel emerge from its complex hierarchical architecture. An accurate, detailed multiscale model of the structure and composition of enamel is important for understanding lesion formation in tooth decay (dental caries), enamel development (amelogenesis) and associated pathologies (e.g., amelogenesis imperfecta or molar hypomineralization), and minimally invasive dentistry. Although features at length scales smaller than 100 nm (individual crystallites) and greater than 50 µm (multiple rods) are well understood, competing field of view and sampling considerations have hindered exploration of mesoscale features, i.e., at the level of single enamel rods and the interrod enamel (1 to 10 µm). Here, we combine synchrotron X-ray diffraction at submicrometer resolution, analysis of crystallite orientation distribution, and unsupervised machine learning to show that crystallographic parameters differ between rod head and rod tail/interrod enamel. This variation strongly suggests that crystallites in different microarchitectural domains also differ in their composition. Thus, we use a dilute linear model to predict the concentrations of minority ions in hydroxylapatite (Mg and CO/Na) that plausibly explain the observed lattice parameter variations. While differences within samples are highly significant and of similar magnitude, absolute values and the sign of the effect for some crystallographic parameters show interindividual variation that warrants further investigation. By revealing additional complexity at the rod/interrod level of human enamel and leaving open the possibility of modulation across larger length scales, these results inform future investigations into mechanisms governing amelogenesis and introduce another feature to consider when modeling the mechanical and chemical performance of enamel.
Topics: Humans; Dental Caries; Crystallography; Amelogenesis Imperfecta; Amelogenesis; Dental Enamel
PubMed: 36534796
DOI: 10.1073/pnas.2211285119 -
L' Orthodontie Francaise Jun 2009Enamel conditioning (elimination of dental plaque and creation of an irregular surface) is an essential step before bonding of orthodontic brackets. The most popular...
Enamel conditioning (elimination of dental plaque and creation of an irregular surface) is an essential step before bonding of orthodontic brackets. The most popular procedure in our practice is bonding with resin which requires enamel etching in order to get enough shear bond strength. Many studies have tried to evaluate the effects of enamel bonding using the acid-etching procedure as well as the changes caused by detachment of brackets. Thanks to the development of other adhesives such as glass ionomer cements which chemically bind to the enamel, new enamel conditioning methods appeared, in particular sandblasting with aluminium oxide particles. This technique is a mechanical preparation of the tooth that avoids the harmful effects of acid products. By suitably choosing the parameters of sandblasting (pressure, time and quantity of powder), enamel loss is lower than with the acid-etch procedure and the surface of the enamel seems less affected. However the bond strength remains superior to the values required for treatment. The presented results indicate that enamel sandblasting can be considered as an alternative for the acid-etching technique currently used in orthodontic practice because it creates sufficient strength and respects enamel thickness better.
Topics: Acid Etching, Dental; Acrylic Resins; Aluminum Oxide; Dental Bonding; Dental Enamel; Dental Materials; Enamel Microabrasion; Humans; Malates; Microscopy, Electron, Scanning; Orthodontic Appliances; Phosphoric Acids; Stress, Mechanical; Surface Properties; Tooth Preparation
PubMed: 19552877
DOI: 10.1051/orthodfr/2009012 -
The Chinese Journal of Dental Research 2014Casein phosphopeptides-amorphous calcium phosphate (CPP-ACP) is a bioactive agent with a base of milk products, which has been formulated from two parts: casein... (Review)
Review
Casein phosphopeptides-amorphous calcium phosphate (CPP-ACP) is a bioactive agent with a base of milk products, which has been formulated from two parts: casein phosphopeptides (CPP) and amorphous calcium phosphate (ACP). CPP was produced from milk protein casein and has a remarkable ability to stabilize calcium phosphate in solution and to substantially increase the level of calcium phosphate in dental plaque. CPP-ACP buffers the free calcium and phosphate ion activities, thereby helping to maintain a state of supersaturation with respect to tooth enamel, reducing demineralisation and promoting remineralisation. The free calcium and phosphate ions move out of the CPP, enter the enamel rods and reform onto apatite crystals. Laboratory, animal and human studies have shown that CPP-ACP inhibits cariogenic activity. CPP-ACP is useful in the treatment of white spot lesions, hypomineralised enamel, mild fluorosis, tooth sensitivity and erosion, and prevents plaque accumulation around brackets and other orthodontic appliances. CPP-ACP also facilitates a normal post-eruptive maturation process and is ideal for protecting primary teeth at a time when oral care is difficult. CPP-ACP has commercial potential as an additive to foods, soft drinks and chewing gum, as well as additive to toothpastes and mouthwashes to control dental caries.
