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

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F20%3A00536820" target="_blank" >RIV/61388963:_____/20:00536820 - isvavai.cz</a>

  • Alternative codes found

    RIV/86652036:_____/20:00536820 RIV/00216208:11130/20:10418465 RIV/00216208:11310/20:10418465 RIV/60461373:22330/20:43921042

  • Result on the web

    <a href="https://doi.org/10.3390/ijms21239293" target="_blank" >https://doi.org/10.3390/ijms21239293</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 Ca2+-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 (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.

  • 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

    Result was created during the realization of more than one project. More information in the Projects tab.

  • 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

  • ISSN

    1422-0067

  • e-ISSN

    1422-0067

  • 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

    9293

  • UT code for WoS article

    000597881700001

  • EID of the result in the Scopus database

    2-s2.0-85097403944