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J Biol Chem, Vol. 274, Issue 30, 21305-21312, July 23, 1999
From the Second Department of Internal Medicine, Kobe University
School of Medicine, 7-5-1 Kusunoki-cho, Chuo-ku, Kobe 650-0017, Japan,
the § Molecular Cardiology Unit, Kyushu University School of
Medicine, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan, and
the ¶ Department of Molecular Physiology and Biophysics,
Vanderbilt University, Nashville, Tennessee 37332-0165
Transcriptional regulation of phosphoenolpyruvate
carboxykinase (PEPCK), the rate-limiting enzyme in hepatic
gluconeogenesis, by insulin was investigated with the use of adenovirus
vectors encoding various mutant signaling proteins. Insulin inhibited transcription induced by dexamethasone and cAMP of a chloramphenicol acetyltransferase (CAT) reporter gene fused with the PEPCK promoter sequence in HL1C cells stably transfected with this construct. A
dominant negative mutant of phosphoinositide (PI) 3-kinase blocked insulin inhibition of transcription of the PEPCK-CAT fusion gene, whereas a constitutively active mutant of PI 3-kinase mimicked the
effect of insulin. Although a constitutively active mutant of Akt
(protein kinase B) inhibited PEPCK-CAT gene transcription induced by
dexamethasone and cAMP, a mutant Akt (Akt-AA) in which the
phosphorylation sites targeted by insulin are replaced by alanine did
not affect the ability of insulin to inhibit transcription of the
fusion gene. Akt-AA almost completely inhibited insulin-induced activation of both endogenous and recombinant Akt in HL1C cells. Furthermore, neither a kinase-defective mutant protein kinase C
Dominant Negative Forms of Akt (Protein Kinase B) and Atypical
Protein Kinase C
Do Not Prevent Insulin Inhibition of
Phosphoenolpyruvate Carboxykinase Gene Transcription
(PKC), which blocked insulin-induced activation of endogenous PKC, nor a dominant negative mutant of the small GTPase Rac
prevented inhibition of PEPCK-CAT gene transcription by insulin. These
data suggest that phosphoinositide 3-kinase is important for
insulin-induced inhibition of PEPCK gene transcription and that a
downstream effector of phosphoinositide 3-kinase distinct from Akt,
PKC, and Rac may exist for mediating the effect of insulin.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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