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Ceruloplasmin binds and inactivates matrix metalloproteinase‐2
Author(s) -
Thompson Michael W.
Publication year - 2012
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.26.1_supplement.557.3
Subject(s) - ceruloplasmin , matrix metalloproteinase , lactoferrin , chemistry , immunoprecipitation , metalloproteinase , in vivo , metalloprotein , protease , biochemistry , transferrin , enzyme , biology , gene , microbiology and biotechnology
An interaction between the iron‐binding protein lactoferrin and matrix metalloproteinase‐2 (MMP‐2) suggests that MMP‐2 may interact with other metal binding proteins. To examine this possibility, the copper binding protein ceruloplasmin was examined to determine its effect on MMP‐2 and pro‐MMP‐2. Apoceruloplasmin, and to a lesser extent, holoceruloplasmin, physically interacted with pro‐MMP‐2 in an immunoprecipitation assay. Furthermore, apoceruloplasmin inhibited the protease activity of active MMP‐2, suggesting that ceruloplasmin may regulate the activity of MMP‐2 in vivo .