Effects of Metal Ions on the Activity of Protein Tyrosine Phosphatase VHR: Highly Potent and Reversible Oxidative Inactivation by Cu2+ Ion

Cited 114 time in scopus
Metadata Downloads

Full metadata record

DC FieldValueLanguage
dc.contributor.authorJin Hahn Kim-
dc.contributor.authorHyeong Jin Cho-
dc.contributor.authorSeong Eon Ryu-
dc.contributor.authorMyung Un Choi-
dc.date.accessioned2017-04-19T08:57:37Z-
dc.date.available2017-04-19T08:57:37Z-
dc.date.issued2000-
dc.identifier.issn00969621-
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/5319-
dc.description.abstractThe posttranslational regulation of protein tyrosine phosphatases (PTPs) has been suggested to have a crucial role in maintaining the phosphotyrosine level in cells. Here we examined the regulatory effects of metal ions on human dual-specificity vaccinia H1-related protein tyrosine phosphatase (VHR) in vitro. Among various metal ions examined, Fe3+, Cu2+, Zn2+, and Cd2+ exerted their inactivational effects on VHR, and Cu2+ is the most potent inactivator. The VHR activity inactivated by the metal ions except Cu2+ was significantly restored by EDTA. The efficacy of Cu2+ for the VHR inactivation was about 200-fold more potent than that of H2O2. Cu2+ also inactivated other PTPs including PTPIB and SHP-1. The Cu2+-mediated inactivation at the submicromolar range was eradicated by dithiothreitol treatment. The loss of VHR activity correlated with the decreased [14C]iodoacetate labeling of active-site cysteine, suggesting that Cu2+ brought about the oxidation of the active-site cysteine. On the contrary, Zn2+ that exerted an inactivational effect at millimolar concentrations appeared not directly linked to the active-site cysteine, as indicated by the fact that [14C]iodoacetate labeling was unaffected and that the effect of Zn2+ on the Y78F mutant was increased. The reduction potential of VHR was estimated to be -331 mV by utilizing the reversibility of the redox state of VHR. Thus, we conclude that the highly potent Cu2+ inactivation of VHR is a consequence of the oxidation of the active-site cysteine and the mode of Zn2+ inactivation is distinct from that of Cu2+.-
dc.publisherElsevier-
dc.titleEffects of Metal Ions on the Activity of Protein Tyrosine Phosphatase VHR: Highly Potent and Reversible Oxidative Inactivation by Cu2+ Ion-
dc.title.alternativeEffects of Metal Ions on the Activity of Protein Tyrosine Phosphatase VHR: Highly Potent and Reversible Oxidative Inactivation by Cu2+ Ion-
dc.typeArticle-
dc.citation.titleArchives of Biochemistry and Biophysics-
dc.citation.number1-
dc.citation.endPage80-
dc.citation.startPage72-
dc.citation.volume382-
dc.contributor.alternativeName김진한-
dc.contributor.alternativeName조형진-
dc.contributor.alternativeName류성언-
dc.contributor.alternativeName최명운-
dc.identifier.bibliographicCitationArchives of Biochemistry and Biophysics, vol. 382, no. 1, pp. 72-80-
dc.identifier.doi10.1006/abbi.2000.1996-
dc.subject.keywordCopper ion-
dc.subject.keywordMetal ions-
dc.subject.keywordOxidative inactivation-
dc.subject.keywordProtein tyrosine phosphatase-
dc.subject.keywordVHR-
dc.subject.localCopper ion-
dc.subject.localMetal ions-
dc.subject.localOxidative inactivation-
dc.subject.localProtein tyrosine phosphatase-
dc.subject.localVHR-
dc.description.journalClassY-
Appears in Collections:
1. Journal Articles > Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.