Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 이공주 | * |
dc.contributor.author | 강상원 | * |
dc.date.accessioned | 2016-08-28T12:08:37Z | - |
dc.date.available | 2016-08-28T12:08:37Z | - |
dc.date.issued | 2009 | * |
dc.identifier.issn | 1932-6203 | * |
dc.identifier.other | OAK-6138 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/220413 | - |
dc.description.abstract | Nucleoside diphosphate kinase (NDPK, Nm23), a housekeeping enzyme, is known to be a multifunctional protein, acting as a metastasis suppressor, transactivation activity on c-myc, and regulating endocytosis. The cellular mechanisms regulating Nm23 functions are poorly understood. In this study, we identified the modifications and interacting proteins of Nm23-H1 in response to oxidative stress. We found that Cys109 in Nm23-H1 is oxidized to various oxidation states including intra- and inter-disulfide crosslinks, glutathionylation, and sulfonic acid formation in response to H2O2 treatment both in vivo and in vitro. The cross-linking sites and modifications of oxidized Nm23-H1 were identified by peptide sequencing using UPLC-ESIq-TOF tandem MS. Glutathionylation and oxidation of Cys109 inhibited the NDPK enzymatic activity of Nm23-H1. We also found that thioredoxin reductase 1 (TrxR1) is an interacting protein of Nm23-H1, and it binds specifically to oxidized Nm23-H1. Oxidized Nm23 is a substrate of NADPH-TrxR1-thioredoxin shuttle system, and the disulfide crosslinking is reversibly reduced and the enzymatic activity is recovered by this system. Oxidation of Cys109 in Nm23-H1 inhibited its metastatic suppressor activity as well as the enzymatic activities. The mutant, Nm23-H1 C109A, retained both the enzymatic and metastasis suppressor activities under oxidative stress. This suggests that key enzymatic and metastasis suppressor functions of Nm23-H1 are regulated by oxido-reduction of its Cys109. © 2009 Lee et al. | * |
dc.language | English | * |
dc.title | Multiple functions of Nm23-H1 are regulated by oxido-reduction system | * |
dc.type | Article | * |
dc.relation.issue | 11 | * |
dc.relation.volume | 4 | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.journaltitle | PLoS ONE | * |
dc.identifier.doi | 10.1371/journal.pone.0007949 | * |
dc.identifier.wosid | WOS:000272827300008 | * |
dc.identifier.scopusid | 2-s2.0-71049133596 | * |
dc.author.google | Lee E. | * |
dc.author.google | Jeong J. | * |
dc.author.google | Kim S.E. | * |
dc.author.google | Song E.J. | * |
dc.author.google | Kang S.W. | * |
dc.author.google | Lee K.-J. | * |
dc.contributor.scopusid | 이공주(7501497635;57191532162) | * |
dc.contributor.scopusid | 강상원(55731433900) | * |
dc.date.modifydate | 20240118155300 | * |