Surface Integrity Governs the Proteome of Hypomineralized Enamel
Growing interest in the treatment and prevention of Molar/Incisor Hypomineralization (MIH) warrants investigation into the protein composition of hypomineralized enamel. Hypothesizing abnormality akin to amelogenesis imperfecta, we profiled proteins in hypomineralized enamel from human permanent fir...
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| Veröffentlicht in: | Journal of dental research 2010-10, Vol.89 (10), p.1160-1165 |
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| creator | Mangum, J.E. Crombie, F.A. Kilpatrick, N. Manton, D.J. Hubbard, M.J. |
| description | Growing interest in the treatment and prevention of Molar/Incisor Hypomineralization (MIH) warrants investigation into the protein composition of hypomineralized enamel. Hypothesizing abnormality akin to amelogenesis imperfecta, we profiled proteins in hypomineralized enamel from human permanent first molars using a biochemical approach. Hypomineralized enamel was found to have from 3- to 15-fold higher protein content than normal, but a near-normal level of residual amelogenins. This distinguished MIH from hypomaturation defects with high residual amelogenins (amelogenesis imperfecta, fluorosis) and so typified it as a hypocalcification defect. Second, hypomineralized enamel was found to have accumulated various proteins from oral fluid and blood, with differential incorporation depending on integrity of the enamel surface. Pathogenically, these results point to a pre-eruptive disturbance of mineralization involving albumin and, in cases with post-eruptive breakdown, subsequent protein adsorption on the exposed hydroxyapatite matrix. These insights into the pathogenesis and properties of hypomineralized enamel hold significance for prevention and treatment of MIH. |
| doi_str_mv | 10.1177/0022034510375824 |
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Hypothesizing abnormality akin to amelogenesis imperfecta, we profiled proteins in hypomineralized enamel from human permanent first molars using a biochemical approach. Hypomineralized enamel was found to have from 3- to 15-fold higher protein content than normal, but a near-normal level of residual amelogenins. This distinguished MIH from hypomaturation defects with high residual amelogenins (amelogenesis imperfecta, fluorosis) and so typified it as a hypocalcification defect. Second, hypomineralized enamel was found to have accumulated various proteins from oral fluid and blood, with differential incorporation depending on integrity of the enamel surface. Pathogenically, these results point to a pre-eruptive disturbance of mineralization involving albumin and, in cases with post-eruptive breakdown, subsequent protein adsorption on the exposed hydroxyapatite matrix. These insights into the pathogenesis and properties of hypomineralized enamel hold significance for prevention and treatment of MIH.</description><identifier>ISSN: 0022-0345</identifier><identifier>EISSN: 1544-0591</identifier><identifier>DOI: 10.1177/0022034510375824</identifier><identifier>PMID: 20651090</identifier><identifier>CODEN: JDREAF</identifier><language>eng</language><publisher>Los Angeles, CA: SAGE Publications</publisher><subject>Adsorption ; Amelogenin - analysis ; Animals ; Biological and medical sciences ; Blood Proteins - analysis ; Child ; Complement C3 - analysis ; Dental Enamel - chemistry ; Dental Enamel - pathology ; Dental Enamel Hypoplasia - metabolism ; Dental Enamel Hypoplasia - pathology ; Dental Enamel Proteins - analysis ; Durapatite - analysis ; Durapatite - metabolism ; Facial bones, jaws, teeth, parodontium: diseases, semeiology ; Hemoglobins - analysis ; Hemoglobins - pharmacokinetics ; Humans ; Medical sciences ; Molar - chemistry ; Molar - pathology ; Non tumoral diseases ; Otorhinolaryngology. 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Hypothesizing abnormality akin to amelogenesis imperfecta, we profiled proteins in hypomineralized enamel from human permanent first molars using a biochemical approach. Hypomineralized enamel was found to have from 3- to 15-fold higher protein content than normal, but a near-normal level of residual amelogenins. This distinguished MIH from hypomaturation defects with high residual amelogenins (amelogenesis imperfecta, fluorosis) and so typified it as a hypocalcification defect. Second, hypomineralized enamel was found to have accumulated various proteins from oral fluid and blood, with differential incorporation depending on integrity of the enamel surface. Pathogenically, these results point to a pre-eruptive disturbance of mineralization involving albumin and, in cases with post-eruptive breakdown, subsequent protein adsorption on the exposed hydroxyapatite matrix. These insights into the pathogenesis and properties of hypomineralized enamel hold significance for prevention and treatment of MIH.