AGR2-AGR3 hetero-oligomeric complexes: Identification and characterization

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F21%3A00078576" target="_blank" >RIV/00209805:_____/21:00078576 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/68081707:_____/21:00544110

Výsledek na webu

<a href="https://www.sciencedirect.com/science/article/abs/pii/S1567539421000712" target="_blank" >https://www.sciencedirect.com/science/article/abs/pii/S1567539421000712</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.bioelechem.2021.107808" target="_blank" >10.1016/j.bioelechem.2021.107808</a>

Jazyk výsledku

angličtina

Název v původním jazyce

AGR2-AGR3 hetero-oligomeric complexes: Identification and characterization

Popis výsledku v původním jazyce

In this paper we compare electrochemical behavior of two homolog proteins, namely anterior gradient 2 (AGR2) and anterior gradient 3 (AGR3), playing an important role in cancer cell biology. The slight variation in their protein structures has an impact on protein adsorption and orientation at charged surface and also enables AGR2 and AGR3 to form heterocomplexes. We confirm interaction between AGR2 and AGR3 (i) in vitro by immunochemical and constant current chronopotentiometric stripping (CPS) analysis and (ii) in vivo by bioluminescence resonance energy transfer (BRET) assay. Mutation of AGR2 in dimerization domain (E60A) prevents development of wild type AGR2 dimers and also negatively affects interaction with wild type AGR3 as shown by CPS analysis. Beside new information about AGR2 and AGR3 protein including their joint interaction, our work introduces possible applications of CPS in bioanalysis of protein complexes, including those relatively unstable, but important in the cancer research.

Název v anglickém jazyce

AGR2-AGR3 hetero-oligomeric complexes: Identification and characterization

Popis výsledku anglicky

In this paper we compare electrochemical behavior of two homolog proteins, namely anterior gradient 2 (AGR2) and anterior gradient 3 (AGR3), playing an important role in cancer cell biology. The slight variation in their protein structures has an impact on protein adsorption and orientation at charged surface and also enables AGR2 and AGR3 to form heterocomplexes. We confirm interaction between AGR2 and AGR3 (i) in vitro by immunochemical and constant current chronopotentiometric stripping (CPS) analysis and (ii) in vivo by bioluminescence resonance energy transfer (BRET) assay. Mutation of AGR2 in dimerization domain (E60A) prevents development of wild type AGR2 dimers and also negatively affects interaction with wild type AGR3 as shown by CPS analysis. Beside new information about AGR2 and AGR3 protein including their joint interaction, our work introduces possible applications of CPS in bioanalysis of protein complexes, including those relatively unstable, but important in the cancer research.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

Projekt

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

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2021

Kód důvěrnosti údajů

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

Název periodika

Bioelectrochemistry

ISSN

1567-5394

e-ISSN

—

Svazek periodika

140

Číslo periodika v rámci svazku

August 2021

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

107808

Kód UT WoS článku

000663599500012

EID výsledku v databázi Scopus

2-s2.0-85103759317