4.6 Article

Inhibitory Effect of Acer truncatum Bunge Seed Coat Extract on Fatty Acid Synthase, Differentiation and Lipid Accumulation in 3T3-L1 Adipocytes

期刊

MOLECULES
卷 27, 期 4, 页码 -

出版社

MDPI
DOI: 10.3390/molecules27041324

关键词

fatty acid synthase; Acer truncatum Bunge; inhibitor; obesity

资金

  1. Biological Resources Program, Chinese Academy of Sciences [KFJ-BRP-007]
  2. Fundamental Research Funds for Central Universities [Y95401AXX2]
  3. Youth Innovation Promotion Association, CAS [2012315]
  4. Zhongke Ruilaiyin (Beijing) Biotechnology Co., Ltd [2021C037]

向作者/读者索取更多资源

Acer truncatum seed coat (ESA) has been found to inhibit fatty acid synthase (FAS) activity, with quinic acid, malic acid, gentisic acid, procyanidin dimer, procyanidin trimer, catechin, and quercetin identified as the main compounds. This study provides new insights for the development of obesity treatments and the industrial production of vegetable oil.
Acer truncatum Bunge is now widely cultivated throughout the world. Fatty acid synthase (FAS) is a potential target in the treatment of both obesity and cancer. Only a few FAS inhibitors have been reported. In this study, the inhibitory effect of A. truncatum seed coat (ESA) on FAS and the inhibition mechanisms were investigated using a FAS activity assay and an enzyme kinetics study. The main chemicals of ESA were analyzed with UPLC-MS/MS. The effects of ESA on 3T3-L1 adipocyte differentiation and lipid accumulation were investigated using Oil red O staining. We first identified seven main compounds (quinic acid, malic acid, gentisic acid, procyanidin dimer, procyanidin trimer, catechin, and quercetin) from 50% ethanol extracts of seed coats of A. truncatum (ESAs), which were then found to inhibit 3T3-L1 adipocyte differentiation at the concentration of 50 mu g/mL. ESA obviously reduced the visible triglyceride droplets accumulation, and dramatically decreased the number of the adipocytes at a comparatively high concentration. It is suggested that the effects are due to the inhibition of FAS by ESA; FAS activity is inhibited by ESA at a half inhibition concentration (IC50) of 0.57 mu g/mL, which is lower than that of classically known FAS inhibitors. Meanwhile, ESA displayed different inhibition kinetics and reacting sites for FAS. These results provide new clues for the development of novel products for obesity treatment and a scientific basis for the full use of byproducts for future industrial production of vegetable oil.

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