(Circulation. 1999;99:3103-3109.)
© 1999 American Heart Association, Inc.
Clinical Investigation and Reports |
Membrane Type 1 Matrix Metalloproteinase Expression in Human Atherosclerotic Plaques
Evidence for Activation by Proinflammatory Mediators
Presented at the 47th annual scientific sessions of the American College of Cardiology, Atlanta, Ga, March 29–April 1, 1998; and published in abstract form (J Am Coll Cardiol. 1998;31:419A).
From the Atherosclerosis Research Center, Burns and Allen Research Institute, Division of Cardiology and Department of Medicine, Cedars-Sinai Medical Center (T.B.R., X.-P.X., S.J., S.M., X.-O.X, N.-N.C., S.K., B.S., P.K.S.), Los Angeles, Calif, and the Departments of Pathology and Laboratory Medicine (M.C.F.), UCLA School of Medicine, Los Angeles, Calif.
Correspondence to Dr T.B. Rajavashisth or Dr P.K. Shah, Atherosclerosis Research Center, Division of Cardiology, Room 5347, Cedars-Sinai Medical Center, 8700 Beverly Blvd, Los Angeles, CA 90048. E-mail rajavashisth@cshs.org or shahp{at}cshs.org
Background—Matrix metalloproteinases (MMPs) are expressed in atherosclerotic plaques, where in their active form, they may contribute to vascular remodeling and plaque disruption. In this study, we tested the hypothesis that membrane type 1 MMP (MT1-MMP), a novel transmembrane MMP that activates pro-MMP-2 (gelatinase A), is expressed in human atherosclerotic plaques and that its expression is regulated by proinflammatory molecules.
Methods and Results—MT1-MMP expression was examined in normal and
atherosclerotic human arteries by immunocytochemistry with specific
antibodies. MT1-MMP expression in human saphenous vein–derived smooth
muscle cells (SMCs) maintained in tissue culture was determined under
basal conditions and in response to proinflammatory molecules
(interleukin [IL]-1
, tumor necrosis factor [TNF]-, and
oxidized LDL [ox-LDL]) by use of Northern blot and ribonuclease
protection assays for mRNA, Western blot and immunoprecipitation for
protein, and gelatin zymography for catalytic activity. Medial SMCs of
normal vessel wall expressed MT1-MMP. In atherosclerotic arteries,
MT1-MMP expression was noted within the complex atheroma
colocalizing with SMCs and macrophages (M
). Cultured SMCs
constitutively expressed MT1-MMP mRNA and protein, which increased 2-
to 4-fold over control in a time-dependent manner within 4 to 8 hours
of exposure to IL-1, TNF-, and ox-LDL (thiobarbituric
acid–reactive substances, 13.4 nmol/mg LDL protein), whereas native
LDL had no effect. Flow cytometry revealed MT1-MMP expression by human
monocyte-derived M, which increased 3.8-fold over baseline within 6
hours after exposure to 10 ng/mL TNF-.
Conclusions—This study demonstrates that MT1-MMP, an
activator of pro-MMP-2, is expressed by SMCs and M in
human atherosclerotic plaques. Furthermore, proinflammatory molecules
upregulate MT1-MMP expression in vascular SMCs and M. Thus,
activation of SMCs and M by proinflammatory molecules may influence
extracellular matrix remodeling in atherosclerosis by
regulating MT1-MMP expression.
Key Words: metalloproteinases • cells • proteins • lipoproteins
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