{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,4]],"date-time":"2026-10-04T13:35:02Z","timestamp":1791120902858,"version":"4.1.0"},"reference-count":64,"publisher":"Oxford University Press (OUP)","issue":"5","license":[{"start":{"date-parts":[[2014,11,18]],"date-time":"2014-11-18T00:00:00Z","timestamp":1416268800000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/academic.oup.com\/journals\/pages\/open_access\/funder_policies\/chorus\/standard_publication_model"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2015,5,1]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n               <jats:sec>\n                  <jats:title>\u2003<\/jats:title>\n                  <jats:p>Amelotin (AMTN) is a recently discovered protein that is specifically expressed during the maturation stage of dental enamel formation. It is localized at the interface between the enamel surface and the apical surface of ameloblasts. AMTN knock-out mice have hypomineralized enamel, whereas transgenic mice overexpressing AMTN have a compact but disorganized enamel hydroxyapatite (HA) microstructure, indicating a possible involvement of AMTN in regulating HA mineralization directly. In this study, we demonstrated that recombinant human (rh) AMTN dissolved in a metastable buffer system, based on light scattering measurements, promotes HA precipitation. The mineral precipitates were characterized by scanning and transmission electron microscopy and electron diffraction. Colloidal gold immunolabeling of AMTN in the mineral deposits showed that protein molecules were associated with HA crystals. The binding affinity of rh-AMTN to HA was found to be comparable to that of amelogenin, the major protein of the forming enamel matrix. Overexpression of AMTN in mouse calvaria cells also increased the formation of calcium deposits in the culture medium. Overexpression of AMTN during the secretory stage of enamel formation in vivo resulted in rapid and uncontrolled enamel mineralization. Site-specific mutagenesis of the potential serine phosphorylation motif SSEEL reduced the in vitro mineral precipitation to less than 25%, revealing that this motif is important for the HA mineralizing function of the protein. A synthetic short peptide containing the SSEEL motif was only able to facilitate mineralization in its phosphorylated form (PSPSEEL), indicating that this motif is necessary but not sufficient for the mineralizing properties of AMTN. These findings demonstrate that AMTN has a direct influence on biomineralization by promoting HA mineralization and suggest a critical role for AMTN in the formation of the compact aprismatic enamel surface layer during the maturation stage of amelogenesis. \u00a9 2015 American Society for Bone and Mineral Research.<\/jats:p>\n               <\/jats:sec>","DOI":"10.1002\/jbmr.2411","type":"journal-article","created":{"date-parts":[[2014,11,18]],"date-time":"2014-11-18T22:05:17Z","timestamp":1416348317000},"page":"775-785","source":"Crossref","is-referenced-by-count":90,"title":["The Enamel Protein Amelotin Is a Promoter of Hydroxyapatite Mineralization"],"prefix":"10.1093","volume":"30","author":[{"given":"Nastaran","family":"Abbarin","sequence":"first","affiliation":[{"name":"Matrix Dynamics GroupFaculty of DentistryUniversity of TorontoTorontoCanada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Symone","family":"San Miguel","sequence":"additional","affiliation":[{"name":"Matrix Dynamics GroupFaculty of DentistryUniversity of TorontoTorontoCanada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"James","family":"Holcroft","sequence":"additional","affiliation":[{"name":"Matrix Dynamics GroupFaculty of DentistryUniversity of TorontoTorontoCanada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kengo","family":"Iwasaki","sequence":"additional","affiliation":[{"name":"Department of NanomedicineGraduate School of Medical and Dental SciencesTokyo Medical and Dental UniversityTokyoJapan"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Bernhard","family":"Ganss","sequence":"additional","affiliation":[{"name":"Matrix Dynamics GroupFaculty of DentistryUniversity of TorontoTorontoCanada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2014,11,18]]},"reference":[{"issue":"6","key":"2024020319162591200_jbmr2411-bib-0001","doi-asserted-by":"crossref","first-page":"1996","DOI":"10.2741\/4034","article-title":"Protein-mediated enamel mineralization","volume":"17","author":"Moradian-Oldak","year":"2012","journal-title":"Front Biosci."},{"key":"2024020319162591200_jbmr2411-bib-0002","volume-title":"Ten Cate's oral histology: development, structure, and function","author":"Nanci","year":"2008","edition":"7th ed"},{"issue":"1","key":"2024020319162591200_jbmr2411-bib-0003","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1159\/000102683","article-title":"Enamel formation and amelogenesis imperfecta","volume":"186","author":"Hu","year":"2007","journal-title":"Cells Tissues Organs 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