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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11130%2F20%3A10418465" target="_blank" >RIV/00216208:11130/20:10418465 - isvavai.cz</a>

  • Alternative codes found

    RIV/00216208:11310/20:10418465 RIV/60461373:22330/20:43921042

  • Result on the web

    <a href="https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=tkKx9HaSg6" target="_blank" >https://verso.is.cuni.cz/pub/verso.fpl?fname=obd_publikace_handle&handle=tkKx9HaSg6</a>

  • DOI - Digital Object Identifier

    <a href="http://dx.doi.org/10.3390/ijms21239293" target="_blank" >10.3390/ijms21239293</a>

Alternative languages

  • Result language

    angličtina

  • Original language name

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

  • Original language description

    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.

  • Czech name

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • OECD FORD branch

    10608 - Biochemistry and molecular biology

Result continuities

  • Project

  • Continuities

    I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Others

  • Publication year

    2020

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Data specific for result type

  • Name of the periodical

    International Journal of Molecular Sciences [online]

  • ISSN

    1422-0067

  • e-ISSN

  • Volume of the periodical

    21

  • Issue of the periodical within the volume

    23

  • Country of publishing house

    CH - SWITZERLAND

  • Number of pages

    17

  • Pages from-to

    E9293

  • UT code for WoS article

    000597881700001

  • EID of the result in the Scopus database

    2-s2.0-85097403944