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dc.contributor.author김화정-
dc.date.accessioned2016-08-28T10:08:23Z-
dc.date.available2016-08-28T10:08:23Z-
dc.date.issued2013-
dc.identifier.issn1535-3893-
dc.identifier.otherOAK-10362-
dc.identifier.urihttps://dspace.ewha.ac.kr/handle/2015.oak/223962-
dc.description.abstractTissue 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.languageEnglish-
dc.titleThe presence of outer arm fucose residues on the N -glycans of tissue inhibitor of metalloproteinases-1 reduces its activity-
dc.typeArticle-
dc.relation.issue8-
dc.relation.volume12-
dc.relation.indexSCI-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.startpage3547-
dc.relation.lastpage3560-
dc.relation.journaltitleJournal of Proteome Research-
dc.identifier.doi10.1021/pr400276r-
dc.identifier.wosidWOS:000322852800001-
dc.identifier.scopusid2-s2.0-84881133528-
dc.author.googleKim H.I.-
dc.author.googleSaldova R.-
dc.author.googlePark J.H.-
dc.author.googleLee Y.H.-
dc.author.googleHarvey D.J.-
dc.author.googleWormald M.R.-
dc.author.googleWynne K.-
dc.author.googleElia G.-
dc.author.googleKim H.-J.-
dc.author.googleRudd P.M.-
dc.author.googleLee S.-T.-
dc.contributor.scopusid김화정(56670336100)-
dc.date.modifydate20211005101611-
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약학대학 > 약학과 > Journal papers
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