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J Biol Chem, Vol. 274, Issue 12, 7946-7951, March 19, 1999
and C/EBP
From the Department of Biochemistry, Boston University School of
Medicine, Boston, Massachusetts 02118
Adipocyte differentiation is regulated by at
least two major transcription factors, CCAAT/enhancer-binding protein
(C/EBP) and peroxisome proliferator-activated receptor 
(PPAR). Expression of PPAR in fibroblasts converts them to
fat-laden cells with an adipocyte-like morphology. Here, we investigate
the ability of PPAR to confer insulin-sensitive glucose transport to
a variety of murine fibroblast cell lines. When cultured in the
presence of a PPAR ligand, Swiss-3T3 and BALB/c-3T3 cells
ectopically expressing PPAR accumulate lipid droplets, express
C/EBP, aP2, insulin-responsive aminopeptidase, and glucose
transporter isoform 4 (GLUT4), and exhibit highly insulin-responsive
2-deoxyglucose uptake. In contrast, PPAR-expressing NIH-3T3 cells,
despite similar lipid accumulation, adipocyte morphology, and aP2
expression, do not express C/EBP or GLUT4 and fail to acquire
insulin sensitivity. In cells ectopically expressing PPAR, the
development of insulin-responsive glucose uptake correlates with
C/EBP expression. Furthermore, ectopic expression of C/EBP in
NIH-3T3 cells converts them to the adipocyte phenotype and restores
insulin-sensitive glucose uptake. We propose that the pathway(s)
leading to fat accumulation and morphological changes are distinct from
that leading to insulin-dependent glucose transport. Our
results suggest that although PPAR is sufficient to trigger the
adipogenic program, C/EBP is required for establishment of
insulin-sensitive glucose transport.
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L. Wang, J. Shao, P. Muhlenkamp, S. Liu, P. Klepcyk, J. Ren, and J. E. Friedman Increased Insulin Receptor Substrate-1 and Enhanced Skeletal Muscle Insulin Sensitivity in Mice Lacking CCAAT/Enhancer-binding Protein beta J. Biol. Chem., May 5, 2000; 275(19): 14173 - 14181. [Abstract] [Full Text] [PDF]
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