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dc.contributor.author오억수-
dc.contributor.author신동해-
dc.contributor.author장보희-
dc.date.accessioned2019-08-22T16:30:11Z-
dc.date.available2019-08-22T16:30:11Z-
dc.date.issued2019-
dc.identifier.issn2045-2322-
dc.identifier.otherOAK-25217-
dc.identifier.urihttps://dspace.ewha.ac.kr/handle/2015.oak/251242-
dc.description.abstractAlthough syndecan-2 is known to interact with the matrix metalloproteinase-7 (MMP-7), the details of their interaction were unknown. Our experiments with a series of syndecan-2 extracellular domain deletion mutants show that the interaction is mediated through an interaction of the extracellular domain of syndecan-2 (residues 41 to 60) with the α2 helix-loop-α3 helix in the pro-domain of MMP-7. NMR and molecular docking model show that Glu7 of the α1 helix, Glu32 of the α2 helix, and Gly48 and Ser52 of the α2 helix-loop-α3 helix of the MMP-7 pro-domain form the syndecan-2-binding pocket, which is occupied by the side chain of tyrosine residue 51 (Tyr51) of syndecan-2. Consistent with this notion, the expression of a syndecan-2 mutant in which Tyr51 was changed to Ala diminished the interaction between the syndecan-2 extracellular domain and the pro-domain of MMP-7. Furthermore, HT-29 colon adenocarcinoma cells expressing the interaction-defective mutant exhibited reductions in the cell-surface localization of MMP-7, the processing of pro-MMP-7 into active MMP-7, the MMP-7-mediated extracellular domain shedding of both syndecan-2 and E-cadherin, and syndecan-2-mediated anchorage-independent growth. Collectively, these data strongly suggest that Tyr51 of the syndecan-2 extracellular domain mediates its interaction with and activating processing of pro-MMP-7 and regulates MMP-7-dependent syndecan-2 functions. © 2019, The Author(s).-
dc.languageEnglish-
dc.publisherNature Publishing Group-
dc.titleTyrosine 51 residue of the syndecan-2 extracellular domain is involved in the interaction with and activation of pro-matrix metalloproteinase-7-
dc.typeArticle-
dc.relation.issue1-
dc.relation.volume9-
dc.relation.indexSCIE-
dc.relation.indexSCOPUS-
dc.relation.journaltitleScientific Reports-
dc.identifier.doi10.1038/s41598-019-47140-5-
dc.identifier.wosidWOS:000476718900012-
dc.identifier.scopusid2-s2.0-85069636963-
dc.author.googleJang B.-
dc.author.googleYun J.-H.-
dc.author.googleChoi S.-
dc.author.googlePark J.-
dc.author.googleShin D.H.-
dc.author.googleLee S.-T.-
dc.author.googleLee W.-
dc.author.googleOh E.-S.-
dc.contributor.scopusid오억수(7101967153)-
dc.contributor.scopusid신동해(57217374185)-
dc.contributor.scopusid장보희(55242403100)-
dc.date.modifydate20230208115524-


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