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J Biol Chem, Vol. 274, Issue 7, 4300-4308, February 12, 1999
From the Department of Veterinary Pathobiology, University of
Missouri, Columbia, Missouri 65211
The serum amyloid A (SAA) protein has been
implicated in the progression and pathogenesis of rheumatoid arthritis
through induction of collagenase activity in synovial fibroblast cells that line the joint tissues. We demonstrate that SAA is synergistically induced in synovial cells by interleukin (IL)-1 and IL-6 that are
present at significantly high level in the synovial fluid of arthritis
patients. These cytokines induced phenotypic changes in synovial cells,
promoting protrusion and increased cellular contact. Induction of SAA
under this condition is mediated by promoter elements located between
Activation of Sp1 and Its Functional Co-operation with Serum
Amyloid A-activating Sequence Binding Factor in Synoviocyte Cells
Trigger Synergistic Action of Interleukin-1 and Interleukin-6 in Serum
Amyloid A Gene Expression
254 and 226, which contains binding sites for transcription factors
Sp1 and SAA activating sequence binding factor (SAF). Mutation of these
sequences abolishes SAA promoter response to IL-1 and IL-6. The role of
Sp1 in SAA induction was demonstrated by increased DNA binding
activity, phosphorylation, and increased protein content of Sp1 during
cytokine treatment. Sp1 interacts with the SAA promoter in association with SAF as an SAF·Sp1 heteromeric complex. Furthermore, using a
phosphatase inhibitor, we demonstrated increased transactivation potential of both Sp1 and SAF as a consequence of a phosphorylation event. These results provide first evidence for cytokine-mediated activation of Sp1 in synovial fibroblast cells and its participation in
regulating SAA expression by acting in conjunction with SAF.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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