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Department of Surgery, Georgetown University Hospital, Washington, D.C. 20007
In a system of endotoxin (LPS)-mediated NO production in ANA-1
murine macrophages, suppression subtractive hybridization was used to
identify genes up-regulated by NO. Osteopontin (OPN), a secreted acidic
phosphoprotein that binds to a cell surface RGD integrin-binding motif,
was found to be differentially expressed in the presence of NO. OPN has
been demonstrated to inhibit NO production in a variety of cell types.
Northern blot and nuclear run-on analyses demonstrated that OPN mRNA
levels and gene transcription were significantly increased in the
presence of LPS-induced NO synthesis. Transient transfection of an OPN
promoter-luciferase reporter plasmid construct showed that promoter
activity is increased in the presence of LPS and NO. Immunoblot
analysis showed that OPN protein is secreted into the extracellular
fluid. Similar results were noted with an alternative cell system, RAW
264.7 macrophages, and alternative inducers of NO synthesis, IFN-
and IL-1
. In the presence of GRGDSP, a hexapeptide that blocks
binding of RGD-containing proteins to cell surface integrins, NO
production is significantly increased in the presence of LPS
stimulation. These data suggest a unique
trans-regulatory mechanism in which LPS-induced NO
synthesis feedback regulates itself through up-regulation of OPN
promoter activity and gene transcription.
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