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Originally published In Press as doi:10.1074/jbc.M107922200 on January 25, 2002

J. Biol. Chem., Vol. 277, Issue 16, 13488-13493, April 19, 2002
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Vasoactive Intestinal Peptide Receptor-1 (VPAC-1) Is a Novel Gene Target of the Hemolymphopoietic Transcription Factor Ikaros*

Glenn DorsamDagger and Edward J. Goetzl

From the Departments of Medicine and Microbiology-Immunology, University of California Medical Center, San Francisco, California 94143-0711

Vasoactive intestinal peptide and its G-protein-coupled receptors, VPAC-1 and VPAC-2, are highly expressed in the immune system and modulate diverse T cell functions. The human VPAC-1 5'-flanking region (1.4 kb) contains four high affinity Ikaros (IK) consensus sequences. Ikaros native protein from T cell nuclear extracts and IK-1 and IK-2 recombinant proteins recognized an IK high affinity binding motif in the VPAC-1 promoter in electrophoretic mobility shift assays by a sequence-specific mechanism, and anti-IK antibodies supershifted this complex. Stable NIH-3T3 clones overexpressing IK-1 or IK-2 isoforms were generated to investigate Ikaros regulation of endogenous VPAC-1 expression as assessed by quantifying VPAC-1 mRNA and protein. By traditional and fluorometric-based kinetic reverse transcription-PCR and 125I-labeled vasoactive intestinal peptide binding, both IK-1 and IK-2 suppressed endogenous VPAC-1 expression in NIH-3T3 clones by a range of 50-93%. When a series of nested deletions of the VPAC-1 luciferase reporter construct were transiently transfected into IK-2 clones there was up to a 41% decrease in transcriptional activity compared with vector control. Two major IK-2 binding domains also were identified at -1076 to -623 bp and at -222 to -35 bp, respectively. As both Ikaros and its novel target VPAC-1 are highly expressed in T cells, this system may be a dominant determinant of the VPAC-1 expression in immune responses.

* This work was funded by National Institutes of Health Grant AI 29912 and National Research Service Award F32DK10107-01.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.

Dagger To whom correspondence should be addressed: University of California, UB8B, Box 0711, 533 Parnassus Ave. at 4th, San Francisco, CA 94143-0711. Tel.: 415-476-1531; Fax: 415-471-6915; E-mail: Glenn-Dorsam@excite.com.

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


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