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Effects of matrix metalloproteinase‐7 (MMP‐7) on myocardial fibroblast proliferation and migration following myocardial infarction
Author(s) -
Lindsey Merry L.,
Matrisian Lynn M.,
Escobar G. Patricia
Publication year - 2006
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.20.5.a1464
Subject(s) - myocardial infarction , fibroblast , matrix metalloproteinase , cell migration , cell growth , medicine , ligation , chemistry , endocrinology , cardiology , cell , in vitro , biochemistry
MMP‐7 cleaves a broad range of matrix and non‐matrix substrates to potentially regulate a variety of cellular functions. We have previously demonstrated that MMP‐7 levels increase following myocardial infarction and that wild type myocardial fibroblasts from the infarcted region display increased proliferation and decreased migration compared to fibroblasts from unoperated controls. To determine what role MMP‐7 plays on fibroblast function, fibroblasts were isolated from the infarcted region of MMP‐7 null mice at 7 days following coronary artery ligation and used through passage 4 (n=8). Compared to wild type myocardial infarction control fibroblasts, proliferation decreased 62±4% (n=8; p<0.001); migration increased 209±27% (n=4; p=0.03); and adhesion to gelatin (a known MMP‐7 substrate) decreased 47±8% (n=4; p=0.01). These data suggest that gelatin cleavage by MMP‐7 may differentially regulate cell proliferation and migration to alter the post‐myocardial infarction fibroblast phenotype. Because MMP‐7 is induced in the setting of myocardial infarction, it is likely that MMP‐7 modulation of fibroblast function contributes to scar formation. This study was supported by NIH HL‐75360.