Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties.

International journal of molecular sciences 2020 Dec 05

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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.

Citation

Veronika Vetyskova, Monika Zouharova, Lucie Bednarova, Ondřej Vaněk, Petra Sázelová, Václav Kašička, Jiri Vymetal, Jaroslav Srp, Michaela Rumlová, Tatsiana Charnavets, Klara Postulkova, Janne E Reseland, Kristyna Bousova, Jiri Vondrasek. Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties. International journal of molecular sciences. 2020 Dec 05;21(23)