Exon4 amelogenin transcripts in enamel biomineralization.
Amelogenins are proteins formed by alternative splicing of the amelogenin gene, and are essential for tooth enamel formation. However, the unique functions of various alternatively spliced amelogenins in enamel formation are not well understood. In this study, we determined the spatiotemporal locati...
| Publicado en: | Journal of Dental Research Vol. 94; no. 6; pp. 836 - 843 |
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| Autores principales: | , , , , , , , , |
| Formato: | research Journal Article |
| Publicado: |
Sage Publications Inc.
Jun2015
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| Acceso en línea: | Ver este registro en EBSCOhost |
| fields | @attributes: recordID: 1 pdfLink: plink: https://search.ebscohost.com/login.aspx?direct=true&db=ccm&AN=109787820&site=ehost-live header: @attributes: shortDbName: ccm uiTerm: 109787820 longDbName: CINAHL Complete uiTag: AN controlInfo: bkinfo: dissinfo: jinfo: jid: 00220345 1H7 jtl: Journal of Dental Research issn: 00220345 maglogo: Y pubinfo: dt: Jun2015 vid: 94 iid: 6 pid: 344 pub: Sage Publications Inc. place: Thousand Oaks, California artinfo: ui: 109787820 NLM25792521 2013019353 10.1177/0022034515577412 NLM25792521 PMC4485327 109787820 ppf: 836 ppct: 7 formats: tig: atl: Exon4 amelogenin transcripts in enamel biomineralization. aug: au: Stahl, J Nakano, Y Horst, J Zhu, L Le, M Zhang, Y Liu, H Li, W Den Besten, P K sug: subj: Dental Enamel Dentition Physiology Genes Animal Studies Biochemical Phenomena Calcium Metabolism Cell Differentiation Physiology Epithelial Cells Physiology Female Fetal Development Mass Spectrometry Mice Minerals Metabolism Phosphates Metabolism Proteins Rats Recombinant Proteins RNA Time Factors Female ab: Amelogenins are proteins formed by alternative splicing of the amelogenin gene, and are essential for tooth enamel formation. However, the unique functions of various alternatively spliced amelogenins in enamel formation are not well understood. In this study, we determined the spatiotemporal location of amelogenins derived from transcripts containing exon4 (AMG+4) in the enamel matrix, and the relative binding of recombinant AMG+4 to hydroxyapatite (HAP). Immunohistochemistry and mass spectrometry analyses showed that AMG+4 proteins were secreted into the enamel matrix at the early maturation stage. A stage-specific increase in the synthesis of AMG+4 was further supported by our observation that in mice overexpressing leucine-rich amelogenin peptide (TgLRAP), in which ameloblasts differentiate earlier, AMG+4 transcripts were also upregulated earlier. In vitro binding studies, supported by in silico modeling of protein binding to calcium and phosphate, showed that more recombinant AMG+4 bound to hydroxyapatite (HAP) as compared with recombinant AMG-4. The temporal and spatial localization of amelogenins containing exon4 peptide, and their functional differences in HAP binding, suggests that the unique properties of amelogenins containing exon4 cause a specific enhancement of biomineralization related to stabilization of early-formed HAP at the maturation stage. pubtype: Academic Journal doctype: research Journal Article ougenre: Article language: English refInfo: holdings: @attributes: islocal: N |
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