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- 저자 : Wormald, Mark R. (검색결과 1 건)
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Kim, Han Ie,Saldova, Radka,Park, Jun Hyoung,Lee, Young Hun,Harvey, David J.,Wormald, Mark R.,Wynne, Kieran,Elia, Giuliano,Kim, Hwa-Jung,Rudd, Pauline M.,Lee, Seung-Taek American Chemical Society 2013 JOURNAL OF PROTEOME RESEARCH Vol.12 No.8
<P>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 <I>N</I>-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 <I>N</I>-glycan structures showed that SF9 TIMP-1 has the simplest <I>N</I>-glycan structures, followed by fibroblast TIMP-1 and 293 TIMP-1, in order of increasing complexity in their <I>N</I>-glycan structures. Further analyses showed that cleavage of outer arm fucose residues from the <I>N</I>-glycans of 293 TIMP-1 or knockdown of both FUT4 and FUT7 (which encode for fucosyltransferases that add outer arm fucose residues to <I>N</I>-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 <I>N</I>-glycans.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2013/jprobs.2013.12.issue-8/pr400276r/production/images/medium/pr-2013-00276r_0011.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/pr400276r'>ACS Electronic Supporting Info</A></P>
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