</description><subject>Adsorption</subject><subject>Amelogenin - analysis</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Blood Proteins - analysis</subject><subject>Child</subject><subject>Complement C3 - analysis</subject><subject>Dental Enamel - chemistry</subject><subject>Dental Enamel - pathology</subject><subject>Dental Enamel Hypoplasia - metabolism</subject><subject>Dental Enamel Hypoplasia - pathology</subject><subject>Dental Enamel Proteins - analysis</subject><subject>Durapatite - analysis</subject><subject>Durapatite - metabolism</subject><subject>Facial bones, jaws, teeth, parodontium: diseases, semeiology</subject><subject>Hemoglobins - analysis</subject><subject>Hemoglobins - pharmacokinetics</subject><subject>Humans</subject><subject>Medical sciences</subject><subject>Molar - chemistry</subject><subject>Molar - pathology</subject><subject>Non tumoral diseases</subject><subject>Otorhinolaryngology. Stomatology</subject><subject>Peptide Fragments - analysis</subject><subject>Proteome - analysis</subject><subject>Rats</subject><subject>Rats, Sprague-Dawley</subject><subject>Salivary Proteins and Peptides - analysis</subject><subject>Serum Albumin - analysis</subject><subject>Serum Albumin - pharmacokinetics</subject><subject>Tooth Calcification</subject><issn>0022-0345</issn><issn>1544-0591</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kM1LAzEUxIMotlbvnmQRPK7mJfuR3JRS20JBQT0vSfalbtmPmuwK9a93S6sFwdM7zG9mHkPIJdBbgDS9o5QxyqMYKE9jwaIjMoQ4ikIaSzgmw60cbvUBOfN-RSlIJvgpGTCa9B5Jh-T-pXNWGQzmdYtLV7SbYNp8oqt90L5j8OyaFpsKg8YGs826qYoanSqLL8yDSa0qLM_JiVWlx4v9HZG3x8nreBYunqbz8cMiNJEUbWipFtoYKYxQGnQuE5AGtEEEVEykPJVAU0tZhErlKtYWhVXWJFozyRXnI3K9y1275qND32arpnN1X5kJiEFyIWkP0R1kXOO9Q5utXVEpt8mAZtvFsr-L9ZarfW6nK8x_DT8T9cDNHlDeqNI6VZvCHzjOEwZC9Fy447xa4uG5f4u_AXrxf_Y</recordid><startdate>20101001</startdate><enddate>20101001</enddate><creator>Mangum, J.E.</creator><creator>Crombie, F.A.</creator><creator>Kilpatrick, N.</creator><creator>Manton, D.J.</creator><creator>Hubbard, M.J.</creator><general>SAGE Publications</general><general>International Association for Dental Research</general><general>SAGE PUBLICATIONS, INC</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7RQ</scope><scope>7RV</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB0</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>NAPCQ</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>S0X</scope><scope>U9A</scope></search><sort><creationdate>20101001</creationdate><title>Surface Integrity Governs the Proteome of Hypomineralized Enamel</title><author>Mangum, J.E. ; Crombie, F.A. ; Kilpatrick, N. ; Manton, D.J. ; Hubbard, M.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c498t-f0b8bcc98c8ab1bd9619c1bcee1ea287379107f024eaada5bfe8fafc6bb293a33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Adsorption</topic><topic>Amelogenin - analysis</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Blood Proteins - analysis</topic><topic>Child</topic><topic>Complement C3 - analysis</topic><topic>Dental Enamel - chemistry</topic><topic>Dental Enamel - pathology</topic><topic>Dental Enamel Hypoplasia - metabolism</topic><topic>Dental Enamel Hypoplasia - pathology</topic><topic>Dental Enamel Proteins - analysis</topic><topic>Durapatite - analysis</topic><topic>Durapatite - metabolism</topic><topic>Facial bones, jaws, teeth, parodontium: diseases, semeiology</topic><topic>Hemoglobins - analysis</topic><topic>Hemoglobins - pharmacokinetics</topic><topic>Humans</topic><topic>Medical sciences</topic><topic>Molar - chemistry</topic><topic>Molar - pathology</topic><topic>Non tumoral diseases</topic><topic>Otorhinolaryngology. 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Hypothesizing abnormality akin to amelogenesis imperfecta, we profiled proteins in hypomineralized enamel from human permanent first molars using a biochemical approach. Hypomineralized enamel was found to have from 3- to 15-fold higher protein content than normal, but a near-normal level of residual amelogenins. This distinguished MIH from hypomaturation defects with high residual amelogenins (amelogenesis imperfecta, fluorosis) and so typified it as a hypocalcification defect. Second, hypomineralized enamel was found to have accumulated various proteins from oral fluid and blood, with differential incorporation depending on integrity of the enamel surface. Pathogenically, these results point to a pre-eruptive disturbance of mineralization involving albumin and, in cases with post-eruptive breakdown, subsequent protein adsorption on the exposed hydroxyapatite matrix. These insights into the pathogenesis and properties of hypomineralized enamel hold significance for prevention and treatment of MIH.</abstract><cop>Los Angeles, CA</cop><pub>SAGE Publications</pub><pmid>20651090</pmid><doi>10.1177/0022034510375824</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adsorption Amelogenin - analysis Animals Biological and medical sciences Blood Proteins - analysis Child Complement C3 - analysis Dental Enamel - chemistry Dental Enamel - pathology Dental Enamel Hypoplasia - metabolism Dental Enamel Hypoplasia - pathology Dental Enamel Proteins - analysis Durapatite - analysis Durapatite - metabolism Facial bones, jaws, teeth, parodontium: diseases, semeiology Hemoglobins - analysis Hemoglobins - pharmacokinetics Humans Medical sciences Molar - chemistry Molar - pathology Non tumoral diseases Otorhinolaryngology. Stomatology Peptide Fragments - analysis Proteome - analysis Rats Rats, Sprague-Dawley Salivary Proteins and Peptides - analysis Serum Albumin - analysis Serum Albumin - pharmacokinetics Tooth Calcification |
| title | Surface Integrity Governs the Proteome of Hypomineralized Enamel |
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