Topics: Calcium Phosphates; Cariostatic Agents; Caseins; Dental Enamel; Dental Plaque; Humans; Protective Agents; Tooth Remineralization; Tooth, Deciduous
PubMed: 25028684
DOI: No ID Found -
Journal of Structural Biology Dec 2021During enamel formation, the organic enamel protein matrix interacts with calcium phosphate minerals to form elongated, parallel, and bundled enamel apatite crystals of... (Review)
Review
During enamel formation, the organic enamel protein matrix interacts with calcium phosphate minerals to form elongated, parallel, and bundled enamel apatite crystals of extraordinary hardness and biomechanical resilience. The enamel protein matrix consists of unique enamel proteins such as amelogenin, ameloblastin, and enamelin, which are secreted by highly specialized cells called ameloblasts. The ameloblasts also facilitate calcium and phosphate ion transport toward the enamel layer. Within ameloblasts, enamel proteins are transported as a polygonal matrix with 5 nm subunits in secretory vesicles. Upon expulsion from the ameloblasts, the enamel protein matrix is re-organized into 20 nm subunit compartments. Enamel matrix subunit compartment assembly and expansion coincide with C-terminal cleavage by the MMP20 enamel protease and N-terminal amelogenin self-assembly. Upon enamel crystal precipitation, the enamel protein phase is reconfigured to surround the elongating enamel crystals and facilitate their elongation in C-axis direction. At this stage of development, and upon further amelogenin cleavage, central and polyproline-rich fragments of the amelogenin molecule associate with the growing mineral crystals through a process termed "shedding", while hexagonal apatite crystals fuse in longitudinal direction. Enamel protein sheath-coated enamel "dahlite" crystals continue to elongate until a dense bundle of parallel apatite crystals is formed, while the enamel matrix is continuously degraded by proteolytic enzymes. Together, these insights portrait enamel mineral nucleation and growth as a complex and dynamic set of interactions between enamel proteins and mineral ions that facilitate regularly seeded apatite growth and parallel enamel crystal elongation.
Topics: Ameloblasts; Amelogenesis; Amelogenin; Animals; Apatites; Calcium; Calcium Phosphates; Crystallization; Dental Enamel; Dental Enamel Proteins; Humans; Microscopy, Electron; Minerals
PubMed: 34748943
DOI: 10.1016/j.jsb.2021.107809 -
Archives of Oral Biology Sep 2023Variation in enamel and dentine mineral concentration and total effective density can be reliably collected using Micro-CT scans. Both variables are suggested to reflect...
OBJECTIVE
Variation in enamel and dentine mineral concentration and total effective density can be reliably collected using Micro-CT scans. Both variables are suggested to reflect mechanical properties such as hardness and elastic modulus in dental tissues, meaning Micro-CT methods allow relative composition and mechanical properties to be collected non-destructively.
DESIGN
16 lower molars from 16 Catarrhine primates were Micro-CT scanned alongside hydroxyapatite phantoms using standardized settings and methods to calculate mineral concentration and total effective density. Mineral concentration, total effective density and thickness of dentine and enamel were calculated for four cusps, representing each 'corner' of the tooth and four lateral crown positions (i.e., mesial, buccal, lingual and distal).
RESULTS
The results show mean mineral concentration and total effective density values were higher in areas of thicker enamel, while the opposite was observed for dentine. Buccal positions had significantly higher mineral concentration and total effective density values than lingual areas. Cuspal positions had higher mean values than lateral enamel, for both dentine (mineral concentration cuspal: 1.26 g/cm; lateral: 1.20 g/cm) and enamel (mineral concentration cuspal: 2.31 g/cm; lateral: 2.25 g/cm). Mesial enamel had significantly lower values than other locations.
CONCLUSIONS
These common patterns across Catarrhine taxa may be linked to functional adaptations related to optimization of mastication and tooth protection. Variation in mineral concentration and total effective density may also be associated with wear and fracture patterns, and can be used as baseline information to investigate the effect of diet, pathological changes and aging on teeth through time.
Topics: Animals; Dentin; Dental Enamel; Molar; Tooth; Primates
PubMed: 37385050
DOI: 10.1016/j.archoralbio.2023.105752 -
Journal of Dental Research Jun 2015Enamel is unique. It is the only epithelial-derived mineralized tissue in mammals and has a distinct micro- and nanostructure with nanofibrous apatite crystals as... (Review)
Review
Enamel is unique. It is the only epithelial-derived mineralized tissue in mammals and has a distinct micro- and nanostructure with nanofibrous apatite crystals as building blocks. It is synthesized by a highly specialized cell, the ameloblast, which secretes matrix proteins with little homology to any other known amino acid sequence, but which is composed of a primary structure that makes it competent to self-assemble and control apatite crystal growth at the nanometer scale. The end-product of ameloblast activity is a marvel of structural engineering: a material optimized to provide the tooth with maximum biting force, withstanding millions of cycles of loads without catastrophic failure, while also protecting the dental pulp from bacterial attack. This review attempts to bring into context the mechanical behavior of enamel with the developmental process of amelogenesis and structural development, since they are linked to tissue function, and the importance of controlling calcium phosphate mineralization at the nanometer scale. The origins of apatite nanofibers, the development of a stiffness gradient, and the biological processes responsible for the synthesis of a hard and fracture-resistant dental tissue are discussed with reference to the evolution of enamel from a fibrous composite to a complex, tough, and damage-tolerant coating on dentin.
