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.
- MeSH
- adsorpce MeSH
- kvarterní struktura proteinů MeSH
- lidé MeSH
- molekulární modely MeSH
- mukoproteiny chemie MeSH
- multimerizace proteinu * MeSH
- nádorové proteiny chemie MeSH
- onkogenní proteiny chemie MeSH
- proteinové domény MeSH
- transportní proteiny chemie MeSH
- Check Tag
- lidé MeSH
- Publikační typ
- časopisecké články MeSH
- Klíčová slova
- Brdičkova reakce základní a filtrátová, Folinovo fenolové činidlo,
- MeSH
- autolýza * diagnóza enzymologie MeSH
- biomedicínský výzkum MeSH
- dusík chemie izolace a purifikace krev MeSH
- experimenty na zvířatech MeSH
- játra * anatomie a histologie enzymologie sekrece MeSH
- mukoproteiny chemie izolace a purifikace krev MeSH
- polarografie metody využití MeSH
- prasata krev metabolismus MeSH
- sérum enzymologie MeSH
- statistika jako téma MeSH
- tkáně * enzymologie chemie MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
