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

Kód výsledku v 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>

Nalezeny alternativní kódy

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

Výsledek na webu

<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>

Jazyk výsledku

angličtina

Název v původním jazyce

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

Popis výsledku v původním jazyce

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.

Název v anglickém jazyce

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

Popis výsledku anglicky

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.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

—

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2020

Kód důvěrnosti údajů

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

Název periodika

International Journal of Molecular Sciences [online]

ISSN

1422-0067

e-ISSN

—

Svazek periodika

21

Číslo periodika v rámci svazku

23

Stát vydavatele periodika

CH - Švýcarská konfederace

Počet stran výsledku

17

Strana od-do

E9293

Kód UT WoS článku

000597881700001

EID výsledku v databázi Scopus

2-s2.0-85097403944