J Korean Diabetes Assoc.
2000 Aug;24(4):413-420.
Regulation of mFABP (fatty acid binding protein) Expression by PPAR in Cultured Human Skeletal Muscle Cell
- Affiliations
-
- 1Department of Internal Medicine, Seoul National University Medical Research Center, Seoul, Korea.
- 2The Institute of Endocrinology, Seoul National University Medical Research Center, Seoul, Korea.
- 3Nutrition and Metabolism research Center, Seoul National University Medical Research Center, Seoul, Korea.
Abstract
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BACKGROUND: Fatty acid binding protein (FABP), putative mammalian fatty acid
transporter, plays a role in fatty acid transport, the modulation of cellular signal
transduction pathways and the protection against detergent like effects of fatty
acids. FABP found in liver, adipose tissue, heart, skeletal muscle and FABP in
skeletal muscle accounts for 2% of total protein mass. FABP expression has shown
to be up-regulated by PPAR in liver and adipocyte. Adipocyte and liver FABP
genes have a functional PPRE (PPAR responsive element) in their promoter region.
This evidence led us to investigate for a possible the regulation of mFABP
expression by PPAR in cultured human skeletal muscle cell.
METHODS
Myoblast were cultured in SkGM for 4weeks and were differentiated into
myocyte in MEM for 4days. The myocytes were treated with PPAR ligand
(troglitazone: 5 g/mL) or transduction with adenovirus-PPAR 1 (Ad-PPAR 1). mFABP
expression was identified by northern blot.
RESULTS
mFABP expression was up-regulated by 4.0+/-1.2 fold in the PPAR ligand
(p<0.05). There was increased in mFABP expression with transduction with
adenovirus-PPAR 1 while there was no change in mFABP expression which
transducted with adenovirus - -galactosidase.
CONCLUSION
These results demonstrates that mFABP expression is up-regulated by
both PPAR ligand and by PPAR 1 over expression in cultured human skeletal
muscle cells.