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Characterization of AMBN I and II Isoforms and Study of Their Ca(2+)-Binding Properties

Publikace na Přírodovědecká fakulta, 1. lékařská fakulta, Fakulta tělesné výchovy a sportu, Ústřední knihovna |
2020

Tento text není v aktuálním jazyce dostupný. Zobrazuje se verze "en".Abstrakt

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 (Ca(2+))-binding properties of AMBN ISO I and ISO II.

The binding properties of AMBN to Ca(2+) may explain the role of AMBN in biomineralization and more generally in Ca(2+) homeostasis processes.