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Originally published In Press as doi:10.1074/jbc.M000621200 on May 26, 2000

J. Biol. Chem., Vol. 275, Issue 41, 31747-31754, October 13, 2000
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Activation of Apolipoprotein AI Gene Expression by Protein Kinase A and Kinase C through Transcription Factor, Sp1*

Xi-Long ZhengDagger §, Shuji MatsubaraDagger §, Catherine DiaoDagger §, Morley D. HollenbergDagger ||, and Norman C. W. WongDagger §**

From the Endocrine Research Group, Departments of Dagger  Medicine and § Biochemistry & Molecular Biology and || Pharmacology & Therapeutics, the Faculty of Medicine, University of Calgary, Calgary, Alberta T2N 4N1, Canada

Our previous finding that insulin induces apolipoprotein AI (apoAI) transcription points to the participation of intracellular signaling. This finding prompted us to ask whether two classical G-protein-coupled signaling pathways requiring activated protein kinase A (PKA) or kinase C (PKC) may also regulate apoAI. Therefore, human hepatoma, Hep G2 cells stably transfected with pAI.474-CAT, a reporter construct spanning -474 to -7 of apoAI DNA fused to chloramphenicol acetyltransferase (CAT) were treated with 10 µM forskolin (FSK) or 50 nM phorbol dibutyrate (PDBu) to activate PKA and PKC, respectively. Results showed that the apoAI promoter activity increased 4-5-fold following 24 h of treatment with either FSK or PDBu. Induction by either agent was blocked with actinomycin D but not the protein synthesis inhibitor, cycloheximide. The PKA inhibitor, PKI 14-22 amide, abrogated induction by FSK, 100 µM 8-bromo-cAMP, or 100 ng/ml cholera toxin, but it had no effect on activation via PKC. Similarly, PDBu induction was attenuated by 2 µM of the PKC inhibitor, GF109203X, but it did not affect FSK activity. Next we used deletional constructs to show that the actions of FSK and PDBu required the insulin-responsive core element (IRCE). This motif matched the consensus binding site for the transcription factor, Sp1. The binding of Sp1 to the IRCE was confirmed by gel-retardation and supershift analysis. Site-directed mutagenesis of the IRCE eliminated Sp1 action and induction by FSK or PDBu. Whereas overexpression of Sp1 enhanced basal and FSK or PDBu induced promoter activity, transfection of an antisense oligomer against Sp1 mRNA attenuated both parameters. In summary, activation of PKA or PKC increases apoAI promoter activity. The activity of both signaling pathways is mediated by the IRCE, a motif that binds the transcription factor, Sp1.

* 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.

Recipient of a fellowship award from the Heart and Stroke Foundation of Canada.

** Recipient of scientist awards from the Medical Research Council and Alberta Heritage Foundation for Medical Research. To whom correspondence should be addressed: Depts. of Medicine and Biochemistry and Molecular Biology, Faculty of Medicine, University of Calgary, Health Sciences Center, 3330 Hospital Dr. NW, Calgary, Alberta T2N 4N1, Canada. Tel.: 403-220-5212; Fax: 403-270-0979; E-mail: ncwwong@acs.ucalgary.ca.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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