Topics: Ameloblasts; Amelogenesis; Apatites; Biomechanical Phenomena; Calcium Phosphates; Crystallization; Dental Enamel; Dental Enamel Proteins; Humans; Nanofibers; Tooth Calcification
PubMed: 25800708
DOI: 10.1177/0022034515577963 -
Matrix Biology : Journal of the... 2016Dental enamel is the hardest tissue in the human body, and although it starts as a tissue rich in proteins, by the time of eruption of the tooth in the oral cavity only... (Review)
Review
Dental enamel is the hardest tissue in the human body, and although it starts as a tissue rich in proteins, by the time of eruption of the tooth in the oral cavity only a small fraction of the protein remains. While this organic matrix of enamel represents less than 1% by weight it plays essential roles in improving both toughness and resilience to chemical attacks. Despite the fact that the first studies of the enamel matrix began in the 19th century, its exact composition and mechanisms of its function remain poorly understood. It was proposed that keratin or a keratin-like primitive epithelial component exists in mature enamel, however due to the extreme insolubility of its organic matrix the presence of keratins there was never clearly established. We have recently identified expression of a number of hair keratins in ameloblasts, the enamel secreting cells, and demonstrated their incorporation into mature enamel. Mutation in epithelial hair keratin KRT75 leads to a skin condition called pseudofollicularis barbae. Carriers of this mutation have an altered enamel structure and mechanical properties. Importantly, these individuals have a much higher prevalence of caries. To the best of our knowledge, this is the first study showing a direct link between a mutation in a protein-coding region of a gene and increased caries rates. In this paper we present an overview of the evidence of keratin-like material in enamel that has accumulated over the last 150years. Furthermore, we propose potential mechanisms of action of KTR75 in enamel and highlight the clinical implications of the link between mutations in KRT75 and caries. Finally, we discuss the potential use of keratins for enamel repair.
Topics: Animals; Dental Caries; Dental Enamel; Hair Diseases; Humans; Keratins, Hair-Specific; Keratins, Type II; Mutation
PubMed: 26709044
DOI: 10.1016/j.matbio.2015.12.007 -
Journal of Dental Research Apr 2017The acquired enamel pellicle is an oral, fluid-derived protein layer that forms on the tooth surface. It is a biologically and clinically important integument that...
The acquired enamel pellicle is an oral, fluid-derived protein layer that forms on the tooth surface. It is a biologically and clinically important integument that protects teeth against enamel demineralization, and abrasion. Tooth surfaces are exposed to different proteinaceous microenvironments depending on the enamel location. For instance, tooth surfaces close to the gingival sulcus contact serum proteins that emanate via this sulcus, which may impact pellicle composition locally. The aims of this study were to define the major salivary and serum components that adsorb to hydroxyapatite, to study competition among them, and to obtain preliminary evidence in an in vivo saliva/serum pellicle model. Hydroxyapatite powder was incubated with saliva and serum, and the proteins that adsorbed were identified by mass spectrometry. To study competition, saliva and serum proteins were labeled with CyDyes, mixed in various proportions, and incubated with hydroxyapatite. In vivo competition was assessed using a split-mouth design, with half the buccal tooth surfaces coated with serum and the other half with saliva. After exposure to the oral environment for 0 min, 30 min and 2 h, the pellicles were analyzed by SDS-PAGE. In pure saliva- or serum-derived pellicles, 82 and 84 proteins were identified, respectively. When present concomitantly, salivary protein adsorbers effectively competed with serum protein adsorbers for the hydroxyapatite surface. Specifically, acidic proline-rich protein, cystatin, statherin and protein S100-A9 proteins competed off apolipoproteins, complement C4-A, haptoglobin, transthyretin and serotransferrin. In vivo evidence further supported the replacement of serum proteins by salivary proteins. In conclusion, although significant numbers of serum proteins emanate from the gingival sulcus, their ability to participate in dental pellicle formation is likely reduced in the presence of strong salivary protein adsorbers. The functional properties of the acquired enamel pellicle will therefore be mostly dictated by the salivary component.
Topics: Adsorption; Biofilms; Blood Proteins; Chromatography, Liquid; Dental Enamel; Dental Pellicle; Durapatite; Humans; Male; Mass Spectrometry; Proteomics; Saliva; Salivary Proteins and Peptides; Surface Properties
PubMed: 27879420
DOI: 10.1177/0022034516680771