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      Analysis and discussion of trace elements in teeth of different animal species

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          Abstract

          Human, bovine and swine teeth were analyzed by Proton Induced X-ray Emission (PIXE). The aim of this work was to determine the concentration of trace elements in enamel and dentine of different animal species. PIXE analysis was carried out at the Laboratório de Análise de Materiais por Feixes Iônicos da USP (LAMFI) using a 2.4 MeV proton beam to probe the samples. Healthy teeth from São Paulo region were analyzed. Thirteen elements were measured and quantified in the samples: P, S, Cl, K, Ca, Cr, Mn, Fe, Ni, Cu, Zn, Sr and Ba. The measured ratio of Ca:P in dentine and enamel teeth is the same expected for hydroxyapatite: 2.13, for all three types. Trace element concentrations were found to be very similar between the three species, except for S, Cl, Fe, Cu and Sr. Ni and Cu concentrations were found to be close to 1 ppm, which is also close to the detection limits of the SP-PIXE system.

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          A review of protein structure and gene organisation for proteins associated with mineralised tissue and calcium phosphate stabilisation encoded on human chromosome 4.

          Several proteins associated with mineralised tissue (teeth and bone) or involved in calcium phosphate stabilisation in the body fluids, milk and saliva have been mapped to the q arm of human chromosome 4. These include the dentine/bone proteins dentine sialophosphoprotein (DSPP), dentine matrix protein 1 (DMP1), bone sialoprotein (BSP), matrix extracellular phosphoglycoprotein, osteopontin (OPN), enamelin, ameloblastin, milk caseins, salivary statherin, and proline-rich proteins. The proposed function of those that are multiphosphorylated is: (i) the stabilisation of calcium phosphate in solution (e.g. casein, statherin) preventing spontaneous precipitation and seeded-crystal growth or (ii) promoting biomineralisation (e.g. the phosphophoryn domain of DSPP), where the protein described as a template macromolecule, is proposed to act as a nucleator/promoter of crystal growth. The genes of these proteins have been subjected to conserved chromosomal synteny during mammalian evolution. The multiphosphorylated proteins statherin, caseins, phosphophoryn, BSP and OPN have been characterised as intrinsically disordered. The codon usage patterns for the amino acid serine reveal a bias for AGC and AGT codons within the human genes dspp, dmp1 and bsp, mouse dspp and dmp1 but not significantly for statherin or caseins. This pattern was also observed in the gene encoding hen phosvitin that also contains stretches of multiphosphorylated serines and in the dmp1 gene sequences of mammalian, reptilian and avian classes. In conclusion, these intrinsically disordered multiphosphorylated proteins are the translation products of genes displaying examples of codon usage bias, internal repeats and conserved chromosomal synteny within the mammalian class.
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            Influence of an intermittent compressive force on matrix protein expression by ROS 17/2.8 cells, with selective stimulation of osteopontin.

            The purpose of this study was to determine the response of bone cells to physical stress. Intermittent compressive force (ICF) was applied to 13 kPa to subconfluent ROS 17/2.8 cells at 18 cycles/min. After 48 h of this application, the cells were labelled with [35S]-methionine or [32PO4]. Application of ICF over this time did not alter the synthesis of type I collagen, fibronectin or bone SPARC (osteonectin) compared to that of control cells. However, the activity of alkaline phosphatase was increased 1.5-fold, and the synthesis of a 32PO4-labelled, 75-kDa phosphoprotein, recognized as osteopontin by immunoprecipitation with specific antibodies, was increased 1.4-fold. Also, an increase in osteopontin mRNA starting within 12h of ICF application was observed. The selective increase in osteopontin expression associated with ICF may be important in the remodelling of bone tissues during growth and development and in response to functional forces.
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              Arch. Oral Biol.

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                Author and article information

                Contributors
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Role: ND
                Journal
                bjp
                Brazilian Journal of Physics
                Braz. J. Phys.
                Sociedade Brasileira de Física (São Paulo )
                1678-4448
                September 2005
                : 35
                : 3b
                : 761-762
                Affiliations
                [1 ] Universidade de São Paulo Brazil
                [2 ] Universidade de São Paulo Brazil
                Article
                S0103-97332005000500010
                10.1590/S0103-97332005000500010
                6c691e64-29e2-4d63-b406-d51c25071334

                http://creativecommons.org/licenses/by/4.0/

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                SciELO Brazil

                Self URI (journal page): http://www.scielo.br/scielo.php?script=sci_serial&pid=0103-9733&lng=en
                Categories
                PHYSICS, MULTIDISCIPLINARY

                General physics
                General physics

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