Butyrate regulates leptin expression through different signaling pathways in adipocytes.
10.4142/jvs.2011.12.4.319
- Author:
Mohamed Mohamed SOLIMAN
1
;
Mohamed Mohamed AHMED
;
Alaa Eldin SALAH-ELDIN
;
Abeer Abdel Alim ABDEL-AAL
Author Information
1. Department of Biochemistry, Faculty of Veterinary Medicine, Benha Universities, P.O 13736, Egypt. mohamedsoliman8896@yahoo.com
- Publication Type:Original Article
- Keywords:
adipocytes;
butyrate;
leptin expression;
MAPK;
PI3K;
signaling pathway
- MeSH:
Adipocytes/*metabolism;
Azo Compounds;
Butyric Acid/*pharmacology;
CREB-Binding Protein/genetics/metabolism;
Cell Differentiation;
Cells, Cultured;
Gene Expression Regulation/*drug effects/physiology;
Humans;
Leptin/genetics/*metabolism;
Mitogen-Activated Protein Kinase Kinases/genetics/metabolism;
Phosphatidylinositol 3-Kinases/genetics/metabolism;
RNA, Messenger/genetics/metabolism;
Signal Transduction/*physiology;
Staining and Labeling
- From:Journal of Veterinary Science
2011;12(4):319-323
- CountryRepublic of Korea
- Language:English
-
Abstract:
Leptin is an adipocytokine that regulates body weight, and maintains energy homeostasis by promoting reduced food intake and increasing energy expenditure. Leptin expression and secretion is regulated by various factors including hormones and fatty acids. Butyrate is a short-chain fatty acid that acts as source of energy in humans. We determined whether this fatty acid can play a role in leptin expression in fully differentiated human adipocytes. Mature differentiated adipocytes were incubated with or without increasing concentrations of butyrate. RNA was extracted and leptin mRNA expression was examined by Northern blot analysis. Moreover, the cells were incubated with regulators that may affect signals which may alter leptin expression and analyzed with Northern blotting. Butyrate stimulated leptin expression, and stimulated mitogen activated protein kinase (MAPK) and phospho-CREB signaling in a time-dependent manner. Prior treatment of the cells with signal transduction inhibitors as pertusis toxin, Gi protein antagonist, PD98059 (a MAPK inhibitor), and wortmannin (a PI3K inhibitor) abolished leptin mRNA expression. These results suggest that butyrate can regulate leptin expression in humans at the transcriptional level. This is accomplished by: 1) Gi protein-coupled receptors specific for short-chain fatty acids, and 2) MAPK and phosphatidylinositol-3-kinase (PI3K) signaling pathways.
