The dipeptide H-Trp-Glu-OH (WE) shows agonistic activity to peroxisome proliferator-activated protein-alpha and reduces hepatic lipid accumulation in lipid-loaded H4IIE cells
- Authors
- Jia, Yaoyao; Kim, Jong-Ho; Nam, Bora; Kim, Jiyoung; Lee, Ji Hae; Hwang, Kwang-Yeon; Lee, Sung-Joon
- Issue Date
- 1-7월-2014
- Publisher
- PERGAMON-ELSEVIER SCIENCE LTD
- Keywords
- Dipeptide; H-Trp-Glu-OH (WE); PPAR alpha; Liver; Lipid metabolism
- Citation
- BIOORGANIC & MEDICINAL CHEMISTRY LETTERS, v.24, no.13, pp.2957 - 2962
- Indexed
- SCIE
SCOPUS
- Journal Title
- BIOORGANIC & MEDICINAL CHEMISTRY LETTERS
- Volume
- 24
- Number
- 13
- Start Page
- 2957
- End Page
- 2962
- URI
- https://scholar.korea.ac.kr/handle/2021.sw.korea/97984
- DOI
- 10.1016/j.bmcl.2014.04.019
- ISSN
- 0960-894X
- Abstract
- Dipeptides digested from dietary proteins can be directly absorbed by the intestine and delivered to the circulatory system. However, the dipeptides' metabolic roles and biological activities are largely unknown. Lipid-loaded HII4E cells stimulated with H-Trp-Glu-OH (WE) exhibited reduced lipid accumulation, of which the effect was abolished by peroxisome proliferator-activated receptor (PPAR) alpha gene knock down. A luciferase assay showed that the WE dipeptide induced PPAR alpha transactivation in a dose-dependent manner. Surface plasmon resonance and time-resolved fluorescence resonance energy transfer analyses demonstrated that WE interacts directly with the PPAR alpha ligand binding domain (K-D, 120 mu M; EC50, 83 mu M). Cells stimulated with WE induced PPAR alpha and its responsive genes and increased cellular fatty acid uptake. In conclusion, WE reduces hepatic lipid accumulation in lipid-loaded hepatocytes via the activation of PPAR alpha by a direct interaction. (C) 2014 Elsevier Ltd. All rights reserved.
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