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J Biol Chem, Vol. 274, Issue 46, 32725-32732, November 12, 1999
From the Departments of Physiology and Biochemistry, Michigan State
University, East Lansing, Michigan 48824
Polyunsaturated fatty acids (PUFA) suppress
hepatic lipogenic gene transcription through a peroxisome proliferator
activated receptor 
(PPAR)- and cyclooxygenase-independent
mechanism. Recently, the sterol response element-binding protein 1 (SREBP1) was implicated in the nutrient control of lipogenic gene
expression. In this report, we have assessed the role SREBP1 plays in
the PUFA control of three hepatic genes, fatty acid synthase,
L-pyruvate kinase (LPK), and the S14 protein (S14). PUFA suppressed
both the hepatic mRNASREBP1 through a
PPAR-independent mechanism as well as SREBP1c nuclear content
(nSREBP1c, 65 kDa). Co-transfection of primary hepatocytes revealed a
differential sensitivity of the fatty acid synthase, S14, and LPK
promoters to nSREBP1c overexpression. Of the three promoters examined,
LPK was the least sensitive to overexpressed nSREBP1c. Promoter
deletion and gel shift analyses of the S14 promoter localized a
functional SREBP1c cis-regulatory element to an E-box-like sequence
(
139TCGCCTGAT131) within the S14 PUFA
response region. Although overexpression of nSREBP1c significantly
reduced PUFA inhibition of S14CAT, overexpression of other factors that
induced S14CAT activity, such as steroid receptor co-activator 1 or
retinoid X receptor , had no effect on S14CAT PUFA sensitivity.
These results suggest that PUFA regulates hepatic nSREBP1c, a factor
that functionally interacts with the S14 PUFA response region.
PUFA regulation of nSREBP1c may account for the PUFA-mediated
suppression of hepatic S14 gene transcription.
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