ArticleArchives of oral biology2018
Identification of major matrix metalloproteinase-20 proteolytic processing products of murine amelogenin and tyrosine-rich amelogenin peptide using a nuclear magnetic resonance spectroscopy based method.
Article in Archives of oral biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 9 citations in OpenAlex.
- Integrative multi-omics and bioinformatic analysis ofThe Japanese dental science review · 2026Review
- SAXS of murine amelogenin identifies a persistent dimeric species from pH 5.0 to 8.0.Journal of structural biology · 2024Article
- Research progress of biomimetic materials in oral medicine.Journal of biological engineering · 2023Review
- High-yield recombinant bacterial expression ofProtein science : a publication of the Protein Society · 2023Article
- Residue-Specific Insights into the Intermolecular Protein-Protein Interfaces Driving Amelogenin Self-Assembly in Solution.Biochemistry · 2022Article
- Advanced materials for enamel remineralization.Frontiers in bioengineering and biotechnology · 2022Review
- Biomimetic mineralisation systems for in situ enamel restoration inspired by amelogenesis.Journal of materials science. Materials in medicine · 2021Review
- Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.Journal of structural biology · 2020Review
- The energetic basis for hydroxyapatite mineralization by amelogenin variants provides insights into the origin ofProceedings of the National Academy of Sciences of the United States of America · 2019Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
objectiveThe aim of this study was to identify major matrix metalloproteinase-20 (MMP20) proteolytic processing products of amelogenin over time and determine if the tyrosine-rich amelogenin peptide (TRAP) was a substrate of MMP20.
designRecombinant
resultsThe primary product in five out of the six major reverse-phase high-performance liquid chromatography bands generated after a 24 h incubation of murine amelogenin with MMP20 were: S55-L163, P2-L147, P2-E162, P2-A167, and P2-R176. After 72 h these products were replaced with five major reverse-phase high-performance liquid chromatography bands containing: L46-A170, P2-S152, P2-F151, P2-W45, and short N-terminal peptides. TRAP was completely digested by MMP20 into multiple small peptides with the initial primary site of cleavage between S16 and Y17.
conclusionsIdentification of the major MMP20 proteolytic products of amelogenin confirm a dynamic process, with sites towards the C-terminus more rapidly attacked than sites near the N-terminus. This observation is consistent with nanosphere models where the C-terminus is exposed and the N-terminus more protected. One previously reported end-product of the MMP20 proteolytic processing of amelogenin, TRAP, is shown to be an in vitro substrate for MMP20.
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