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Papers In Press, published online ahead of print January 25, 2002
Medicine, Immunology and Allergy, University of California, San Francisco, CA 94143-0711
Corresponding Author: mesangial{at}aol.com
Vasoactive intestinal peptide (VIP) 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 (1.4kb) contains 4 high-affinity Ikaros 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 of 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 RT-PCR and 125I-VIP 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 to vector control. Two major IK-2 binding domains also were identified at -1076 to –623bp and at –222 to –35bp, 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. (Funded by NIH grant AI 29912 and a National Research Service Award F32DK10107-01).
J. Biol. Chem, 10.1074/jbc.M107922200
Submitted on August 17, 2001
Revised on January 7, 2002
Accepted on January 25, 2002
Vasoactive intestinal peptide receptor - 1 (VPAC-1) is a novel gene target of the Hemolymphopoietic transcription factor ikaros
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