Prion protein and its interactions with metal ions (Cu2+, Zn2+, and Cd2+) and metallothionein 3

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dc.contributor.authorRuttkay-Nedecký, Branislavcs
dc.contributor.authorSedláčková, Eliškacs
dc.contributor.authorHegerová, Dagmarcs
dc.contributor.authorČíhalová, Kristýnacs
dc.contributor.authorJimenez Jimenez, Ana Mariacs
dc.contributor.authorKřížková, Soňacs
dc.contributor.authorRichtera, Lukášcs
dc.contributor.authorAdam, Vojtěchcs
dc.contributor.authorKizek, Renécs
dc.coverage.issue3cs
dc.coverage.volume3cs
dc.date.accessioned2021-08-18T14:54:58Z
dc.date.available2021-08-18T14:54:58Z
dc.date.issued2015-12-01cs
dc.description.abstractThe effects of heavy metals (Zn2+, Cu2+, and/or Cd2+) on Escherichia coli expressing either prion (hPrP(C)) or metallothionein 3 (MT-3) brain proteins capable of binding these metals were investigated. The expression of hPrPC or MT-3 in E. coli was confirmed using western-blot and dot-blot methods. After analyzing growth curves, we found that bacteria expressing prion protein better tolerated the presence of Zn2+ in comparison with wild-type bacteria and bacteria expressing MT-3. The addition of Cd2+ and Cu2+ was well tolerated by bacteria expressing MT-3, whereas the bacteria expressing prion protein displayed slower growth when compared to the wild-type. We subsequently determined total content of the MT in bacteria using differential pulsed voltammetry (DPV), and depending on the treatment of the individual metals. MT expression in MT3 transformed cells as well as in control E. coli cells increased at the lowest metal concentration (25 mu M), followed by a decrease at higher metal concentrations (50, 75, and 150 mu M). The highest increase by Cd2+ were observed. MT expression pattern in hPrP(C) transformed cells was different. After application of Cu2+ an increase in MT expression continued also at higher metal concentrations; and after application of Cd2+ and Zn2+ no decrease in MT expression at higher metal concentrations was observed.en
dc.formattextcs
dc.format.extent287-295cs
dc.format.mimetypeapplication/pdfcs
dc.identifier.citationADMET & DMPK. 2015, vol. 3, issue 3, p. 287-295.en
dc.identifier.doi10.5599/admet.3.3.191cs
dc.identifier.issn1848-7718cs
dc.identifier.other163358cs
dc.identifier.urihttp://hdl.handle.net/11012/201035
dc.language.isoencs
dc.publisherInternational Association of Physical Chemistscs
dc.relation.ispartofADMET & DMPKcs
dc.relation.urihttp://www.pub.iapchem.org/ojs/index.php/admet/article/view/191/pdfcs
dc.rightsCreative Commons Attribution 4.0 Internationalcs
dc.rights.accessopenAccesscs
dc.rights.sherpahttp://www.sherpa.ac.uk/romeo/issn/1848-7718/cs
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/cs
dc.subjectprion diseasesen
dc.subjectPrPCen
dc.subjectPrPScen
dc.subjectMTen
dc.subjectMT-3en
dc.subjectcopperen
dc.subjectzincen
dc.subjectcadmiumen
dc.titlePrion protein and its interactions with metal ions (Cu2+, Zn2+, and Cd2+) and metallothionein 3en
dc.type.driverarticleen
dc.type.statusPeer-revieweden
dc.type.versionpublishedVersionen
sync.item.dbidVAV-163358en
sync.item.dbtypeVAVen
sync.item.insts2021.08.18 16:54:58en
sync.item.modts2021.08.18 16:14:21en
thesis.grantorVysoké učení technické v Brně. Středoevropský technologický institut VUT. Chytré nanonástrojecs
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