Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F13%3A10191606" target="_blank" >RIV/00216208:11310/13:10191606 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/86652036:_____/13:00396044 RIV/67985823:_____/13:00396044 RIV/61388971:_____/13:00396044 RIV/61388963:_____/13:00396044 RIV/44555601:13440/13:43885015

Výsledek na webu

<a href="http://dx.doi.org/10.1074/jbc.M113.456012" target="_blank" >http://dx.doi.org/10.1074/jbc.M113.456012</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1074/jbc.M113.456012" target="_blank" >10.1074/jbc.M113.456012</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5

Popis výsledku v původním jazyce

Tooth enamel, the hardest tissue in the body, is formed by the evolutionarily highly conserved biomineralization process that is controlled by extracellular matrix proteins. The intrinsically disordered matrix protein ameloblastin (AMBN) is the most abundant nonamelogenin protein of the developing enamel and a key element for correct enamel formation. AMBN was suggested to be a cell adhesion molecule that regulates proliferation and differentiation of ameloblasts. Nevertheless, detailed structural and functional studies on AMBN have been substantially limited by the paucity of the purified non-degraded protein. Here we developed a procedure for production of a highly purified form of recombinant human AMBN in quantities that allowed its structural characterization. Using size-exclusion chromatography, analytical ultracentrifugation, transmission electron and atomic-force microscopy techniques, we show that AMBN self-associates into ribbon-like supramolecular structures with an average

Název v anglickém jazyce

Intrinsically disordered enamel matrix protein ameloblastin forms ribbon-like supramolecular structures via an N-terminal segment encoded by exon 5

Popis výsledku anglicky

Tooth enamel, the hardest tissue in the body, is formed by the evolutionarily highly conserved biomineralization process that is controlled by extracellular matrix proteins. The intrinsically disordered matrix protein ameloblastin (AMBN) is the most abundant nonamelogenin protein of the developing enamel and a key element for correct enamel formation. AMBN was suggested to be a cell adhesion molecule that regulates proliferation and differentiation of ameloblasts. Nevertheless, detailed structural and functional studies on AMBN have been substantially limited by the paucity of the purified non-degraded protein. Here we developed a procedure for production of a highly purified form of recombinant human AMBN in quantities that allowed its structural characterization. Using size-exclusion chromatography, analytical ultracentrifugation, transmission electron and atomic-force microscopy techniques, we show that AMBN self-associates into ribbon-like supramolecular structures with an average

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CE - Biochemie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2013

Kód důvěrnosti údajů

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

Název periodika

Journal of Biological Chemistry

ISSN

0021-9258

e-ISSN

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Svazek periodika

288

Číslo periodika v rámci svazku

31

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

13

Strana od-do

22333-22345

Kód UT WoS článku

000330596300015

EID výsledku v databázi Scopus

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