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Originally published In Press as doi:10.1074/jbc.M200463200 on April 22, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36244-36252, September 27, 2002
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Ets-1 Positively Regulates Fas Ligand Transcription via Cooperative Interactions with Sp1*

Mary M. KavurmaDagger , Yuri Bobryshev§, and Levon M. KhachigianDagger

From the Dagger  Centre for Thrombosis and Vascular Research and § Surgical Professional Unit, St. Vincents Hospital, The University of New South Wales, Sydney 2052, Australia

The FasL/Fas system has been implicated in smooth muscle cell apoptosis and atherosclerotic plaque instability, a process that can lead to plaque rupture, precipitating myocardial infarction and sudden death. The transcriptional mechanisms regulating FasL gene expression in vascular smooth muscle cells are poorly understood. We recently described a novel mechanism mediating inducible FasL gene expression in smooth muscle cells involving the zinc finger transcription factor Sp1 (Kavurma, M. M., Santiago, F. S., Bofocco, E., and Khachigian, L. M. (2001) J. Biol. Chem. 276, 4964-4971). We now show that FasL gene expression is governed by cooperative activation between Sp1 and the Ets family of transcription factors. The overexpression of Ets-1 was sufficient to induce FasL promoter-dependent expression and protein synthesis. Ets-1 activation of the promoter was abrogated either by deletion or mutation of the Sp1 binding site. The overexpression of Ets-1 together with Sp1 produced cooperative activation of the FasL promoter. Sp1 induction of the FasL promoter was abrogated by an Ets-1 mutant lacking the activation domain. Conversely, Ets-1 activation of the promoter was blocked by an Sp1 mutant bearing the DNA-binding domain. The mutation of the -365GGAA-362 element in the FasL promoter abolished Ets-1 activation and attenuated Sp1-inducible gene expression. Immunoprecipitation and supershift experiments revealed that endogenous Ets-1 and Sp1 physically interact and co-occupy this site. Thus, FasL gene expression in vascular smooth muscle cells is mediated by cooperativity between Ets-1 and Sp1.

* This work was supported by grants from the New South Wales State Department of Health and by National Health and Medical Research Council of Australia (NHMRC).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Principal Research Fellow of the NHMRC. To whom correspondence should be addressed: Centre for Thrombosis and Vascular Research, Dept. of Pathology, The University of New South Wales, Sydney NSW 2052, Australia. Tel.: 61-2-9385-2537; Fax: 61-2-9385-1389; E-mail: L.Khachigian@unsw.edu.au.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.


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