Ameloblastin (Ambn) as an intrinsically disordered protein (IDP) stands for an important role in the formation of enamel-the hardest biomineralized tissue commonly formed in vertebrates. The human ameloblastin (AMBN) is expressed in two isoforms: full-length isoform I (AMBN ISO I) and isoform II (AMBN ISO II), which is about 15 amino acid residues shorter than AMBN ISO I. The significant feature of AMBN-its oligomerization ability-is enabled due to a specific sequence encoded by exon 5 present at the N-terminal part in both known isoforms. In this study, we characterized AMBN ISO I and AMBN ISO II by biochemical and biophysical methods to determine their common features and differences. We confirmed that both AMBN ISO I and AMBN ISO II form oligomers in in vitro conditions. Due to an important role of AMBN in biomineralization, we further addressed the calcium (Ca2+)-binding properties of AMBN ISO I and ISO II. The binding properties of AMBN to Ca2+ may explain the role of AMBN in biomineralization and more generally in Ca2+ homeostasis processes.

• Klíčová slova
• ameloblastin, biomineralization, calcium binding, intrinsically disordered protein (IDPs), oligomerization,
• MeSH
• biologické modely MeSH
• hydrodynamika MeSH
• lidé MeSH
• multimerizace proteinu MeSH
• protein - isoformy MeSH
• proteiny vázající vápník chemie   metabolismus   MeSH
• proteiny zubní skloviny chemie   metabolismus   MeSH
• spektrální analýza MeSH
• teplota MeSH
• vápník metabolismus   MeSH
• vazba proteinů MeSH
• vnitřně neuspořádané proteiny metabolismus   MeSH
• Check Tag
• lidé MeSH
• Publikační typ
• časopisecké články MeSH
• Názvy látek
• AMBN protein, human MeSH Prohlížeč
• protein - isoformy MeSH
• proteiny vázající vápník MeSH
• proteiny zubní skloviny MeSH
• vápník MeSH
• vnitřně neuspořádané proteiny MeSH