ArticleFrontiers in physiology2014
Analysis of co-assembly and co-localization of ameloblastin and amelogenin.
Article in Frontiers in physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 27 citations in OpenAlex.
- Amelogenin Phosphorylation Affects Protein-Protein Interactions In Vivo.Calcified tissue international · 2026Article
- Ameloblastin and its multifunctionality in amelogenesis: A review.Matrix biology : journal of the International Society for Matrix Biology · 2024Review
- Article
- The Dynamic Interactions of a Multitargeting Domain in Ameloblastin Protein with Amelogenin and Membrane.International journal of molecular sciences · 2023Article
- The phosphorylation of serineMatrix biology : journal of the International Society for Matrix Biology · 2022Article
- Biomineralization of Enamel and Dentin Mediated by Matrix Proteins.Journal of dental research · 2021Review
- Characterization of AMBN I and II Isoforms and Study of Their CaInternational journal of molecular sciences · 2020Article
- An Evolutionarily Conserved Helix Mediates Ameloblastin-Cell Interaction.Journal of dental research · 2020Article
- Amelogenin phosphorylation regulates tooth enamel formation by stabilizing a transient amorphous mineral precursor.The Journal of biological chemistry · 2020Article
- Co-Immunoprecipitation Reveals Interactions Between Amelogenin and AmeloblastinFrontiers in physiology · 2020Article
- Characterization of protein extracts from different types of human teeth and insight in biomineralization.Scientific reports · 2019Article
- Ameloblastin Binds to Phospholipid Bilayers via a Helix-Forming Motif within the Sequence Encoded by Exon 5.ACS omega · 2019Article
- Immunohistochemical Co-Localization of Amelogenin and Ameloblastin in Developing Enamel Matrix.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Intrinsically disordered proteins drive enamel formation via an evolutionarily conserved self-assembly motif.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Ameloblastin peptide encoded by exon 5 interacts with amelogenin N-terminus.Biochemistry and biophysics reports · 2016Article
- Amelogenin-Ameloblastin Spatial Interaction around Maturing Enamel Rods.Journal of dental research · 2016Article
- Helium ion microscopy of enamel crystallites and extracellular tooth enamel matrix.Frontiers in physiology · 2014Article
- Intrinsically disordered proteins and biomineralization.Matrix biology : journal of the International Society for Matrix BiologyReview
- Amelogenin and Enamel Biomimetics.Journal of materials chemistry. BArticle
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Epithelially-derived ameloblasts secrete extracellular matrix proteins including amelogenin, enamelin, and ameloblastin. Complex intermolecular interactions among these proteins are believed to be important in controlling enamel formation. Here we provide in vitro and in vivo evidence of co-assembly and co-localization of ameloblastin with amelogenin using both biophysical and immunohistochemical methods. We performed co-localization studies using immunofluorescence confocal microscopy with paraffin-embedded tissue sections from mandibular molars of mice at 1, 5, and 8 days of age. Commercially-available ameloblastin antibody (M300) against mouse ameloblastin residues 107-407 and an antibody against full-length recombinant mouse (rM179) amelogenin were used. Ameloblastin-M300 clearly reacted along the secretory face of ameloblasts from days 1-8. Quantitative co-localization was analyzed (QCA) in several configurations by choosing appropriate regions of interest (ROIs). Analysis of ROIs along the secretory face of ameloblasts revealed that at day 1, very high percentages of both the ameloblastin and amelogenin co-localized. At day 8 along the ameloblast cells the percentage of co-localization remained high for the ameloblastin whereas co-localization percentage was reduced for amelogenin. Analysis of the entire thickness on day 8 revealed no significant co-localization of amelogenin and ameloblastin. With the progress of amelogenesis and ameloblastin degradation, there was a segregation of ameloblastin and co-localization with the C-terminal region decreased. CD spectra indicated that structural changes in ameloblastin occurred upon addition of amelogenin. Our data suggest that amelogenin-ameloblastin complexes may be the functional entities at the early stage of enamel mineralization.
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