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Volume 272, Number 46, Issue of November 14, 1997 pp. 28948-28953
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

Induction of Serum Amyloid A (SAA) Gene by SAA-activating Sequence-binding Factor (SAF) in Monocyte/Macrophage Cells
EVIDENCE FOR A FUNCTIONAL SYNERGY BETWEEN SAF AND Sp1

(Received for publication, June 27, 1997, and in revised form, July 30, 1997)

From the Department of Veterinary Pathobiology, University of Missouri, Columbia, Missouri 65211

Serum amyloid A (SAA) is a plasma protein that is associated with many inflammatory diseases including amyloidosis, arthritis, and atherosclerosis. SAA level is significantly increased during inflammatory condition, and such abnormal expression of this protein is linked to the pathogenesis of the above-mentioned diseases. A promoter element, designated as SAA-activating sequence (SAS), located between 280 and 226 has been implicated in the induction mechanism and a nuclear factor, SAS-binding factor (SAF), has been shown to bind to this region. In this report, using a cloned SAF gene in transient transfection assay, we provide evidence that SAF potentiates SAA gene expression through SAS element. Furthermore, we show that during lipopolysaccharide-mediated induction of SAF, heteromeric complex with transcription factor Sp1 is formed. Transfection assays using both transcription factor genes have demonstrated that SAF-Sp1 heteromer is a highly potent transactivator of SAA expression.

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