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      Tooth Enamel and Its Dynamic Protein Matrix

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          Abstract

          Tooth enamel is the outer covering of tooth crowns, the hardest material in the mammalian body, yet fracture resistant. The extremely high content of 95 wt% calcium phosphate in healthy adult teeth is achieved through mineralization of a proteinaceous matrix that changes in abundance and composition. Enamel-specific proteins and proteases are known to be critical for proper enamel formation. Recent proteomics analyses revealed many other proteins with their roles in enamel formation yet to be unraveled. Although the exact protein composition of healthy tooth enamel is still unknown, it is apparent that compromised enamel deviates in amount and composition of its organic material. Why these differences affect both the mineralization process before tooth eruption and the properties of erupted teeth will become apparent as proteomics protocols are adjusted to the variability between species, tooth size, sample size and ephemeral organic content of forming teeth. This review summarizes the current knowledge and published proteomics data of healthy and diseased tooth enamel, including advancements in forensic applications and disease models in animals. A summary and discussion of the status quo highlights how recent proteomics findings advance our understating of the complexity and temporal changes of extracellular matrix composition during tooth enamel formation.

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          The structural biology of the developing dental enamel matrix.

          The biomineralization of the dental enamel matrix with a carbonated hydroxyapatite mineral generates one of the most remarkable examples of a vertebrate mineralized tissue. Recent advances in the molecular biology of ameloblast gene products have now revealed the primary structures of the principal proteins involved in this extracellular mineralizing system, amelogenins, tuftelins, ameloblastins, enamelins, and proteinases, but details of their secondary, tertiary, and quaternary structures, their interactions with other matrix and or cell surface proteins, and their functional role in dental enamel matrix mineralization are still largely unknown. This paper reviews our current knowledge of these molecules, the probable molecular structure of the enamel matrix, and the functional role of these extracellular matrix proteins. Recent studies on the major structural role played by the amelogenin proteins are discussed, and some new data on synthetic amelogenin matrices are reviewed. Copyright 1999 Academic Press.
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            Ancient proteins resolve the evolutionary history of Darwin's South American ungulates.

            No large group of recently extinct placental mammals remains as evolutionarily cryptic as the approximately 280 genera grouped as 'South American native ungulates'. To Charles Darwin, who first collected their remains, they included perhaps the 'strangest animal[s] ever discovered'. Today, much like 180 years ago, it is no clearer whether they had one origin or several, arose before or after the Cretaceous/Palaeogene transition 66.2 million years ago, or are more likely to belong with the elephants and sirenians of superorder Afrotheria than with the euungulates (cattle, horses, and allies) of superorder Laurasiatheria. Morphology-based analyses have proved unconvincing because convergences are pervasive among unrelated ungulate-like placentals. Approaches using ancient DNA have also been unsuccessful, probably because of rapid DNA degradation in semitropical and temperate deposits. Here we apply proteomic analysis to screen bone samples of the Late Quaternary South American native ungulate taxa Toxodon (Notoungulata) and Macrauchenia (Litopterna) for phylogenetically informative protein sequences. For each ungulate, we obtain approximately 90% direct sequence coverage of type I collagen α1- and α2-chains, representing approximately 900 of 1,140 amino-acid residues for each subunit. A phylogeny is estimated from an alignment of these fossil sequences with collagen (I) gene transcripts from available mammalian genomes or mass spectrometrically derived sequence data obtained for this study. The resulting consensus tree agrees well with recent higher-level mammalian phylogenies. Toxodon and Macrauchenia form a monophyletic group whose sister taxon is not Afrotheria or any of its constituent clades as recently claimed, but instead crown Perissodactyla (horses, tapirs, and rhinoceroses). These results are consistent with the origin of at least some South American native ungulates from 'condylarths', a paraphyletic assembly of archaic placentals. With ongoing improvements in instrumentation and analytical procedures, proteomics may produce a revolution in systematics such as that achieved by genomics, but with the possibility of reaching much further back in time.
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              A late Middle Pleistocene Denisovan mandible from the Tibetan Plateau

              Denisovans are members of a hominin group who are currently only known directly from fragmentary fossils, the genomes of which have been studied from a single site, Denisova Cave1-3 in Siberia. They are also known indirectly from their genetic legacy through gene flow into several low-altitude East Asian populations4,5 and high-altitude modern Tibetans6. The lack of morphologically informative Denisovan fossils hinders our ability to connect geographically and temporally dispersed fossil hominins from Asia and to understand in a coherent manner their relation to recent Asian populations. This includes understanding the genetic adaptation of humans to the high-altitude Tibetan Plateau7,8, which was inherited from the Denisovans. Here we report a Denisovan mandible, identified by ancient protein analysis9,10, found on the Tibetan Plateau in Baishiya Karst Cave, Xiahe, Gansu, China. We determine the mandible to be at least 160 thousand years old through U-series dating of an adhering carbonate matrix. The Xiahe specimen provides direct evidence of the Denisovans outside the Altai Mountains and its analysis unique insights into Denisovan mandibular and dental morphology. Our results indicate that archaic hominins occupied the Tibetan Plateau in the Middle Pleistocene epoch and successfully adapted to high-altitude hypoxic environments long before the regional arrival of modern Homo sapiens.
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                Author and article information

                Journal
                Int J Mol Sci
                Int J Mol Sci
                ijms
                International Journal of Molecular Sciences
                MDPI
                1422-0067
                23 June 2020
                June 2020
                : 21
                : 12
                : 4458
                Affiliations
                [1 ]The Forsyth Institute, Cambridge, MA 02142, USA
                [2 ]Department of Developmental Biology, Harvard School of Dental Medicine, Boston, MA 02115, USA
                Author notes
                [* ]Correspondence: agildebona@ 123456forsyth.org (A.G.-B.); fbidlack@ 123456forsyth.org (F.B.B.)
                Article
                ijms-21-04458
                10.3390/ijms21124458
                7352428
                32585904
                6d49823c-0eba-4cfe-a0f4-168322e3a211
                © 2020 by the authors.

                Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license ( http://creativecommons.org/licenses/by/4.0/).

                History
                : 26 May 2020
                : 20 June 2020
                Categories
                Review

                Molecular biology
                tooth enamel,enamel proteome,amelogenin,amelogenin-y (amely),enamel peptide,molar hypomineralization,dental anthropology,dental fluorosis,serum albumin

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