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A more recent version of this article appeared on September 10, 2004
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Papers In Press, published online ahead of print July 7, 2004
J. Biol. Chem, 10.1074/jbc.M403738200
Submitted on April 5, 2004
Revised on July 6, 2004
Accepted on July 7, 2004

Class II MHC transactivator (CIITA) inhibits matrix metalloproteinase-9 gene expression

Susan Nozell, Zhendong Ma, Cynthia Wilson, Reesha Shah, and Etty N. Benveniste

Department of Cell Biology, University of Alabama at Birmingham, Birmingham, AL 35294-0005

Corresponding Author: tika{at}uab.edu

Matrix metalloproteinases (MMPs) are a family of structurally related proteins with the collective capability to degrade all components of the extracellular matrix (ECM). Although MMP-mediated degradation of the ECM occurs physiologically, numerous pathological conditions exhibit increased MMP levels and excessive matrix degradation. Previous work from our laboratory has shown that interferon-gamma (IFN-gamma ) inhibits MMP-9 expression in a manner dependent upon Signal Transducer and Activator of Transcription-1alpha (STAT-1alpha ). Herein, we extend our previous observations and show that the class II MHC transactivator (CIITA), a transcriptional target of STAT-1alpha , is also capable of inhibiting MMP-9 expression. Using stable cell lines that inducibly express CIITA or various mutant forms of CIITA, we show that CIITA requires the ability to bind the CREB-binding protein (CBP) to effectively inhibit MMP-9 expression. Furthermore, we show that CIITA-mediated inhibition of the MMP-9 gene does not rely on CIITA’s transcriptional capability. These findings support a model wherein CIITA inhibits MMP-9 expression by binding to and sequestering CBP, which reduces the levels of CBP at the MMP-9 promoter, inhibits levels of acetylated histone 3 at the MMP-9 promoter, and subsequently inhibits MMP-9 expression.


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