© 1998 American Heart Association, Inc.
Original Contributions |
IL-1ß–Induced Monocyte Chemoattractant Protein-1 Gene Expression in Endothelial Cells Is Blocked by Proteasome Inhibitors
From the Department of Biology, Tanabe Research Laboratories (T.M., K.A.F., R.R.C.), San Diego; and the Department of Immunology, The Scripps Research Institute (G.C.N.P.), La Jolla, Calif.
Correspondence to Dr Ronald R. Cobb, Department of Biology, Tanabe Research Laboratories, 4540 Towne Centre Ct, San Diego, CA 92121. E-mail rcobb{at}trlusa.com
Abstract—Human monocyte
chemoattractant protein-1 (MCP-1) is expressed by a variety of cell
types in response to various stimuli. MCP-1 expressed by the
endothelium plays an important role in cell migration
and activation. MCP-1 is a major chemoattractant for monocytes, T
lymphocytes, and basophils. In the present study, we present
evidence that the proteasome complex is involved in mediating the
interleukin (IL)-1ß induction of MCP-1 in endothelial
cells. We present evidence that a proteasome inhibitor,
N-acetyl-leucinyl-leucinyl-norleucinal (norLeu), and the
protease inhibitor
tosyl-Phe-chloromethylketone (TPCK) block IL-1ß
induction of MCP-1 protein expression. norLeu and TPCK also blocked
IL-1ß–induced MCP-1 promoter-driven reporter gene expression as well
as nuclear factor (NF)-
B–mediated reporter gene expression. The
effects of norLeu were due to its inhibition of the proteasome rather
than calpain, because other calpain inhibitors had no
effect on MCP-1 expression. In contrast to TPCK, which blocked NF-B
translocation to the nucleus, norLeu had no effect on NF-B nuclear
translocation or IL-1ß–induced phosphorylation of
p65. This study demonstrates that the proteasome pathway is involved in
IL-1ß–induced MCP-1 gene expression in human endothelial cells.
Key Words: monocyte chemoattractant protein-1 • endothelial cells • proteasome inhibitors
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