Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 김화정 | * |
dc.date.accessioned | 2016-08-28T10:08:23Z | - |
dc.date.available | 2016-08-28T10:08:23Z | - |
dc.date.issued | 2013 | * |
dc.identifier.issn | 1535-3893 | * |
dc.identifier.other | OAK-10362 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/223962 | - |
dc.description.abstract | Tissue inhibitor of metalloproteinases-1 (TIMP-1) inhibits matrix metalloproteinases (MMPs) by binding at a 1:1 stoichiometry. Here we have shown the involvement of N-glycosylation in the MMP inhibitory ability of TIMP-1. TIMP-1, purified from HEK 293 cells overexpressing TIMP-1 (293 TIMP-1), showed less binding and inhibitory abilities to MMPs than TIMP-1 purified from fibroblasts or SF9 insect cells infected with TIMP-1 baculovirus. Following deglycosylation of TIMP-1, all forms of TIMP-1 showed similar levels of MMP binding and inhibition, suggesting that glycosylation is involved in the regulation of these TIMP-1 activities. Analysis of the N-glycan structures showed that SF9 TIMP-1 has the simplest N-glycan structures, followed by fibroblast TIMP-1 and 293 TIMP-1, in order of increasing complexity in their N-glycan structures. Further analyses showed that cleavage of outer arm fucose residues from the N-glycans of 293 TIMP-1 or knockdown of both FUT4 and FUT7 (which encode for fucosyltransferases that add outer arm fucose residues to N-glycans) enhanced the MMP-binding and catalytic abilities of 293 TIMP-1, bringing them up to the levels of the other TIMP-1. These results demonstrate that the ability of TIMP-1 to inhibit MMPs is at least in part regulated by outer arm fucosylation of its N-glycans. © 2013 American Chemical Society. | * |
dc.language | English | * |
dc.title | The presence of outer arm fucose residues on the N -glycans of tissue inhibitor of metalloproteinases-1 reduces its activity | * |
dc.type | Article | * |
dc.relation.issue | 8 | * |
dc.relation.volume | 12 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 3547 | * |
dc.relation.lastpage | 3560 | * |
dc.relation.journaltitle | Journal of Proteome Research | * |
dc.identifier.doi | 10.1021/pr400276r | * |
dc.identifier.wosid | WOS:000322852800001 | * |
dc.identifier.scopusid | 2-s2.0-84881133528 | * |
dc.author.google | Kim H.I. | * |
dc.author.google | Saldova R. | * |
dc.author.google | Park J.H. | * |
dc.author.google | Lee Y.H. | * |
dc.author.google | Harvey D.J. | * |
dc.author.google | Wormald M.R. | * |
dc.author.google | Wynne K. | * |
dc.author.google | Elia G. | * |
dc.author.google | Kim H.-J. | * |
dc.author.google | Rudd P.M. | * |
dc.author.google | Lee S.-T. | * |
dc.contributor.scopusid | 김화정(56670336100) | * |
dc.date.modifydate | 20240118124308 | * |