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Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties
- 1.0536820 - ÚOCHB 2021 RIV CH eng J - Journal Article
Vetýšková, Veronika - Zouharová, Monika - Bednárová, Lucie - Vaněk, O. - Sázelová, Petra - Kašička, Václav - Vymětal, Jiří - Srp, Jaroslav - Rumlová, M. - Charnavets, Tatsiana - Poštulková, Klára - Reseland, J. E. - Boušová, Kristýna - Vondrášek, Jiří
Characterization of AMBN I and II Isoforms and Study of Their Ca2+-Binding Properties.
International Journal of Molecular Sciences. Roč. 21, č. 23 (2020), č. článku 9293. E-ISSN 1422-0067
R&D Projects: GA MŠMT(CZ) EF16_019/0000729; GA MŠMT(CZ) LM2018127
Institutional support: RVO:61388963 ; RVO:86652036
Keywords : ameloblastin * biomineralization * oligomerization * calcium binding * intrinsically disordered protein (IDPs)
OECD category: Biochemistry and molecular biology; Biochemistry and molecular biology (BTO-N)
Impact factor: 5.924, year: 2020
Method of publishing: Open access
https://doi.org/10.3390/ijms21239293
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.
Permanent Link: http://hdl.handle.net/11104/0314572
Number of the records: 1